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Conserved domains on  [gi|1720435493|ref|XP_030107270|]
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CTP synthase 2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02327 super family cl33465
CTP synthase
 1-401 0e+00

CTP synthase


The actual alignment was detected with superfamily member PLN02327:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 590.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:PLN02327  157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:PLN02327  237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLS 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:PLN02327  316 VLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEE 320
Cdd:PLN02327  396 GICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDE 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 321 RHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQ 400
Cdd:PLN02327  476 RHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555


                  .
gi 1720435493 401 Q 401
Cdd:PLN02327  556 S 556
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-401 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 590.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:PLN02327  157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:PLN02327  237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLS 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:PLN02327  316 VLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEE 320
Cdd:PLN02327  396 GICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDE 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 321 RHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQ 400
Cdd:PLN02327  476 RHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555


                  .
gi 1720435493 401 Q 401
Cdd:PLN02327  556 S 556
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 3-391 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: 537.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   3 FVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNP 82
Cdd:COG0504   153 FLEAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPE 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  83 EQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVF 162
Cdd:COG0504   233 EAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL---EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVV 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 163 KALEHSALAINHKLNLMYIDSIDLEPvtkaedpvkfHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGI 242
Cdd:COG0504   310 EALKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGI 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 243 CLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVfTTENSILKKLYGDvPYIEE 320
Cdd:COG0504   380 CLGMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCK-LKPGTLAAEAYGK-EEISE 456

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435493 321 RHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 391
Cdd:COG0504   457 RHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-390 1.43e-180

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: 513.80  E-value: 1.43e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:TIGR00337 151 LPFLEAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDV 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:TIGR00337 231 EEEAVISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLS 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpVKFHEAwqklclADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:TIGR00337 308 VIEALKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFL 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNP-GDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIE 319
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCIL-KPGTLAFKLYGK-EEVY 454

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435493 320 ERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLA 390
Cdd:TIGR00337 455 ERHRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 143-388 1.52e-137

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: 393.46  E-value: 1.52e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 143 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpvkfheAWQKLCLADGILVPGGFGIRGT 222
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 223 LGKLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPE-HNPGDLGGTMRLGLRRTVF 301
Cdd:cd01746    71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 302 tTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPS 381
Cdd:cd01746   151 -KPGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                  ....*..
gi 1720435493 382 PPYLGLL 388
Cdd:cd01746   229 PLFVGFV 235
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-116 8.42e-68

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: 216.44  E-value: 8.42e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:pfam06418 150 LPFLEAIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNV 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGL 116
Cdd:pfam06418 230 PKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-401 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 590.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:PLN02327  157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:PLN02327  237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLS 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:PLN02327  316 VLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEE 320
Cdd:PLN02327  396 GICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDE 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 321 RHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQ 400
Cdd:PLN02327  476 RHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555


                  .
gi 1720435493 401 Q 401
Cdd:PLN02327  556 S 556
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 3-391 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: 537.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   3 FVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNP 82
Cdd:COG0504   153 FLEAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPE 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  83 EQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVF 162
Cdd:COG0504   233 EAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL---EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVV 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 163 KALEHSALAINHKLNLMYIDSIDLEPvtkaedpvkfHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGI 242
Cdd:COG0504   310 EALKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGI 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 243 CLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVfTTENSILKKLYGDvPYIEE 320
Cdd:COG0504   380 CLGMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCK-LKPGTLAAEAYGK-EEISE 456

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435493 321 RHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 391
Cdd:COG0504   457 RHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
pyrG PRK05380
CTP synthetase; Validated
 1-391 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 535.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:PRK05380  150 LPFLEAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNV 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:PRK05380  230 PEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGL---EAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKS 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTKAEdpvkfheawqKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:PRK05380  307 VIEALKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFL 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVFtTENSILKKLYGDvPYI 318
Cdd:PRK05380  377 GICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIYGK-EEI 453

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435493 319 EERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 391
Cdd:PRK05380  454 YERHRHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-390 1.43e-180

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: 513.80  E-value: 1.43e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:TIGR00337 151 LPFLEAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDV 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYAS 160
Cdd:TIGR00337 231 EEEAVISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLS 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 161 VFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpVKFHEAwqklclADGILVPGGFGIRGTLGKLQAISWARTKKIPFL 240
Cdd:TIGR00337 308 VIEALKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFL 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 241 GICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNP-GDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIE 319
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCIL-KPGTLAFKLYGK-EEVY 454

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435493 320 ERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLA 390
Cdd:TIGR00337 455 ERHRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 143-388 1.52e-137

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: 393.46  E-value: 1.52e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 143 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpvkfheAWQKLCLADGILVPGGFGIRGT 222
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 223 LGKLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPE-HNPGDLGGTMRLGLRRTVF 301
Cdd:cd01746    71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 302 tTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPS 381
Cdd:cd01746   151 -KPGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                  ....*..
gi 1720435493 382 PPYLGLL 388
Cdd:cd01746   229 PLFVGFV 235
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-116 8.42e-68

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: 216.44  E-value: 8.42e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:pfam06418 150 LPFLEAIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNV 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQERLGL 116
Cdd:pfam06418 230 PKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-112 4.01e-64

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: 206.95  E-value: 4.01e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493   1 MAFVEAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHV 80
Cdd:cd03113   150 LPFLEALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNV 229

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720435493  81 NPEQVICIHDVSSIYRVPLLLEEQGVVKYFQE 112
Cdd:cd03113   230 PPEAVISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase pfam00117
Glutamine amidotransferase class-I;
154-390 6.00e-45

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 154.32  E-value: 6.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 154 LRDCYASVFKALEHSALAINHKLNLMYIDSIDLEpvTKAEDPvkfheawqklclaDGILVPGGFGIRGTLG-KLQAISWA 232
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEE--ILEENP-------------DGIILSGGPGSPGAAGgAIEAIREA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 233 RTKKIPFLGICLGMQLAVIEFARNCLNLKDanstefepntpvplvidmpehnPGDLGGTMRLGLRRTvfttensilKKLY 312
Cdd:pfam00117  67 RELKIPILGICLGHQLLALAFGGKVVKAKK----------------------FGHHGKNSPVGDDGC---------GLFY 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720435493 313 GDVPYIEERHRHRYEVNPNlinqFENKDLCFVGEDVDG-KRMEIVELTSHpyFIGVQFHPEFSSRPMKPSPPYLGLLLA 390
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 145-391 2.80e-30

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 116.60  E-value: 2.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 145 IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLepvTKAEDPVKFHEAWqklcladgiLVPGGfGIRGTLG 224
Cdd:PRK06186    4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI---TDPEDLAGFDGIW---------CVPGS-PYRNDDG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 225 KLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTP----VPLVIDMPEHNpgdlgGTMRLglrrtv 300
Cdd:PRK06186   71 ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDrpviAPLSCSLVEKT-----GDIRL------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 301 ftTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGkrmEI--VELTSHPYFIGVQFHPEFSSRPM 378
Cdd:PRK06186  140 --RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALAG 213

                         250
                  ....*....|...
gi 1720435493 379 KPSPPYLGLLLAA 391
Cdd:PRK06186  214 RPPPLVRAFLRAA 226
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 145-251 1.69e-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: 57.99  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 145 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 223
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720435493 224 ---GKLQAISWARTKKIPFLGICLGMQLAVI 251
Cdd:cd01653    64 rdeALLALLREAAAAGKPILGICLGAQLLVL 94
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 174-373 5.98e-10

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 59.03  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 174 HKLNLMYIDSID-------LEPVTKAEDPVKfheawQKLCLADGILVPGG-------FG--IRGTLGK---------LQA 228
Cdd:COG2071    14 HYLPEDYVRAVRaagglpvLLPPVGDEEDLD-----ELLDRLDGLVLTGGadvdpalYGeePHPELGPidperdafeLAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 229 ISWARTKKIPFLGICLGMQLaviefarncLNlkdanstefepntpV----PLVIDMPEHNPGDLG---GTMRLGLRRTVF 301
Cdd:COG2071    89 IRAALERGKPVLGICRGMQL---------LN--------------ValggTLYQDLPDQVPGALDhrqPAPRYAPRHTVE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 302 TTENSILKKLYGdvpyieerhRHRYEVNpnlinqfenkdlCF-------VGEDV-------DGkrmeIVE---LTSHPYF 364
Cdd:COG2071   146 IEPGSRLARILG---------EEEIRVN------------SLhhqavkrLGPGLrvsarapDG----VIEaieSPGAPFV 200


                  ....*....
gi 1720435493 365 IGVQFHPEF 373
Cdd:COG2071   201 LGVQWHPEW 209
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 145-248 3.23e-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: 53.74  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 145 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 223
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                          90       100
                  ....*....|....*....|....*...
gi 1720435493 224 ---GKLQAISWARTKKIPFLGICLGMQL 248
Cdd:cd03128    64 wdeALLALLREAAAAGKPVLGICLGAQL 91
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 203-376 1.01e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 49.09  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 203 QKLCLADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLavieFAR-------NCLNLKDANSTEFE 269
Cdd:PRK13181   33 EEIAGADKVILPGvgafGQAMRSlrESGLDEALKEHVEKKQPVLGICLGMQL----LFEsseegnvKGLGLIPGDVKRFR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 270 PNT-PVPlvidmpehnpgdlggtmRLGLRRTVFTTENSILKKlygdvpyIEERHR----HRYEVNPNlinqfenkdlcfV 344
Cdd:PRK13181  109 SEPlKVP-----------------QMGWNSVKPLKESPLFKG-------IEEGSYfyfvHSYYVPCE------------D 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720435493 345 GEDVDGKRMEIVELTSHPY---FIGVQFHPEFSSR 376
Cdd:PRK13181  153 PEDVLATTEYGVPFCSAVAkdnIYAVQFHPEKSGK 187
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 236-372 4.19e-06

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 47.64  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 236 KIPFLGICLGMQLAVIEFARNcLNLkDANStefepntpVPLVIDMPEHNPGDLGGTmrlglRRTVFTTENSILKKLYGDv 315
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGT-LYQ-DIQE--------QPGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASLLGS- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435493 316 pyiEErhrhrYEVNpNLINQFENK---DLCFVGEDVDGKrMEIVELTSHPYF-IGVQFHPE 372
Cdd:pfam07722 169 ---EE-----FRVN-SLHHQAIDRlapGLRVEAVAPDGT-IEAIESPNAKGFaLGVQWHPE 219
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 208-248 2.26e-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: 45.03  E-value: 2.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720435493 208 ADGILVPG-G-FG-----IRGtLGKLQAISWARTKKIPFLGICLGMQL 248
Cdd:COG0118    39 ADRLVLPGvGaFGdamenLRE-RGLDEAIREAVAGGKPVLGICLGMQL 85
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 208-248 4.32e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 44.09  E-value: 4.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720435493 208 ADGILVPG--GFGIRGT-LGKL-QAISWARTKKIPFLGICLGMQL 248
Cdd:PRK13143   39 ADGIVLPGvgAFGAAMEnLSPLrDVILEAARSGKPFLGICLGMQL 83
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 208-376 1.32e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 42.87  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 208 ADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLAvieFAR-------NCLNLKDANSTEFEPNTPV 274
Cdd:cd01748    37 ADKLILPGvgafGDAMANlrERGLIEALKEAIASGKPFLGICLGMQLL---FESseegggtKGLGLIPGKVVRFPASEGL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 275 PLvidmPeHnpgdlggtMrlGLRRTVFTTENSILKklygdvpYIEERHR----HRYEVNPNlinqfENKDL---CFVGED 347
Cdd:cd01748   114 KV----P-H--------M--GWNQLEITKESPLFK-------GIPDGSYfyfvHSYYAPPD-----DPDYIlatTDYGGK 166

                         170       180
                  ....*....|....*....|....*....
gi 1720435493 348 VDGkrmeIVEltsHPYFIGVQFHPEFSSR 376
Cdd:cd01748   167 FPA----AVE---KDNIFGTQFHPEKSGK 188
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 203-372 1.90e-04

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 43.08  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 203 QKLCLADGILVPGGFGirgtlgKLQAISWARTKKI---------------PFLGICLGMQLAVIEFARNCLNLKDANSTE 267
Cdd:cd01747    50 KLFKSINGILFPGGAV------DIDTSGYARTAKIiynlalerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEATN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 268 fepntpvplvIDMPEHNPGDLggtmrlgLRRTVF-TTENSILKKLyGDVPYIEerHRHRYEVNPN------LINQFENkd 340
Cdd:cd01747   124 ----------SALPLNFTEDA-------LQSRLFkRFPPDLLKSL-ATEPLTM--NNHRYGISPEnftengLLSDFFN-- 181

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720435493 341 LCFVGEDVDGKR-MEIVELTSHPYFiGVQFHPE 372
Cdd:cd01747   182 VLTTNDDWNGVEfISTVEAYKYPIY-GVQWHPE 213
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 159-248 2.46e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 42.04  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 159 ASVFKALEhsalainhKLNLMYIdsidlepVTKaeDPvkfheawQKLCLADGILVPG--GFG-----IRGTlGKLQAISW 231
Cdd:PRK13141   13 RSVEKALE--------RLGAEAV-------ITS--DP-------EEILAADGVILPGvgAFPdamanLRER-GLDEVIKE 67

                          90
                  ....*....|....*..
gi 1720435493 232 ARTKKIPFLGICLGMQL 248
Cdd:PRK13141   68 AVASGKPLLGICLGMQL 84
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 208-248 6.01e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.92  E-value: 6.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720435493 208 ADGILVPG---------GFGIRGTLGKLQAISWARTKkiPFLGICLGMQL 248
Cdd:PRK13146   42 ADRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLGICVGMQL 89
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 226-373 3.37e-03

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 38.33  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435493 226 LQAISWARTKKIPFLGICLGMQLaviefarncLNlkDAnstefepntpvplvidmpehnpgdLGGTMRLGLRrtVftteN 305
Cdd:cd01745    90 LALLRAALERGKPILGICRGMQL---------LN--VA------------------------LGGTLYQDIR--V----N 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435493 306 SIlkklygdvpyieerhrHRYEVnpnlinqfenKDL--CFVGE--DVDGKrMEIVELTSHPYFIGVQFHPEF 373
Cdd:cd01745   129 SL----------------HHQAI----------KRLadGLRVEarAPDGV-IEAIESPDRPFVLGVQWHPEW 173
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 226-248 4.50e-03

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 38.39  E-value: 4.50e-03
                          10        20
                  ....*....|....*....|...
gi 1720435493 226 LQAISWARTKKIPFLGICLGMQL 248
Cdd:COG0518    72 PALIREAFELGKPVLGICYGAQL 94
 
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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