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Conserved domains on  [gi|9055198|ref|NP_061207|]
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CTP synthase 2 isoform a [Mus musculus]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 929.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVDGNKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   321 LEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9055198   481 RYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 929.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVDGNKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   321 LEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9055198   481 RYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-547 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 842.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL---EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  321 LEHSALAINHKLNLMYIDSIDLEPvtkaedpvkfHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVfTTENSILKKLYGDvPYIEERH 478
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCK-LKPGTLAAEAYGK-EEISERH 458

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055198  479 RHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:COG0504 459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 801.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198      1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK------ISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    321 LEHSALAINHKLNLMYIDSIDLEPVTkaedpVKFHEAwqklclADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNP-GDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCIL-KPGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9055198    480 HRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 556.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198      2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFVE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 9055198    242 ICIHDVSSIYRVPLLLEEQGVVKYFQERLGL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 530.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:cd03113   1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVdgnkedPQICVIELGGTIGDIEGMAFVE 161
Cdd:cd03113  81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPE------PDVCIVEIGGTVGDIESLPFLE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                       250       260
                ....*....|....*....|....*..
gi 9055198  242 ICIHDVSSIYRVPLLLEEQGVVKYFQE 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 929.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVDGNKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   321 LEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9055198   481 RYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-547 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 842.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL---EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  321 LEHSALAINHKLNLMYIDSIDLEPvtkaedpvkfHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVfTTENSILKKLYGDvPYIEERH 478
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCK-LKPGTLAAEAYGK-EEISERH 458

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055198  479 RHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:COG0504 459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
pyrG PRK05380
CTP synthetase; Validated
 1-547 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 839.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAkvsvdgnkEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGL---EAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEA 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   321 LEHSALAINHKLNLMYIDSIDLEPVTKAEdpvkfheawqKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PRK05380 311 LKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICL 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIEERH 478
Cdd:PRK05380 381 GMQLAVIEFARNVLGLEDANSTEFDPDTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIYGK-EEIYERH 457

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055198   479 RHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:PRK05380 458 RHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 801.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198      1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK------ISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    321 LEHSALAINHKLNLMYIDSIDLEPVTkaedpVKFHEAwqklclADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNP-GDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCIL-KPGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9055198    480 HRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 556.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198      2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198     82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFVE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 9055198    242 ICIHDVSSIYRVPLLLEEQGVVKYFQERLGL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 530.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:cd03113   1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVdgnkedPQICVIELGGTIGDIEGMAFVE 161
Cdd:cd03113  81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPE------PDVCIVEIGGTVGDIESLPFLE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                       250       260
                ....*....|....*....|....*..
gi 9055198  242 ICIHDVSSIYRVPLLLEEQGVVKYFQE 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 299-544 1.94e-134

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 391.15  E-value: 1.94e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  299 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpvkfheAWQKLCLADGILVPGGFGIRGT 378
Cdd:cd01746   1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  379 LGKLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPE-HNPGDLGGTMRLGLRRTVF 457
Cdd:cd01746  71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  458 tTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPS 537
Cdd:cd01746 151 -KPGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                ....*..
gi 9055198  538 PPYLGLL 544
Cdd:cd01746 229 PLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
310-546 6.88e-43

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 152.01  E-value: 6.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    310 LRDCYASVFKALEHSALAINHKLNLMYIDSIDLEpvTKAEDPvkfheawqklclaDGILVPGGFGIRGTLG-KLQAISWA 388
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEE--ILEENP-------------DGIILSGGPGSPGAAGgAIEAIREA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    389 RTKKIPFLGICLGMQLAVIEFARNCLNLKDanstefepntpvplvidmpehnPGDLGGTMRLGLRRTvfttensilKKLY 468
Cdd:pfam00117  67 RELKIPILGICLGHQLLALAFGGKVVKAKK----------------------FGHHGKNSPVGDDGC---------GLFY 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055198    469 GDVPYIEERHRHRYEVNPNlinqFENKDLCFVGEDVDG-KRMEIVELTSHpyFIGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 301-547 1.25e-29

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 116.60  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   301 IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLepvTKAEDPVKFHEAWqklcladgiLVPGGfGIRGTLG 380
Cdd:PRK06186   4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI---TDPEDLAGFDGIW---------CVPGS-PYRNDDG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   381 KLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTP----VPLVIDMPEHNpgdlgGTMRLglrrtv 456
Cdd:PRK06186  71 ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDrpviAPLSCSLVEKT-----GDIRL------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   457 ftTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGkrmEI--VELTSHPYFIGVQFHPEFSSRPM 534
Cdd:PRK06186 140 --RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALAG 213

                        250
                 ....*....|...
gi 9055198   535 KPSPPYLGLLLAA 547
Cdd:PRK06186 214 RPPPLVRAFLRAA 226
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-407 6.35e-10

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.84  E-value: 6.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 379
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                        90       100       110
                ....*....|....*....|....*....|.
gi 9055198  380 ---GKLQAISWARTKKIPFLGICLGMQLAVI 407
Cdd:cd01653  64 rdeALLALLREAAAAGKPILGICLGAQLLVL 94
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 330-529 9.27e-10

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


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 59.03  E-value: 9.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  330 HKLNLMYIDSID-------LEPVTKAEDPVKfheawQKLCLADGILVPGG-------FG--IRGTLGK---------LQA 384
Cdd:COG2071  14 HYLPEDYVRAVRaagglpvLLPPVGDEEDLD-----ELLDRLDGLVLTGGadvdpalYGeePHPELGPidperdafeLAL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  385 ISWARTKKIPFLGICLGMQLaviefarncLNlkdanstefepntpV----PLVIDMPEHNPGDLG---GTMRLGLRRTVF 457
Cdd:COG2071  89 IRAALERGKPVLGICRGMQL---------LN--------------ValggTLYQDLPDQVPGALDhrqPAPRYAPRHTVE 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  458 TTENSILKKLYGdvpyieerhRHRYEVNpnlinqfenkdlCF-------VGEDV-------DGkrmeIVE---LTSHPYF 520
Cdd:COG2071 146 IEPGSRLARILG---------EEEIRVN------------SLhhqavkrLGPGLrvsarapDG----VIEaieSPGAPFV 200


                ....*....
gi 9055198  521 IGVQFHPEF 529
Cdd:COG2071 201 LGVQWHPEW 209
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-404 2.03e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 51.82  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 379
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                        90       100
                ....*....|....*....|....*...
gi 9055198  380 ---GKLQAISWARTKKIPFLGICLGMQL 404
Cdd:cd03128  64 wdeALLALLREAAAAGKPVLGICLGAQL 91
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 359-532 2.37e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 48.32  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   359 QKLCLADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLavieFAR-------NCLNLKDANSTEFE 425
Cdd:PRK13181  33 EEIAGADKVILPGvgafGQAMRSlrESGLDEALKEHVEKKQPVLGICLGMQL----LFEsseegnvKGLGLIPGDVKRFR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   426 PNT-PVPlvidmpehnpgdlggtmRLGLRRTVFTTENSILKKlygdvpyIEERHR----HRYEVNPNlinqfenkdlcfV 500
Cdd:PRK13181 109 SEPlKVP-----------------QMGWNSVKPLKESPLFKG-------IEEGSYfyfvHSYYVPCE------------D 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 9055198   501 GEDVDGKRMEIVELTSHPY---FIGVQFHPEFSSR 532
Cdd:PRK13181 153 PEDVLATTEYGVPFCSAVAkdnIYAVQFHPEKSGK 187
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 392-528 7.91e-06

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 47.25  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198    392 KIPFLGICLGMQLAVIEFARNcLNLkDANStefepntpVPLVIDMPEHNPGDLGGTmrlglRRTVFTTENSILKKLYGDv 471
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGT-LYQ-DIQE--------QPGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASLLGS- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9055198    472 pyiEErhrhrYEVNpNLINQFENK---DLCFVGEDVDGKrMEIVELTSHPYF-IGVQFHPE 528
Cdd:pfam07722 169 ---EE-----FRVN-SLHHQAIDRlapGLRVEAVAPDGT-IEAIESPNAKGFaLGVQWHPE 219
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-66 4.73e-05

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 42.80  E-value: 4.73e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9055198    2 KYILVTGGViSGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAG--------------TFSPYEHGEVFVLNDGGE 66
Cdd:cd01983   1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGggletglllgtivaLLALKKADEVIVVVDPEL 78
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 364-404 4.74e-05

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 44.64  E-value: 4.74e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 9055198  364 ADGILVPG-G-FG-----IRGtLGKLQAISWARTKKIPFLGICLGMQL 404
Cdd:COG0118  39 ADRLVLPGvGaFGdamenLRE-RGLDEAIREAVAGGKPVLGICLGMQL 85
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 364-404 1.24e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 43.32  E-value: 1.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 9055198   364 ADGILVPG--GFGIRGT-LGKL-QAISWARTKKIPFLGICLGMQL 404
Cdd:PRK13143  39 ADGIVLPGvgAFGAAMEnLSPLrDVILEAARSGKPFLGICLGMQL 83
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 359-528 2.45e-04

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


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 43.08  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  359 QKLCLADGILVPGGFGirgtlgKLQAISWARTKKI---------------PFLGICLGMQLAVIEFARNCLNLKDANSTE 423
Cdd:cd01747  50 KLFKSINGILFPGGAV------DIDTSGYARTAKIiynlalerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEATN 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  424 fepntpvplvIDMPEHNPGDLggtmrlgLRRTVF-TTENSILKKLyGDVPYIEerHRHRYEVNPN------LINQFENkd 496
Cdd:cd01747 124 ----------SALPLNFTEDA-------LQSRLFkRFPPDLLKSL-ATEPLTM--NNHRYGISPEnftengLLSDFFN-- 181

                       170       180       190
                ....*....|....*....|....*....|...
gi 9055198  497 LCFVGEDVDGKR-MEIVELTSHPYFiGVQFHPE 528
Cdd:cd01747 182 VLTTNDDWNGVEfISTVEAYKYPIY-GVQWHPE 213
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 364-532 4.53e-04

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


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 41.71  E-value: 4.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  364 ADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLAvieFAR-------NCLNLKDANSTEFEPNTPV 430
Cdd:cd01748  37 ADKLILPGvgafGDAMANlrERGLIEALKEAIASGKPFLGICLGMQLL---FESseegggtKGLGLIPGKVVRFPASEGL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198  431 PLvidmPeHnpgdlggtMrlGLRRTVFTTENSILKklygdvpYIEERHR----HRYEVNPNlinqfENKDL---CFVGED 503
Cdd:cd01748 114 KV----P-H--------M--GWNQLEITKESPLFK-------GIPDGSYfyfvHSYYAPPD-----DPDYIlatTDYGGK 166

                       170       180
                ....*....|....*....|....*....
gi 9055198  504 VDGkrmeIVEltsHPYFIGVQFHPEFSSR 532
Cdd:cd01748 167 FPA----AVE---KDNIFGTQFHPEKSGK 188
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 315-404 6.65e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 41.27  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9055198   315 ASVFKALEhsalainhKLNLMYIdsidlepVTKaeDPvkfheawQKLCLADGILVPG--GFG-----IRGTlGKLQAISW 387
Cdd:PRK13141  13 RSVEKALE--------RLGAEAV-------ITS--DP-------EEILAADGVILPGvgAFPdamanLRER-GLDEVIKE 67

                         90
                 ....*....|....*..
gi 9055198   388 ARTKKIPFLGICLGMQL 404
Cdd:PRK13141  68 AVASGKPLLGICLGMQL 84
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 364-404 8.94e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 40.92  E-value: 8.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 9055198   364 ADGILVPG---------GFGIRGTLGKLQAISWARTKkiPFLGICLGMQL 404
Cdd:PRK13146  42 ADRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLGICVGMQL 89
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 382-404 6.69e-03

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 38.39  E-value: 6.69e-03
                        10        20
                ....*....|....*....|...
gi 9055198  382 LQAISWARTKKIPFLGICLGMQL 404
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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