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Conserved domains on  [gi|489004604|ref|WP_002915214|]
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MULTISPECIES: glutamine hydrolyzing CTP synthase [Klebsiella]

Protein Classification

CTP synthase( domain architecture ID 11480813)

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

EC:  6.3.4.2
Gene Ontology:  GO:0000166|GO:0006241|GO:0046872|GO:0003883
PubMed:  15296735

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 3-543 0e+00

CTP synthetase; Validated


:

Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1093.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 243 SIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 323 VNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 402 TEFVPDCKYPVVALITEWRDEdgnvevrsekSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLKSI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489004604 482 EAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEYQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 3-543 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1093.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 243 SIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 323 VNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 402 TEFVPDCKYPVVALITEWRDEdgnvevrsekSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLKSI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489004604 482 EAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEYQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 3-544 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: 1075.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 241 VDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 321 VTVNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENA 399
Cdd:COG0504  321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 400 NSTEFVPDCKYPVVALITEwrdedgnvevRSEKSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLK 479
Cdd:COG0504  401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004604 480 SIEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEYQKRQA 544
Cdd:COG0504  471 QLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 3-535 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: 971.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  241 VDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  321 VTVNIKLIDSQDVETRGVEILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  401 STEFVPDCKYPVVALITEWRDedgnvevrseKSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLKS 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489004604  481 IEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 5-266 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: 524.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604    5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   85 TRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241

                         250       260
                  ....*....|....*....|....
gi 489004604  243 SIYKIPGLLKSQGLDDYICKRFSL 266
Cdd:pfam06418 242 SIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 5-262 1.58e-167

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: 475.05  E-value: 1.58e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113    2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  85 TRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERV--LAGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113   82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIrrVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113  162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241

                        250       260
                 ....*....|....*....|
gi 489004604 243 SIYKIPGLLKSQGLDDYICK 262
Cdd:cd03113  242 SIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 3-543 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1093.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 243 SIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 323 VNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 402 TEFVPDCKYPVVALITEWRDEdgnvevrsekSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLKSI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489004604 482 EAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEYQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 3-544 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: 1075.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 241 VDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 321 VTVNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENA 399
Cdd:COG0504  321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 400 NSTEFVPDCKYPVVALITEwrdedgnvevRSEKSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLK 479
Cdd:COG0504  401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004604 480 SIEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEYQKRQA 544
Cdd:COG0504  471 QLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 3-535 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: 971.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  241 VDSIYKIPGLLKSQGLDDYICKRFSLTCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  321 VTVNIKLIDSQDVETRGVEILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLGMQVALIEFARNVAGMENAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  401 STEFVPDCKYPVVALITEWRDedgnvevrseKSDLGGTMRLGAQQCQLSDDSLVRQLYGEPTITERHRHRYEVNNMLLKS 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489004604  481 IEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
PLN02327 PLN02327
CTP synthase
 3-537 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 644.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  83 KMTRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIK---ERV----LAGGEGH-DVVLVEIGGTVGDIESLPFL 154
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQewiERVakipVDGKEGPaDVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 155 EAIRQMAVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKA 234
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 235 VISLKDVDSIYKIPGLLKSQGLDDYICKRFSL--TCPEANLAEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEAL 312
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlsVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 313 KHGGLKNRVTVNIKLIDSQDVETRGV-----------EILKDLDAILIPGGFGYRGVEGKIATARYARENNIPYLGICLG 381
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAketpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 382 MQVALIEFARNVAGMENANSTEFVPDCKYPVVALITEwrdedgnvevrSEKSDLGGTMRLGAQQCQLSD-DSLVRQLYG- 459
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPE-----------GSKTHMGGTMRLGSRRTYFQTpDCKSAKLYGn 469

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489004604 460 EPTITERHRHRYEVNNMLLKSIEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAS 537
Cdd:PLN02327 470 VSFVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAAS 547
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 5-266 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: 524.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604    5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   85 TRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLAGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241

                         250       260
                  ....*....|....*....|....
gi 489004604  243 SIYKIPGLLKSQGLDDYICKRFSL 266
Cdd:pfam06418 242 SIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 5-262 1.58e-167

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: 475.05  E-value: 1.58e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113    2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  85 TRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERV--LAGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113   82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIrrVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113  162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241

                        250       260
                 ....*....|....*....|
gi 489004604 243 SIYKIPGLLKSQGLDDYICK 262
Cdd:cd03113  242 SIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 290-533 1.22e-138

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: 400.39  E-value: 1.22e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 290 VTIGMVGKYIELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVETRGV-EILKDLDAILIPGGFGYRGVEGKIATARYA 368
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAeEALKGADGILVPGGFGIRGVEGKILAIKYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 369 RENNIPYLGICLGMQVALIEFARNVAGMENANSTEFVPDCKYPVVALITEWRDedgnvevrseKSDLGGTMRLGAQQCQL 448
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKG----------VKDLGGTMRLGAYPVIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 449 SDDSLVRQLYGEPTITERHRHRYEVNNMLLKSIEAAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPL 528
Cdd:cd01746  151 KPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230


                 ....*
gi 489004604 529 FAGFV 533
Cdd:cd01746  231 FVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
300-535 2.22e-47

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 163.18  E-value: 2.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  300 ELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVETRGVEIlkdlDAILIPGGFGYRG-VEGKIATARYARENNIPYLGI 378
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENP----DGIILSGGPGSPGaAGGAIEAIREARELKIPILGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  379 CLGMQVALIEFArnvagmenanstefvpdckypvvalitewrdedGNVEVRSEKSDLGGTMRLGAQQCQLsddslvrqLY 458
Cdd:pfam00117  77 CLGHQLLALAFG---------------------------------GKVVKAKKFGHHGKNSPVGDDGCGL--------FY 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489004604  459 GEP-TITERHRHRYEVNNMLLKsieaAGLRVAGRSGDD-QLVEIIEVPNhPWFvACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:pfam00117 116 GLPnVFIVRRYHSYAVDPDTLP----DGLEVTATSENDgTIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 292-538 1.40e-36

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 135.48  E-value: 1.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 292 IGMVGKYIELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVetRGVEILKDLDAI-LIPGGfGYRGVEGKIATARYARE 370
Cdd:PRK06186   4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI--TDPEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 371 NNIPYLGICLGMQVALIEFARNVAGMENANSTEFVPDCKYPVVA-LITEWRDEDGNVEVRSeksdlggtmrlgaqqcqls 449
Cdd:PRK06186  81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDIRLRP------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 450 dDSLVRQLYGEPTITERHRHRYEVNNMLLKSIEAAGLRVAGRsGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLF 529
Cdd:PRK06186 142 -GSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGW-DEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLV 219


                 ....*....
gi 489004604 530 AGFVKAASE 538
Cdd:PRK06186 220 RAFLRAARA 228
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 327-539 1.20e-17

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: 82.14  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 327 LIDSQDVETRGVEILKDLDAILIPGG-------FGYRGVEGK-----------IATARYARENNIPYLGICLGMQVAlie 388
Cdd:COG2071   33 LLPPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLL--- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 389 farNVA--GmenanstefvpdckypvvALITEWRDEDGNVEVRSEKSDlggtMRLGAQQCQLSDDSLVRQLYGEPTIter 466
Cdd:COG2071  110 ---NVAlgG------------------TLYQDLPDQVPGALDHRQPAP----RYAPRHTVEIEPGSRLARILGEEEI--- 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489004604 467 hrhryEVN---NMLLKSIeAAGLRVAGRSgDDQLVEIIEVPNHPWFVACQFHPEF-TSTPRDGHPLFAGFVKAASEY 539
Cdd:COG2071  162 -----RVNslhHQAVKRL-GPGLRVSARA-PDGVIEAIESPGAPFVLGVQWHPEWlAASDPLSRRLFEAFVEAARAR 231
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 292-387 1.25e-12

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: 64.54  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvtVNIKLIDSQDVETRGVEILKDLDAILIPGGFGYRGV----EGKIATARY 367
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlardEALLALLRE 74

                         90       100
                 ....*....|....*....|
gi 489004604 368 ARENNIPYLGICLGMQVALI 387
Cdd:cd01653   75 AAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 292-384 2.43e-11

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: 60.29  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvtVNIKLIDSQDVETRGVEILKDLDAILIPGGFGYRGV----EGKIATARY 367
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlawdEALLALLRE 74

                         90
                 ....*....|....*..
gi 489004604 368 ARENNIPYLGICLGMQV 384
Cdd:cd03128   75 AAAAGKPVLGICLGAQL 91
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 327-533 1.94e-09

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: 57.20  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 327 LIDSQDVETRGVEILKDLDAILIPGG-----FGYRGV-------------EGKIATARYARENNIPYLGICLGMQvaLIe 388
Cdd:cd01745   37 LLPPVDDEEDLEQYLELLDGLLLTGGgdvdpPLYGEEphpelgpidperdAFELALLRAALERGKPILGICRGMQ--LL- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 389 farNVAgmenanstefvpdckypvvalitewrdedgnvevrseksdLGGTMrlgaqqcqlsddslvrqlygEPTITERHR 468
Cdd:cd01745  114 ---NVA----------------------------------------LGGTL--------------------YQDIRVNSL 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489004604 469 HRYEVNNMllksieAAGLRVAGRSGDdQLVEIIEVPNHPWFVACQFHPEFTSTPRDGH-PLFAGFV 533
Cdd:cd01745  131 HHQAIKRL------ADGLRVEARAPD-GVIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 329-517 3.59e-08

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 54.19  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  329 DSQDVETrgveILKDLDAILIPGG-------FGYRGVEG-----------KIATARYARENNIPYLGICLGMQvaLIefa 390
Cdd:pfam07722  48 DPEDAAA----ILDRLDGLLLTGGpnvdphfYGEEPSESggpydpardayELALIRAALARGKPILGICRGFQ--LL--- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  391 rNVA--GmenanstefvpdckypvvALITEWRDEDGNVEVRSEKSDLGGtmrLGAQQCQLSDDSLVRQLYGEPTIterhr 468
Cdd:pfam07722 119 -NVAlgG------------------TLYQDIQEQPGFTDHREHCQVAPY---APSHAVNVEPGSLLASLLGSEEF----- 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489004604  469 hryEVNNMLLKSIE--AAGLRVAGRSgDDQLVEIIEVPNHPWFV-ACQFHPE 517
Cdd:pfam07722 172 ---RVNSLHHQAIDrlAPGLRVEAVA-PDGTIEAIESPNAKGFAlGVQWHPE 219
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 339-543 4.28e-06

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 48.36  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 339 EILKDLDAILIPGG--------FGYRGVE-----GK----IATARYARENNIPYLGICLGMQVALIEfarnvagmenANS 401
Cdd:PRK11366  57 QLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALINAALERRIPIFAICRGLQELVVA----------TGG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 402 TEFVPDCKYPvvALITEWRDEDGNVEVRSEKSdlggtmrlgaQQCQLSDDSLVRQLYGEPTiterhrhRYEVNNMLLKSI 481
Cdd:PRK11366 127 SLHRKLCEQP--ELLEHREDPELPVEQQYAPS----------HEVQVEEGGLLSALLPECS-------NFWVNSLHGQGA 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004604 482 E--AAGLRVAGRSGDDqLVEIIEVPNHPWFVACQFHPEFTSTPRD-GHPLFAGFVKAASEYQKRQ 543
Cdd:PRK11366 188 KvvSPRLRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITACQHHIAEK 251
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 135-210 7.23e-06

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: 45.11  E-value: 7.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489004604 135 DVVLVEIGGTVGDIESLPFleairQMAVEIGREHTLFMHLTLVPYMAAAGEVKTKptqhSVKELLSIGIQPDILIC 210
Cdd:cd01983   39 DYVLIDGGGGLETGLLLGT-----IVALLALKKADEVIVVVDPELGSLLEAVKLL----LALLLLGIGIRPDGIVL 105
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 306-383 3.98e-05

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 44.62  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604  306 KSVIEALKHGGLKNRVTVNiklidsqdvetrgVEILKDLDAILIPG----GFGYRGVE--GKIATARYARENNIPYLGIC 379
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVVKD-------------SKEAELADKLILPGvgafGAAMARLRenGLDLFVELVVRLGKPVLGIC 78


                  ....
gi 489004604  380 LGMQ 383
Cdd:TIGR01855  79 LGMQ 82
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 306-384 7.80e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.88  E-value: 7.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 306 KSVIEALKHGGLKNRVTvniklidsqdvetRGVEILKDLDAILIPG--GFG-------YRGVEGKIataRYARENNIPYL 376
Cdd:PRK13141  13 RSVEKALERLGAEAVIT-------------SDPEEILAADGVILPGvgAFPdamanlrERGLDEVI---KEAVASGKPLL 76


                 ....*...
gi 489004604 377 GICLGMQV 384
Cdd:PRK13141  77 GICLGMQL 84
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 306-384 1.23e-03

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


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 40.17  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 306 KSVIEALKHGGLKNRVTvniklidsqdvetRGVEILKDLDAILIPG-G-FG-------YRGVEGKIataRYARENNIPYL 376
Cdd:cd01748   12 RSVANALERLGAEVIIT-------------SDPEEILSADKLILPGvGaFGdamanlrERGLIEAL---KEAIASGKPFL 75


                 ....*...
gi 489004604 377 GICLGMQV 384
Cdd:cd01748   76 GICLGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 307-384 1.24e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 40.24  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 307 SVIEALKHGGLKNRVTVNIklidsqdvetrgvEILKDLDAILIPG----GFGYRGVEGKIATARYARENNIPYLGICLGM 382
Cdd:PRK13143  15 SVSKALERAGAEVVITSDP-------------EEILDADGIVLPGvgafGAAMENLSPLRDVILEAARSGKPFLGICLGM 81


                 ..
gi 489004604 383 QV 384
Cdd:PRK13143  82 QL 83
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 358-534 5.41e-03

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 39.23  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 358 VEGKIATARYARENNIPYLGICLGMQValieFARnvagmenAN--STEfvpdcK---------YPVVALITewrdedGNV 426
Cdd:COG0505  233 LDYAIETIRELLGKGIPIFGICLGHQL----LAL-------ALgaKTY-----KlkfghrganHPVKDLET------GRV 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 427 EVRSeksdlggtmrlgaqqcqlsddslvrqlygeptiterHRHRYEVNNmllKSIEAAGLRVAGRSGDDQLVEIIEVPNH 506
Cdd:COG0505  291 EITS------------------------------------QNHGFAVDE---DSLPATDLEVTHVNLNDGTVEGLRHKDL 331

                        170       180
                 ....*....|....*....|....*....
gi 489004604 507 PWF-VacQFHPEFTSTPRDGHPLFAGFVK 534
Cdd:COG0505  332 PAFsV--QYHPEASPGPHDSAYLFDRFIE 358
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 341-433 8.39e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 37.98  E-value: 8.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004604 341 LKDLDAILIPGGFGY----RGveGKIATARYARENNI--------PYLGICLGMQVaLIEfARNVAGMENANSTEfvpdc 408
Cdd:cd01740   41 LDDYDGVVLPGGFSYgdylRA--GAIAAASPLLMEEVkefaerggLVLGICNGFQI-LVE-LGLLPGALIRNKGL----- 111

                         90       100
                 ....*....|....*....|....*
gi 489004604 409 kypvvALITEWRDEDGNVEVRSEKS 433
Cdd:cd01740  112 -----KFICRWQNRFVTLRVENNDS 131
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 328-382 9.40e-03

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 37.56  E-value: 9.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489004604 328 IDSQDVETRGVEILKDLDAILIPGG--------FGYRGVEGKIataRYARENNIPYLGICLGM 382
Cdd:PRK13527  28 IDGEVVEVRRPGDLPDCDALIIPGGesttigrlMKREGILDEI---KEKIEEGLPILGTCAGL 87
 
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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