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Conserved domains on  [gi|1100260834|gb|OIK42301|]
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CTP synthase [Citrobacter portucalensis]

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
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: 1094.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380    2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380   82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380  162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380  242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 323 VNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNANS 401
Cdd:PRK05380  322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 402 TEFVPDCKYPVVALITEWRDEdgnvevrtekSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380  402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100260834 482 EAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQ 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: 1094.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380    2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380   82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380  162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380  242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 323 VNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNANS 401
Cdd:PRK05380  322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 402 TEFVPDCKYPVVALITEWRDEdgnvevrtekSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380  402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100260834 482 EAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQ 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: 1076.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504   161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504   241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 321 VTVNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNA 399
Cdd:COG0504   321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 400 NSTEFVPDCKYPVVALITEwrdedgnvevRTEKSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLK 479
Cdd:COG0504   401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100260834 480 QIEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQA 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: 972.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 321 VTVNIKLIDSQDVETRGVEILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 401 STEFVPDCKYPVVALITEWRDedgnvevrteKSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQ 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1100260834 481 IEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 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 1100260834   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241
                         250       260
                  ....*....|....*....|....
gi 1100260834 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 2.43e-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: 474.67  E-value: 2.43e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113     2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGH--DVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113    82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPepDVCIVEIGGTVGDIESLPFLEALRQFQF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113   162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241
                         250       260
                  ....*....|....*....|
gi 1100260834 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: 1094.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380    2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380   82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380  162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVT 322
Cdd:PRK05380  242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 323 VNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNANS 401
Cdd:PRK05380  322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 402 TEFVPDCKYPVVALITEWRDEdgnvevrtekSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380  402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100260834 482 EAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQ 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: 1076.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504   161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504   241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 321 VTVNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNA 399
Cdd:COG0504   321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 400 NSTEFVPDCKYPVVALITEwrdedgnvevRTEKSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLK 479
Cdd:COG0504   401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100260834 480 QIEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEHQKRQA 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: 972.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 161 AVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 321 VTVNIKLIDSQDVETRGVEILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLGMQVALIEFARNVVGMDNAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 401 STEFVPDCKYPVVALITEWRDedgnvevrteKSDLGGTMRLGAQQCQLSDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQ 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1100260834 481 IEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 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: 643.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PLN02327    1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIK---ERV----LEGGEGH-DVVLVEIGGTVGDIESLPFL 154
Cdd:PLN02327   81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQewiERVakipVDGKEGPaDVCVIELGGTVGDIESMPFI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 155 EAIRQMAVEIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKA 234
Cdd:PLN02327  161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 235 VISLKDVDSIYKIPGLLKSQGLDDYICKRFSL--NCPEANLSEWEQVIYEEANPAGEVTIGMVGKYIELPDAYKSVIEAL 312
Cdd:PLN02327  241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlsVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 313 KHGGLKNRVTVNIKLIDSQDVETRGV-----------EILKGLDAILIPGGFGYRGVEGKIATARFARENNIPYLGICLG 381
Cdd:PLN02327  321 LHASVACSRKLVIDWVAASDLEDETAketpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 382 MQVALIEFARNVVGMDNANSTEFVPDCKYPVVALITEwrdedgnvevrTEKSDLGGTMRLGAQQCQLSD-DSLVRQLYGA 460
Cdd:PLN02327  401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPE-----------GSKTHMGGTMRLGSRRTYFQTpDCKSAKLYGN 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1100260834 461 PTIV-ERHRHRYEVNNMLLKQIEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAS 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 1100260834   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241
                         250       260
                  ....*....|....*....|....
gi 1100260834 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 2.43e-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: 474.67  E-value: 2.43e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113     2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGH--DVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113    82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPepDVCIVEIGGTVGDIESLPFLEALRQFQF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 163 EIGREHTLFMHLTLVPYMAAAGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113   162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241
                         250       260
                  ....*....|....*....|
gi 1100260834 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 5.26e-139

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


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 401.55  E-value: 5.26e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 290 VTIGMVGKYIELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVETRGV-EILKGLDAILIPGGFGYRGVEGKIATARFA 368
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAeEALKGADGILVPGGFGIRGVEGKILAIKYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 369 RENNIPYLGICLGMQVALIEFARNVVGMDNANSTEFVPDCKYPVVALITEWRDedgnvevrteKSDLGGTMRLGAQQCQL 448
Cdd:cd01746    81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKG----------VKDLGGTMRLGAYPVIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 449 SDDSLVRQLYGAPTIVERHRHRYEVNNMLLKQIEAAGLRIAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPL 528
Cdd:cd01746   151 KPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230

                  ....*
gi 1100260834 529 FAGFV 533
Cdd:cd01746   231 FVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
300-535 9.53e-47

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 161.64  E-value: 9.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 300 ELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVETRGVEIlkglDAILIPGGFGYRG-VEGKIATARFARENNIPYLGI 378
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENP----DGIILSGGPGSPGaAGGAIEAIREARELKIPILGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 379 CLGMQVALIEFARNVVGMdnanstefvpdckypvvalitewrdedgnvevrTEKSDLGGTMRLGAQQCQLSDDSlvrqly 458
Cdd:pfam00117  77 CLGHQLLALAFGGKVVKA---------------------------------KKFGHHGKNSPVGDDGCGLFYGL------ 117
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1100260834 459 gAPTIVERHRHRYEVNNMLLKqieaAGLRIAGRSGDD-QLVEIIEVPNhPWFvACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:pfam00117 118 -PNVFIVRRYHSYAVDPDTLP----DGLEVTATSENDgTIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
292-539 1.76e-38

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 140.87  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 292 IGMVGKYIELPDAYKSVIEALKHGGLKNRVTVNIKLIDSQDVetRGVEILKGLDAI-LIPGGfGYRGVEGKIATARFARE 370
Cdd:PRK06186    4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI--TDPEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 371 NNIPYLGICLGMQVALIEFARNVVGMDNANSTEFVPDCKYPVVA-LITEWRDEDGNVEVRteksdlggtmrlgaqqcqls 449
Cdd:PRK06186   81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDIRLR-------------------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 450 DDSLVRQLYGAPTIVERHRHRYEVNNMLLKQIEAAGLRIAGRsGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLF 529
Cdd:PRK06186  141 PGSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGW-DEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLV 219
                         250
                  ....*....|
gi 1100260834 530 AGFVKAASEH 539
Cdd:PRK06186  220 RAFLRAARAA 229
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
327-539 3.51e-16

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: 77.90  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 327 LIDSQDVETRGVEILKGLDAILIPGG-------FGYRGVEGK-----------IATARFARENNIPYLGICLGMQVAlie 388
Cdd:COG2071    33 LLPPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLL--- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 389 farNVV--GmdnanstefvpdckypvvALITEWRDEDGNVEVRTEKSDlggtMRLGAQQCQLSDDSLVRQLYGAPTIver 466
Cdd:COG2071   110 ---NVAlgG------------------TLYQDLPDQVPGALDHRQPAP----RYAPRHTVEIEPGSRLARILGEEEI--- 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100260834 467 hrhryEVN---NMLLKQIeAAGLRIAGRSgDDQLVEIIEVPNHPWFVACQFHPEF-TSTPRDGHPLFAGFVKAASEH 539
Cdd:COG2071   162 -----RVNslhHQAVKRL-GPGLRVSARA-PDGVIEAIESPGAPFVLGVQWHPEWlAASDPLSRRLFEAFVEAARAR 231
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
292-387 8.91e-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: 62.23  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvtVNIKLIDSQDVETRGVEILKGLDAILIPGGFGYRGV----EGKIATARF 367
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlardEALLALLRE 74
                          90       100
                  ....*....|....*....|
gi 1100260834 368 ARENNIPYLGICLGMQVALI 387
Cdd:cd01653    75 AAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
292-384 1.57e-10

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 57.98  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvtVNIKLIDSQDVETRGVEILKGLDAILIPGGFGYRGV----EGKIATARF 367
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlawdEALLALLRE 74
                          90
                  ....*....|....*..
gi 1100260834 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 5.27e-08

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: 52.96  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 327 LIDSQDVETRGVEILKGLDAILIPGG-----FGYRGV-------------EGKIATARFARENNIPYLGICLGMQvaLIe 388
Cdd:cd01745    37 LLPPVDDEEDLEQYLELLDGLLLTGGgdvdpPLYGEEphpelgpidperdAFELALLRAALERGKPILGICRGMQ--LL- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 389 farNVVgmdnanstefvpdckypvvalitewrdedgnvevrteksdLGGTMRLgaqqcqlsdDSLVRQLygaptiverhr 468
Cdd:cd01745   114 ---NVA----------------------------------------LGGTLYQ---------DIRVNSL----------- 130
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1100260834 469 HRYEVNNMllkqieAAGLRIAGRSGDdQLVEIIEVPNHPWFVACQFHPEFTSTPRDGH-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 1.43e-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: 49.18  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 329 DSQDVETrgveILKGLDAILIPGG-------FGYRGVEG-----------KIATARFARENNIPYLGICLGMQ---VAL- 386
Cdd:pfam07722  48 DPEDAAA----ILDRLDGLLLTGGpnvdphfYGEEPSESggpydpardayELALIRAALARGKPILGICRGFQllnVALg 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 387 ------IEfarnvvgmDNANSTEFVPDCKYPVVAlitewrdedgnvevrteksdlggtmrlGAQQCQLSDDSLVRQLYGA 460
Cdd:pfam07722 124 gtlyqdIQ--------EQPGFTDHREHCQVAPYA---------------------------PSHAVNVEPGSLLASLLGS 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100260834 461 PTIVERHRHRYEVNNMllkqieAAGLRIAGRSgDDQLVEIIEVPNHPWFV-ACQFHPE 517
Cdd:pfam07722 169 EEFRVNSLHHQAIDRL------APGLRVEAVA-PDGTIEAIESPNAKGFAlGVQWHPE 219
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
135-210 7.37e-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: 7.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1100260834 135 DVVLVEIGGTVGDIESLPFleairQMAVEIGREHTLFMHLTLVPYMAAAGEVKTKptqhSVKELLSIGIQPDILIC 210
Cdd:cd01983    39 DYVLIDGGGGLETGLLLGT-----IVALLALKKADEVIVVVDPELGSLLEAVKLL----LALLLLGIGIRPDGIVL 105
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
339-543 1.48e-05

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 46.82  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 339 EILKGLDAILIPGG--------FGYRGVE-----GK----IATARFARENNIPYLGICLGMQVALIEfarnvvgmdnANS 401
Cdd:PRK11366   57 QLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALINAALERRIPIFAICRGLQELVVA----------TGG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 402 TEFVPDCKYPvvALITEWRDEDGNVEVRTEKSdlggtmrlgaQQCQLSDDSLVRQLYgaPTIverhrHRYEVNNMLLK-- 479
Cdd:PRK11366  127 SLHRKLCEQP--ELLEHREDPELPVEQQYAPS----------HEVQVEEGGLLSALL--PEC-----SNFWVNSLHGQga 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100260834 480 QIEAAGLRIAGRSGDDqLVEIIEVPNHPWFVACQFHPEFTSTPRD-GHPLFAGFVKAASEHQKRQ 543
Cdd:PRK11366  188 KVVSPRLRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITACQHHIAEK 251
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
306-383 6.52e-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: 44.24  E-value: 6.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 306 KSVIEALKHGGLKNRVTVNiklidsqdvetrgVEILKGLDAILIPG----GFGYRGVE--GKIATARFARENNIPYLGIC 379
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVVKD-------------SKEAELADKLILPGvgafGAAMARLRenGLDLFVELVVRLGKPVLGIC 78

                  ....
gi 1100260834 380 LGMQ 383
Cdd:TIGR01855  79 LGMQ 82
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
306-384 1.18e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.50  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 306 KSVIEALKHGGLKNRVTvniklidsqdvetRGVEILKGLDAILIPG--GFG-------YRGVEGKIataRFARENNIPYL 376
Cdd:PRK13141   13 RSVEKALERLGAEAVIT-------------SDPEEILAADGVILPGvgAFPdamanlrERGLDEVI---KEAVASGKPLL 76

                  ....*...
gi 1100260834 377 GICLGMQV 384
Cdd:PRK13141   77 GICLGMQL 84
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
341-388 1.77e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 40.10  E-value: 1.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100260834 341 LKGLDAILIPGGFGY----R-GvegkiATARFAR---------ENNIPYLGICLGMQVaLIE 388
Cdd:PRK03619   39 LDGVDAVVLPGGFSYgdylRcG-----AIAAFSPimkavkefaEKGKPVLGICNGFQI-LTE 94
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
306-384 3.37e-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: 39.02  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 306 KSVIEALKHGGLKNRVTVNIKLIDSQDvetrgveilkgldAILIPG-G-FG-------YRGVEGKIataRFARENNIPYL 376
Cdd:cd01748    12 RSVANALERLGAEVIITSDPEEILSAD-------------KLILPGvGaFGdamanlrERGLIEAL---KEAIASGKPFL 75

                  ....*...
gi 1100260834 377 GICLGMQV 384
Cdd:cd01748    76 GICLGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
307-384 3.53e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 39.08  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100260834 307 SVIEALKHGGLKNRVTVNIKLIDSQDvetrgveilkgldAILIPG----GFGYRGVEGKIATARFARENNIPYLGICLGM 382
Cdd:PRK13143   15 SVSKALERAGAEVVITSDPEEILDAD-------------GIVLPGvgafGAAMENLSPLRDVILEAARSGKPFLGICLGM 81

                  ..
gi 1100260834 383 QV 384
Cdd:PRK13143   82 QL 83
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
341-384 8.24e-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: 8.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1100260834 341 LKGLDAILIPGGFGY----RGveGKIATARFARENNI--------PYLGICLGMQV 384
Cdd:cd01740    41 LDDYDGVVLPGGFSYgdylRA--GAIAAASPLLMEEVkefaerggLVLGICNGFQI 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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