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Conserved domains on  [gi|882678|gb|AAA69294|]
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GTP pyrophosphokinase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

bifunctional (p)ppGpp synthetase/guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase( domain architecture ID 11485050)

bifunctional (p)ppGpp synthetase/guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase mediates the stringent response by producing and regulating the metabolism of the intracellular signaling alarmone (p)ppGpp

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
1-743 0e+00

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


:

Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 1637.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      1 MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
Cdd:PRK10872   1 MVAVRSAHLNKAGEFDPDKWIASLGITSQQSCERLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     81 LFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHL 160
Cdd:PRK10872  81 LFPLADANVVSEDVLRESVGKSIVNLIHGVRDMDAIRQLKATHNDSVSSEQVDNVRRMLLAMVEDFRCVVIKLAERIAHL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEM 240
Cdd:PRK10872 161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPDEYKRIAKLLHERRIDREHYIEEFVGHLRAEM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    241 KAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
Cdd:PRK10872 241 KAEGVKAEVYGRPKHIYSIWRKMQKKSLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    321 SIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGARSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
Cdd:PRK10872 321 SIHTVVLGPGGKTVEIQIRTRQMHEDAELGVAAHWKYKEGAAAGGGRSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
Cdd:PRK10872 401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFL 560
Cdd:PRK10872 481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNSLDELLAAIGGGDIRLNQMVNFL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    561 QSQFNKPSAEEQDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISVHRADCEQ 640
Cdd:PRK10872 561 QSQFNKPSAEEQDAAALKQLQQKTYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISIHRADCEQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    641 LAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
Cdd:PRK10872 641 LAELRSHAPERIVDAVWGESYSSGYSLVVRVTANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
                        730       740
                 ....*....|....*....|...
gi 882678    721 VLGRVLGKLNQVPDVIDARRLHG 743
Cdd:PRK10872 721 VLGRVLGKLNQVPDVIDARRLHG 743
 
Name Accession Description Interval E-value
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
1-743 0e+00

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 1637.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      1 MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
Cdd:PRK10872   1 MVAVRSAHLNKAGEFDPDKWIASLGITSQQSCERLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     81 LFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHL 160
Cdd:PRK10872  81 LFPLADANVVSEDVLRESVGKSIVNLIHGVRDMDAIRQLKATHNDSVSSEQVDNVRRMLLAMVEDFRCVVIKLAERIAHL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEM 240
Cdd:PRK10872 161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPDEYKRIAKLLHERRIDREHYIEEFVGHLRAEM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    241 KAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
Cdd:PRK10872 241 KAEGVKAEVYGRPKHIYSIWRKMQKKSLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    321 SIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGARSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
Cdd:PRK10872 321 SIHTVVLGPGGKTVEIQIRTRQMHEDAELGVAAHWKYKEGAAAGGGRSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
Cdd:PRK10872 401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFL 560
Cdd:PRK10872 481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNSLDELLAAIGGGDIRLNQMVNFL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    561 QSQFNKPSAEEQDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISVHRADCEQ 640
Cdd:PRK10872 561 QSQFNKPSAEEQDAAALKQLQQKTYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISIHRADCEQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    641 LAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
Cdd:PRK10872 641 LAELRSHAPERIVDAVWGESYSSGYSLVVRVTANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
                        730       740
                 ....*....|....*....|...
gi 882678    721 VLGRVLGKLNQVPDVIDARRLHG 743
Cdd:PRK10872 721 VLGRVLGKLNQVPDVIDARRLHG 743
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
59-743 0e+00

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 998.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    59 GVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQlkathtDSVSSEQVDNVRRM 138
Cdd:COG0317  58 PLAVAEILAELGLDAETIAAALLHDVVEDTDVTLEEIEEEFGEEVAELVDGVTKLSKIEF------GSKEEAQAENFRKM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   139 LLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLL 218
Cdd:COG0317 132 LLAMAKDIRVILIKLADRLHNMRTLKAMPPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKLL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   219 HERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHT 298
Cdd:COG0317 212 KEKRGEREEYIEEIIEELKEELAEAGIKAEVSGRPKHIYSIYRKMQRKGLSFEEIYDLYAFRIIVDTVDDCYAALGIVHS 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   299 HYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGarSGHEDRIAWLR 378
Cdd:COG0317 292 LWKPIPGRFKDYIAIPKPNGYQSLHTTVIGPDGKPVEVQIRTEEMHEIAEYGVAAHWKYKEGGGSGD--SSYDEKIAWLR 369
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   379 KLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMG 458
Cdd:COG0317 370 QLLEWQEEAGDSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAYAIHTEVGHRCVGAKVNGRLVPLSTPLKNG 449
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   459 DQIEIITQKQPNPSRDWLNpnlgYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAE-KHLLPRYNFN 537
Cdd:COG0317 450 DTVEIITSKNAGPSRDWLN----FVKTSRARSKIRQWFKKQRREENIELGRELLEKELKRLGLTLDDENlEKLAKKLGFK 525
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   538 DVDELLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAAALKqlqqksytPQNRSKDNGRVVVEGVGNLMHHIARCCQPIP 617
Cdd:COG0317 526 SLDDLLAAIGLGEISLRQVVNRLLPELEKEEPEEEDEELLK--------KSKKKKSDSGVLIDGVDGLLVKLAKCCNPIP 597
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   618 GDEIVGFITQGRGISVHRADCEQLAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGV 697
Cdd:COG0317 598 GDPIVGFVTRGRGVSVHRKDCPNLAELREREPERLIDVEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSV 677
                       650       660       670       680
                ....*....|....*....|....*....|....*....|....*.
gi 882678   698 ASRSDtKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARRLHG 743
Cdd:COG0317 678 NTRSR-DDGTATIRFTVEVRDLDHLARVLRKLRKVPGVISVRRVRG 722
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
65-740 0e+00

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 593.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      65 ILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIrqlkatHTDSVSSEQVDNVRRMLLAMVD 144
Cdd:TIGR00691  30 ILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAELVDGVTKITKL------KKKSRQELQAENFRKMILAMAQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     145 DFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLD 224
Cdd:TIGR00691 104 DIRVIVIKLADRLHNMRTLDFLPPEKQKRIAKETLEIYAPLAHRLGMSSIKTELEDLSFKYLYPKEYENIKSLVNEQKVN 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     225 REHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLP 304
Cdd:TIGR00691 184 RENKLEKFKSELEKRLEDSGIEAELEGRSKHLYSIYQKMTRKGQNFDEIHDLLAIRIIVKSELDCYRVLGIIHLLFKPIP 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     305 DEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGgarSGHEDRIAWLRKLIAWQ 384
Cdd:TIGR00691 264 GRFKDYIASPKENGYQSLHTTVRGPKGLPVEIQIRTEDMDRVAEYGIAAHWIYKEGNPQK---EALIDDMRWLNYLVEWQ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     385 EEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEII 464
Cdd:TIGR00691 341 QESANFFEFIENLKSDLFNEEIYVFTPKGDVVELPSGSTPVDFAYAVHTDVGNKCTGAKVNGKIVPLDKELENGDVVEII 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     465 TQKQPNPSRDWLNpnlgYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHL---LPRYNFNDVDE 541
Cdd:TIGR00691 421 TGKNSNPSVIWLN----FVVTSKARNKIRQWLKKLRREVAISEGKNILEKELGRSGLKLEDLTQYIqkrLNRLRFKKLSE 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     542 LLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAaalkqlqqKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEI 621
Cdd:TIGR00691 497 LLAEIGKGNFSSKEVAKLLAQNNSKWQALTKPL--------KFAFSPKVFENSSFESIEGIEITKIVIAKCCSPIPGDPI 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     622 VGFITQGRGISVHRADCeqlAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRS 701
Cdd:TIGR00691 569 IGIVTKGKGLSVHHKDC---KNLKNYKQEKIIEVEWNASKPRRFIVDINIEAVDRKGVLSDLTTAISENDSNIVSISTKT 645
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 882678     702 DTKqQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARR 740
Cdd:TIGR00691 646 YGK-REAILNITVEIKNYKHLLKIMLKIKTKNDVIVVKR 683
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
251-359 1.55e-58

Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and SpoT of Escherichia coli, and their homologs in plants and in other eubacteria. RelA is a guanosine 3',5'-bis-pyrophosphate (ppGpp) synthetase (EC:2.7.6.5) while SpoT is thought to be a bifunctional enzyme catalysing both ppGpp synthesis and degradation (ppGpp 3'-pyrophosphohydrolase, (EC:3.1.7.2)). This region is often found in association with HD (pfam01966), a metal-dependent phosphohydrolase, TGS (pfam02824) which is a possible nucleotide-binding region, and the ACT regulatory domain (pfam01842).


Pssm-ID: 428031 [Multi-domain]  Cd Length: 113  Bit Score: 193.53  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     251 GRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVL-GP 329
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTVIiGP 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 882678     330 GGKTVEIQIRTKQMHEDAELGVAAHWKYKE 359
Cdd:pfam04607  81 EGVPVEIQIRTIAMHFWAEYGIAHHWRYKE 110
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
251-359 1.21e-55

Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species.


Pssm-ID: 214934 [Multi-domain]  Cd Length: 111  Bit Score: 185.85  E-value: 1.21e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      251 GRPKHIYSIWRKMQKKN-LAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGP 329
Cdd:smart00954   1 GRVKHLYSIYKKMRRKGeISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTVIGP 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 882678      330 GGKTVEIQIRTKQMHEDAELGVAAHWKYKE 359
Cdd:smart00954  81 EGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
TGS_RSH cd01668
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ...
407-465 1.82e-35

TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT homolog (RSH) family consists of long RSH proteins and short RSH proteins. Long RSH proteins have been characterized as containing an N-terminal region and a C-terminal region. The N-terminal region contains a pseudo-hydrolase (inactive-hydrolase) domain and a (p)ppGpp synthetase domain. The C-terminal region contains a ubiquitin-like TGS (ThrRS, GTPase and SpoT) domain, a conserved cysteine domain (CC), helical and ACT (aspartate kinase, chorismate mutase, TyrA domain) domains connected by a linker region. Short RSH proteins have a truncated C-terminal region without ACT domain. The RSH family includes two classes of enzyme: i) monofunctional (p)ppGpp synthetase I, RelA, and ii) bifunctional (p)ppGpp synthetase II/hydrolase, SpoT (also called Rel). Both classes are capable of synthesizing (p)ppGpp but only bifunctional enzymes are capable of (p)ppGpp hydrolysis. SpoT is a ribosome-associated protein that is activated during amino acid starvation and thought to mediate the stringent response. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in respond to environmental stress. RelA is an ATP:GTP(GDP) pyrophosphate transferase that is recruited to stalled ribosomes and activated to synthesize (p)ppGpp, which acts as a pleiotropic secondary messenger.


Pssm-ID: 340459 [Multi-domain]  Cd Length: 59  Bit Score: 128.03  E-value: 1.82e-35
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 882678   407 YVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIIT 465
Cdd:cd01668   1 FVFTPKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT 59
 
Name Accession Description Interval E-value
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
1-743 0e+00

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 1637.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      1 MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
Cdd:PRK10872   1 MVAVRSAHLNKAGEFDPDKWIASLGITSQQSCERLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     81 LFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHL 160
Cdd:PRK10872  81 LFPLADANVVSEDVLRESVGKSIVNLIHGVRDMDAIRQLKATHNDSVSSEQVDNVRRMLLAMVEDFRCVVIKLAERIAHL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEM 240
Cdd:PRK10872 161 REVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPDEYKRIAKLLHERRIDREHYIEEFVGHLRAEM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    241 KAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
Cdd:PRK10872 241 KAEGVKAEVYGRPKHIYSIWRKMQKKSLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    321 SIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGARSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
Cdd:PRK10872 321 SIHTVVLGPGGKTVEIQIRTRQMHEDAELGVAAHWKYKEGAAAGGGRSGHEDRIAWLRKLIAWQEEMADSGEMLDEVRSQ 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
Cdd:PRK10872 401 VFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQPNPSRDWLNPNL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFL 560
Cdd:PRK10872 481 GYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHLLPRYNFNSLDELLAAIGGGDIRLNQMVNFL 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    561 QSQFNKPSAEEQDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISVHRADCEQ 640
Cdd:PRK10872 561 QSQFNKPSAEEQDAAALKQLQQKTYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEIVGFITQGRGISIHRADCEQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    641 LAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
Cdd:PRK10872 641 LAELRSHAPERIVDAVWGESYSSGYSLVVRVTANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQ 720
                        730       740
                 ....*....|....*....|...
gi 882678    721 VLGRVLGKLNQVPDVIDARRLHG 743
Cdd:PRK10872 721 VLGRVLGKLNQVPDVIDARRLHG 743
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
59-743 0e+00

(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 998.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    59 GVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQlkathtDSVSSEQVDNVRRM 138
Cdd:COG0317  58 PLAVAEILAELGLDAETIAAALLHDVVEDTDVTLEEIEEEFGEEVAELVDGVTKLSKIEF------GSKEEAQAENFRKM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   139 LLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLL 218
Cdd:COG0317 132 LLAMAKDIRVILIKLADRLHNMRTLKAMPPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKLL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   219 HERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHT 298
Cdd:COG0317 212 KEKRGEREEYIEEIIEELKEELAEAGIKAEVSGRPKHIYSIYRKMQRKGLSFEEIYDLYAFRIIVDTVDDCYAALGIVHS 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   299 HYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGGarSGHEDRIAWLR 378
Cdd:COG0317 292 LWKPIPGRFKDYIAIPKPNGYQSLHTTVIGPDGKPVEVQIRTEEMHEIAEYGVAAHWKYKEGGGSGD--SSYDEKIAWLR 369
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   379 KLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMG 458
Cdd:COG0317 370 QLLEWQEEAGDSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAYAIHTEVGHRCVGAKVNGRLVPLSTPLKNG 449
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   459 DQIEIITQKQPNPSRDWLNpnlgYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAE-KHLLPRYNFN 537
Cdd:COG0317 450 DTVEIITSKNAGPSRDWLN----FVKTSRARSKIRQWFKKQRREENIELGRELLEKELKRLGLTLDDENlEKLAKKLGFK 525
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   538 DVDELLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAAALKqlqqksytPQNRSKDNGRVVVEGVGNLMHHIARCCQPIP 617
Cdd:COG0317 526 SLDDLLAAIGLGEISLRQVVNRLLPELEKEEPEEEDEELLK--------KSKKKKSDSGVLIDGVDGLLVKLAKCCNPIP 597
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   618 GDEIVGFITQGRGISVHRADCEQLAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGV 697
Cdd:COG0317 598 GDPIVGFVTRGRGVSVHRKDCPNLAELREREPERLIDVEWGEDSSGVFPVDIRIEALDRPGLLADITSVIAEEKINILSV 677
                       650       660       670       680
                ....*....|....*....|....*....|....*....|....*.
gi 882678   698 ASRSDtKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARRLHG 743
Cdd:COG0317 678 NTRSR-DDGTATIRFTVEVRDLDHLARVLRKLRKVPGVISVRRVRG 722
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
65-740 0e+00

(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. RelA (EC 2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC 3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 213552 [Multi-domain]  Cd Length: 683  Bit Score: 593.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      65 ILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIrqlkatHTDSVSSEQVDNVRRMLLAMVD 144
Cdd:TIGR00691  30 ILAELGMDEETVCAALLHDVIEDTPVTEEEIEEEFGEEVAELVDGVTKITKL------KKKSRQELQAENFRKMILAMAQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     145 DFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLD 224
Cdd:TIGR00691 104 DIRVIVIKLADRLHNMRTLDFLPPEKQKRIAKETLEIYAPLAHRLGMSSIKTELEDLSFKYLYPKEYENIKSLVNEQKVN 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     225 REHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLP 304
Cdd:TIGR00691 184 RENKLEKFKSELEKRLEDSGIEAELEGRSKHLYSIYQKMTRKGQNFDEIHDLLAIRIIVKSELDCYRVLGIIHLLFKPIP 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     305 DEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEGAAAGgarSGHEDRIAWLRKLIAWQ 384
Cdd:TIGR00691 264 GRFKDYIASPKENGYQSLHTTVRGPKGLPVEIQIRTEDMDRVAEYGIAAHWIYKEGNPQK---EALIDDMRWLNYLVEWQ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     385 EEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEII 464
Cdd:TIGR00691 341 QESANFFEFIENLKSDLFNEEIYVFTPKGDVVELPSGSTPVDFAYAVHTDVGNKCTGAKVNGKIVPLDKELENGDVVEII 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     465 TQKQPNPSRDWLNpnlgYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDELEHLGISLKEAEKHL---LPRYNFNDVDE 541
Cdd:TIGR00691 421 TGKNSNPSVIWLN----FVVTSKARNKIRQWLKKLRREVAISEGKNILEKELGRSGLKLEDLTQYIqkrLNRLRFKKLSE 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     542 LLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAaalkqlqqKSYTPQNRSKDNGRVVVEGVGNLMHHIARCCQPIPGDEI 621
Cdd:TIGR00691 497 LLAEIGKGNFSSKEVAKLLAQNNSKWQALTKPL--------KFAFSPKVFENSSFESIEGIEITKIVIAKCCSPIPGDPI 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     622 VGFITQGRGISVHRADCeqlAELRSHAPERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRS 701
Cdd:TIGR00691 569 IGIVTKGKGLSVHHKDC---KNLKNYKQEKIIEVEWNASKPRRFIVDINIEAVDRKGVLSDLTTAISENDSNIVSISTKT 645
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 882678     702 DTKqQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARR 740
Cdd:TIGR00691 646 YGK-REAILNITVEIKNYKHLLKIMLKIKTKNDVIVVKR 683
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
60-740 7.78e-136

bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 417.21  E-value: 7.78e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     60 VEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVR--DMAAIRQLKAThtdsvsseQVDNVRR 137
Cdd:PRK11092  50 VAVACILAEMRLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSklDKLKFRDKKEA--------QAENFRK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    138 MLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKL 217
Cdd:PRK11092 122 MIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    218 LHERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVH 297
Cdd:PRK11092 202 VKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVDDSDTCYRVLGQMH 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    298 THYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKTVEIQIRTKQMHEDAELGVAAHWKYKEgaaagGARSGHEDRI--- 374
Cdd:PRK11092 282 SLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKE-----HGETGTTAQIraq 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    375 AWLRKLIAWQEEMADSGEMLDEVRSQVFDDRVYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQ 454
Cdd:PRK11092 357 RWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQP 436
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    455 LQMGDQIEIITQKQPNPSRDWLNpnlgYVTTSRGRSKIHAWFRKQDRDKNILAGRQILDDEL-EHLGISLKEAE--KHLL 531
Cdd:PRK11092 437 LTSGQTVEIITAPGARPNAAWLN----FVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALgGSRKLDEIPQEniQREL 512
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    532 PRYNFNDVDELLAAIGGGdirlNQMvnflqsqfnkpsaeeqDAAALKQLQQKSYTPQNRSKDNGRVVVEGVGNLMHHIAR 611
Cdd:PRK11092 513 DRMKLATLDDLLAEIGLG----NAM----------------SVVVAKNLLGDDAELPTATSSHGKLPIKGADGVLITFAK 572
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678    612 CCQPIPGDEIVGFITQGRGISVHRADCeqlAELRSHA--PERIVDAVWGESYSAGYSLVVRVVANDRSGLLRDITTILAN 689
Cdd:PRK11092 573 CCRPIPGDPIIAHVSPGKGLVIHHESC---RNIRGYQkePEKFMAVEWDKETEQEFIAEIKVEMFNHQGALANLTAAINT 649
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|..
gi 882678    690 EKVNVLGVASRS-DTKQQLATIDMTIEiyNLQVLGRVLGKLNQVPDVIDARR 740
Cdd:PRK11092 650 TGSNIQSLNTEEkDGRVYSAFIRLTAR--DRVHLANIMRKIRVMPDVIKVTR 699
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
251-359 1.55e-58

Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and SpoT of Escherichia coli, and their homologs in plants and in other eubacteria. RelA is a guanosine 3',5'-bis-pyrophosphate (ppGpp) synthetase (EC:2.7.6.5) while SpoT is thought to be a bifunctional enzyme catalysing both ppGpp synthesis and degradation (ppGpp 3'-pyrophosphohydrolase, (EC:3.1.7.2)). This region is often found in association with HD (pfam01966), a metal-dependent phosphohydrolase, TGS (pfam02824) which is a possible nucleotide-binding region, and the ACT regulatory domain (pfam01842).


Pssm-ID: 428031 [Multi-domain]  Cd Length: 113  Bit Score: 193.53  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     251 GRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVL-GP 329
Cdd:pfam04607   1 GRVKSPYSIYEKMQRKGLLFEEIYDLIGIRIIVQFVDDCYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRSLHTTVIiGP 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 882678     330 GGKTVEIQIRTKQMHEDAELGVAAHWKYKE 359
Cdd:pfam04607  81 EGVPVEIQIRTIAMHFWAEYGIAHHWRYKE 110
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
251-359 1.21e-55

Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ somewhat. RelA produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homolog to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation. (p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species.


Pssm-ID: 214934 [Multi-domain]  Cd Length: 111  Bit Score: 185.85  E-value: 1.21e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      251 GRPKHIYSIWRKMQKKN-LAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGP 329
Cdd:smart00954   1 GRVKHLYSIYKKMRRKGeISFDEITDLAGVRIIVDFVDDCYRVLGILHSLFDPIPGRFKDYIANPKPNGYRSLHTTVIGP 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 882678      330 GGKTVEIQIRTKQMHEDAELGVAAHWKYKE 359
Cdd:smart00954  81 EGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
HD_4 pfam13328
HD domain; HD domains are metal dependent phosphohydrolases.
39-192 3.80e-44

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433119 [Multi-domain]  Cd Length: 157  Bit Score: 155.89  E-value: 3.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678      39 WAYCLQQTQGH--PDASLLLWRGVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAI 116
Cdd:pfam13328   2 LALAAPLHAGQrkGTGEPYLSHALGVAAILAELGLDADTVIAALLHDVVEDTGGSLEEIEERFGDEVARLVEGVSRLDRI 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 882678     117 RQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIG 192
Cdd:pfam13328  82 QKLAARDWAERKAAQAENLRKMLLAMVEDIRVVLVKLADRLQTLRSLAAAPPEKQRAIARETLDIYAPLANRLGIW 157
TGS_RSH cd01668
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ...
407-465 1.82e-35

TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT homolog (RSH) family consists of long RSH proteins and short RSH proteins. Long RSH proteins have been characterized as containing an N-terminal region and a C-terminal region. The N-terminal region contains a pseudo-hydrolase (inactive-hydrolase) domain and a (p)ppGpp synthetase domain. The C-terminal region contains a ubiquitin-like TGS (ThrRS, GTPase and SpoT) domain, a conserved cysteine domain (CC), helical and ACT (aspartate kinase, chorismate mutase, TyrA domain) domains connected by a linker region. Short RSH proteins have a truncated C-terminal region without ACT domain. The RSH family includes two classes of enzyme: i) monofunctional (p)ppGpp synthetase I, RelA, and ii) bifunctional (p)ppGpp synthetase II/hydrolase, SpoT (also called Rel). Both classes are capable of synthesizing (p)ppGpp but only bifunctional enzymes are capable of (p)ppGpp hydrolysis. SpoT is a ribosome-associated protein that is activated during amino acid starvation and thought to mediate the stringent response. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in respond to environmental stress. RelA is an ATP:GTP(GDP) pyrophosphate transferase that is recruited to stalled ribosomes and activated to synthesize (p)ppGpp, which acts as a pleiotropic secondary messenger.


Pssm-ID: 340459 [Multi-domain]  Cd Length: 59  Bit Score: 128.03  E-value: 1.82e-35
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 882678   407 YVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIIT 465
Cdd:cd01668   1 FVFTPKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT 59
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
227-349 6.71e-34

Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; This family includes the catalytic domains of Escherichia coli ppGpp synthetase (RelA), ppGpp synthetase/hydrolase (SpoT), and related proteins. RelA synthesizes (p)ppGpp in response to amino-acid starvation and in association with ribosomes. (p)ppGpp triggers the bacterial stringent response. SpoT catalyzes (p)ppGpp synthesis under carbon limitation in a ribosome-independent manner. It also catalyzes (p)ppGpp degradation. Gram-negative bacteria have two enzymes involved in (p)ppGpp metabolism while most Gram-positive organisms have a single Rel-Spo enzyme (Rel), which both synthesizes and degrades (p)ppGpp. The Arabidopsis thaliana Rel-Spo proteins, At-RSH1,-2, and-3 appear to regulate a rapid (p)ppGpp-mediated response to pathogens and other stresses. This catalytic domain is found in association with an N-terminal HD domain and a C-terminal metal dependent phosphohydrolase domain (TGS). Some Rel-Spo proteins also have a C-terminal regulatory ACT domain. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition.Two of the three catalytic carboxylates are found in Rel-Spo enzymes, with the second carboxylate of the DXD motif missing. Evidence supports a single-cation synthetase mechanism.


Pssm-ID: 143389 [Multi-domain]  Cd Length: 129  Bit Score: 125.92  E-value: 6.71e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   227 HYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKN---LAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHL 303
Cdd:cd05399   1 KAALEEIADLLRDAGIIGRVASVSGRVKSPYSIYEKLRRKGkdlPILDEITDLVGVRVVLLFVDDCYRVLDLLHSLFKVI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 882678   304 PDEFDDYVANPKPNGYQSIHTVVLGPG---GKTVEIQIRTKQMHEDAEL 349
Cdd:cd05399  81 PGRVKDYIAEPKENGYQSLHLVVRGPEdkaGVLIEIQIRTILMHAWAEL 129
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
406-465 3.51e-23

TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 92.99  E-value: 3.51e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     406 VYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIIT 465
Cdd:pfam02824   1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
669-740 4.91e-23

ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153148 [Multi-domain]  Cd Length: 71  Bit Score: 92.90  E-value: 4.91e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882678   669 VRVVANDRSGLLRDITTILANEKVNVLGVASRSDtKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARR 740
Cdd:cd04876   1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTD-DDGLATIRLTLEVRDLEHLARIMRKLRQIPGVIDVRR 71
ACT_4 pfam13291
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ...
665-740 4.03e-18

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.


Pssm-ID: 463831 [Multi-domain]  Cd Length: 79  Bit Score: 79.14  E-value: 4.03e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 882678     665 YSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARR 740
Cdd:pfam13291   4 YPVDLEVEAIDRPGLLADITQVISEEKANIVSVNAKTRKKDGTAEIKITLEVKDVEHLERLMAKLRRIPGVIDVER 79
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
212-344 1.50e-14

ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441924 [Multi-domain]  Cd Length: 286  Bit Score: 74.81  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   212 KRIAKLLHERRLDREHYIEEFVGHLRAEMKAEGVKAE-----VYGRPKHIYSIWRKMQKKNL------AFDELFDVRAVR 280
Cdd:COG2357   9 REFLADYERFLPPYEAALEELKTKLEILLDEFEKHGGspiehVTSRVKSPESIIEKLRRKGLpltyenILEEITDIAGIR 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882678   281 IVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVV-------LGPGGKTVEIQIRTKQMH 344
Cdd:COG2357  89 IICYFVDDIYRVAELLRSQFDVKIIEEKDYIKNPKPNGYRSLHLIVrvpvflsDGPKGVPVEIQIRTIAMD 159
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
408-464 3.83e-12

TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; This family includes eukaryotic and some bacterial threonyl-tRNA synthetases (ThrRSs), a distinct Obg family GTPases, and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, as well as uridine kinase (UDK) from Thermotogales. All family members contain a TGS domain named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. It is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions. The functions of the TGS domain remains unclear, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, with a regulatory role.


Pssm-ID: 340455 [Multi-domain]  Cd Length: 61  Bit Score: 61.85  E-value: 3.83e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678   408 VFTPK---GDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEII 464
Cdd:cd01616   2 VFTVGktpGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKFL 61
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
668-734 2.34e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 48.46  E-value: 2.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 882678     668 VVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKQqlATIDMTIEIYNLQVLGRVLGKLNQVPD 734
Cdd:pfam01842   2 VLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDK--GGIVFVVIVVDEEDLEEVLEALKKLEG 66
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
414-465 3.51e-07

TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized GTP-binding protein MJ1332 and similar proteins; This family includes a group of uncharacterized GTP-binding proteins from archaea, which belong to the Obg family of GTPases. The family members contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as a C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold.


Pssm-ID: 340460 [Multi-domain]  Cd Length: 78  Bit Score: 48.08  E-value: 3.51e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 882678   414 DVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIG--GRIVPFTYQLQMGDQIEIIT 465
Cdd:cd01669  25 DAILLKRGSTPRDLAYKIHTDLGKGFLYAIDArtKMRLGEDYELKHGDVVKIVS 78
RelA_AH_RIS pfam19296
RelA/SpoT, AH and RIS domains; This entry represents the alpha helical (AH) and ...
508-651 4.85e-07

RelA/SpoT, AH and RIS domains; This entry represents the alpha helical (AH) and Ribosome-InterSubunit (RIS) domains found in RelA/SpoT proteins, adjacent to the ACT domain. AH domain interacts with A/R tRNA and links the very C-terminal subdomains with TGS domain. The RIS domain is part of the binding interface between the C-terminal region and the ribosome, bridging the large and the small ribosomal subunits. RIS contains a four-stranded beta-sheet and a short alpha-helix. RelA/SpoT-homolog proteins (RHS) mediate the stringent response in bacteria which enables its metabolic adaptation under stress conditions. These enzymes synthesize the second messenger (p)ppGpp, which is a regulatory metabolite of the stringent response characterized by growth arrest and the modulation of gene expression in response to various nutritional stresses.


Pssm-ID: 437128 [Multi-domain]  Cd Length: 185  Bit Score: 50.63  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     508 GRQILDDELEHLGISLKEAE-KHLLPRYNFNDVDELLAAIGGGDIRLNQMVNFLQSQFNKPSAEEQDAAA-------LKQ 579
Cdd:pfam19296  29 GRQILERAFERAGKEFSDEElKPALPRLGRKDVEDLLAAVGRGEISSEDVLRAVYPDYQDERATKLPPVAdeegwfnLRK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882678     580 LQQ-KSYTPQNRSKDNGRVV----VEGV-GNLMHHIArccqP---IPGDEIVGFITQGRGISVHRADCEQLAELRSHaPE 650
Cdd:pfam19296 109 AAGmKFRVPGGQRSGPAKAKaaipIRGLdGDLPVRFA----PegaVPGDRIVGILTPGEGITIYPIQSPALQAFDDE-PE 183

                  .
gi 882678     651 R 651
Cdd:pfam19296 184 R 184
PRK09602 PRK09602
translation-associated GTPase; Reviewed
414-465 7.63e-07

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 52.12  E-value: 7.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 882678    414 DVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIG--GRIVPFTYQLQMGDQIEIIT 465
Cdd:PRK09602 341 DAFLLPKGSTARDLAYKIHTDIGEGFLYAIDArtKRRIGEDYELKDGDVIKIVS 394
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
669-729 2.69e-06

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 44.98  E-value: 2.69e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882678   669 VRVVANDRSGLLRDITTILANEKVNVLGVASRSDTKqqLATIDMTIEIYNLQVLGRVLGKL 729
Cdd:cd02116   1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGD--GGEADIFIVVDGDGDLEKLLEAL 59
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
662-716 5.47e-04

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 41.36  E-value: 5.47e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 882678   662 SAGYSLVVRVVANDRSGLLRDITTILANEKVNVLGVASRS----DTKQQLATIDMTIEI 716
Cdd:COG2716  86 PAGLPYVVEVVGNDRPGIVAEVTQFLAERGINIEDLSTKTypapMSGTPLFSAQITVHV 144
TGS_ThrRS cd01667
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ...
411-469 7.82e-04

TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar proteins; ThrRS, also termed cytoplasmic threonine--tRNA ligase, is a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and SpoT/RelA proteins where it occurs. TGS is a small domain with a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340458 [Multi-domain]  Cd Length: 65  Bit Score: 38.24  E-value: 7.82e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 882678   411 PKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQKQP 469
Cdd:cd01667   6 PDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILTFDDP 64
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
671-741 1.62e-03

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 37.44  E-value: 1.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882678   671 VVANDRSGLLRDITTILANEKVNVLGVASRSDTKQQLATidMTIEIyNLQVLGRVLGKLNQVPDVIDARRL 741
Cdd:cd04879   4 IVHKDVPGVIGKVGTILGEHGINIAAMQVGRKEKGGIAY--MVLDV-DSPVPEEVLEELKALPGIIRVRLI 71
ACT_GcvR_2 cd04869
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ...
668-716 2.23e-03

ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains; This CD includes the second of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. The glycine cleavage enzyme system in Escherichia coli provides one-carbon units for cellular methylation reactions. This enzyme system, encoded by the gcvTHP operon and lpd gene, catalyzes the cleavage of glycine into CO2 + NH3 and transfers a one-carbon unit to tetrahydrofolate, producing 5,10-methylenetetrahydrofolate. The gcvTHP operon is activated by the GcvA protein in response to glycine and repressed by a GcvA/GcvR interaction in the absence of glycine. It has been proposed that the co-activator glycine acts through a mechanism of de-repression by binding to GcvR and preventing GcvR from interacting with GcvA to block GcvA's activator function. Evidence also suggests that GcvR interacts directly with GcvA rather than binding to DNA to cause repression. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153141 [Multi-domain]  Cd Length: 81  Bit Score: 37.59  E-value: 2.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 882678   668 VVRVVANDRSGLLRDITTILANEKVNVLGVASRSDTK----QQLATIDMTIEI 716
Cdd:cd04869   1 VVEVVGNDRPGIVHEVTQFLAQRNINIEDLSTETYSApmsgTPLFKAQATLAL 53
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
404-465 3.09e-03

TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein (DRG) family; DRG-1 and DRG-2 comprise a highly conserved DRG subfamily of GTP-binding proteins found in archaea, plants, fungi and animals. The exact function of DRG proteins is unknown, although phylogenetic and biochemical fraction studies have linked them to translation, differentiation and growth. Their abnormal expressions may trigger cell transformation or cell cycle arrest. DRG-1 and DRG-2 bind to DFRP1 (DRG family regulatory protein 1) and DFRP2, respectively. Both DRG-1 and DRG-2 contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as the C-terminal TGS (ThrRS, GTPase and SpoT) domain, which has a predominantly beta-grasp ubiquitin-like fold and may be related to RNA binding. DRG subfamily belongs to the Obg family of GTPases.


Pssm-ID: 340457 [Multi-domain]  Cd Length: 77  Bit Score: 36.83  E-value: 3.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 882678   404 DRVYVFT-PKGDVVD------LPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPF-------TYQLQMGDQIEIIT 465
Cdd:cd01666   2 GIIRVYTkPPGKKPDfdepfiLRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFdgqrvglDHVLEDGDIVEIHK 77
 
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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