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Conserved domains on  [gi|7141304|gb|AAF37281|]
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RSH1 [Arabidopsis thaliana]

Protein Classification

RelA/SpoT family protein( domain architecture ID 11416884)

RelA/SpoT family protein is involved in guanosine tetraphosphate metabolic process, such as GTP pyrophosphokinase that catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp; contains HD, nucleotidyltransferase (NT), TGS, alpha helical (AH), Ribosome-InterSubunit (RIS) and ACT domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
127-863 0e+00

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


:

Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 587.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  127 TVETLWEDLFPSI-SYLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDT 205
Cdd:COG0317   8 AIEARLEELLERLkAYLPPADIALIRRAYEFAEEAHEGQKRKSGEPYITHPLAVAEILAELGLDAETIAAALLHDVVEDT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  206 NfITFEKIEEEFGATVRHIVEGetkVSKLGKLKCKTESEtiqdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHM 285
Cdd:COG0317  88 D-VTLEEIEEEFGEEVAELVDG---VTKLSKIEFGSKEE----AQAENFRKMLLAMAKDIRVILIKLADRLHNMRTLKAM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  286 PPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQfl 365
Cdd:COG0317 160 PPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKLLKEKRGEREEYIEEIIEELKEELAEAG-- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  366 dlvtVNTDVRSVCKETYSIYKAALKSKGSIND-YNQIAqLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTV 444
Cdd:COG0317 238 ----IKAEVSGRPKHIYSIYRKMQRKGLSFEEiYDLYA-FRIIVDTVDD------------CYAALGIVHSLWKPIPGRF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  445 KDYIATPKPNGYQSLHTTVI-PflyESMfRLEVQIRTEEMDLIAERGIA---VYYNGKSLStglvgnavplgrnsrgktg 520
Cdd:COG0317 301 KDYIAIPKPNGYQSLHTTVIgP---DGK-PVEVQIRTEEMHEIAEYGVAahwKYKEGGGSG------------------- 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  521 clnNADFALRVGWLNAIREWQEEFVgnmSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMV 600
Cdd:COG0317 358 ---DSSYDEKIAWLRQLLEWQEEAG---DSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAYAIHTEVGHRCV 431
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  601 AAKVNGNLVSPTHVLENAEVVEIVTynalSSKSAFQRhkQWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDF--- 677
Cdd:COG0317 432 GAKVNGRLVPLSTPLKNGDTVEIIT----SKNAGPSR--DWLNFVKTSRARSKIRQWFKKQRREENIELGRELLEKElkr 505
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  678 --VADSDSDVEDLTEDSR-KSLqwwEKILVNV-----------KQFqsQDKSRDTTPAPQNGSVWAPKVNGKHNKAIKNS 743
Cdd:COG0317 506 lgLTLDDENLEKLAKKLGfKSL---DDLLAAIglgeislrqvvNRL--LPELEKEEPEEEDEELLKKSKKKKSDSGVLID 580
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  744 SSDEPEFLL-------PGDGIA------------RILPANIPAYKEVLPglDSWRDskiATWH-HLEGQSIEWLCVVSMD 803
Cdd:COG0317 581 GVDGLLVKLakccnpiPGDPIVgfvtrgrgvsvhRKDCPNLAELREREP--ERLID---VEWGeDSSGVFPVDIRIEALD 655
                       730       740       750       760       770       780
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7141304  804 RKGIIAEVTTVLAAEGIALCScVAEIDRGRGLAVMLFQIE-ANIESLVSVCAKVDLVLGVL 863
Cdd:COG0317 656 RPGLLADITSVIAEEKINILS-VNTRSRDDGTATIRFTVEvRDLDHLARVLRKLRKVPGVI 715
 
Name Accession Description Interval E-value
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
127-863 0e+00

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 587.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  127 TVETLWEDLFPSI-SYLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDT 205
Cdd:COG0317   8 AIEARLEELLERLkAYLPPADIALIRRAYEFAEEAHEGQKRKSGEPYITHPLAVAEILAELGLDAETIAAALLHDVVEDT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  206 NfITFEKIEEEFGATVRHIVEGetkVSKLGKLKCKTESEtiqdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHM 285
Cdd:COG0317  88 D-VTLEEIEEEFGEEVAELVDG---VTKLSKIEFGSKEE----AQAENFRKMLLAMAKDIRVILIKLADRLHNMRTLKAM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  286 PPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQfl 365
Cdd:COG0317 160 PPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKLLKEKRGEREEYIEEIIEELKEELAEAG-- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  366 dlvtVNTDVRSVCKETYSIYKAALKSKGSIND-YNQIAqLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTV 444
Cdd:COG0317 238 ----IKAEVSGRPKHIYSIYRKMQRKGLSFEEiYDLYA-FRIIVDTVDD------------CYAALGIVHSLWKPIPGRF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  445 KDYIATPKPNGYQSLHTTVI-PflyESMfRLEVQIRTEEMDLIAERGIA---VYYNGKSLStglvgnavplgrnsrgktg 520
Cdd:COG0317 301 KDYIAIPKPNGYQSLHTTVIgP---DGK-PVEVQIRTEEMHEIAEYGVAahwKYKEGGGSG------------------- 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  521 clnNADFALRVGWLNAIREWQEEFVgnmSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMV 600
Cdd:COG0317 358 ---DSSYDEKIAWLRQLLEWQEEAG---DSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAYAIHTEVGHRCV 431
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  601 AAKVNGNLVSPTHVLENAEVVEIVTynalSSKSAFQRhkQWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDF--- 677
Cdd:COG0317 432 GAKVNGRLVPLSTPLKNGDTVEIIT----SKNAGPSR--DWLNFVKTSRARSKIRQWFKKQRREENIELGRELLEKElkr 505
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  678 --VADSDSDVEDLTEDSR-KSLqwwEKILVNV-----------KQFqsQDKSRDTTPAPQNGSVWAPKVNGKHNKAIKNS 743
Cdd:COG0317 506 lgLTLDDENLEKLAKKLGfKSL---DDLLAAIglgeislrqvvNRL--LPELEKEEPEEEDEELLKKSKKKKSDSGVLID 580
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  744 SSDEPEFLL-------PGDGIA------------RILPANIPAYKEVLPglDSWRDskiATWH-HLEGQSIEWLCVVSMD 803
Cdd:COG0317 581 GVDGLLVKLakccnpiPGDPIVgfvtrgrgvsvhRKDCPNLAELREREP--ERLID---VEWGeDSSGVFPVDIRIEALD 655
                       730       740       750       760       770       780
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7141304  804 RKGIIAEVTTVLAAEGIALCScVAEIDRGRGLAVMLFQIE-ANIESLVSVCAKVDLVLGVL 863
Cdd:COG0317 656 RPGLLADITSVIAEEKINILS-VNTRSRDDGTATIRFTVEvRDLDHLARVLRKLRKVPGVI 715
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
154-865 8.83e-147

(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: 449.53  E-value: 8.83e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    154 LKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfITFEKIEEEFGATVRHIVEGetkVSK 233
Cdd:TIGR00691   2 LEIAKDLHEGQKRKSGEPYIIHPLAVALILAELGMDEETVCAALLHDVIEDTP-VTEEEIEEEFGEEVAELVDG---VTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    234 LGKLKCKTESEtiqdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGMYSI 313
Cdd:TIGR00691  78 ITKLKKKSRQE----LQAENFRKMILAMAQDIRVIVIKLADRLHNMRTLDFLPPEKQKRIAKETLEIYAPLAHRLGMSSI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    314 KSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQFLDLVTvntdVRSvcKETYSIYKaALKSKG 393
Cdd:TIGR00691 154 KTELEDLSFKYLYPKEYENIKSLVNEQKVNRENKLEKFKSELEKRLEDSGIEAELE----GRS--KHLYSIYQ-KMTRKG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    394 S-INDYNQIAQLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQSLHTTVIpfLYESMF 472
Cdd:TIGR00691 227 QnFDEIHDLLAIRIIVKSELD------------CYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHTTVR--GPKGLP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    473 rLEVQIRTEEMDLIAERGIAVYYNGKSLSTGLVGNAvplgrnsrgktgclnnADFAlrvgWLNAIREWQEEfVGNMSsrE 552
Cdd:TIGR00691 293 -VEIQIRTEDMDRVAEYGIAAHWIYKEGNPQKEALI----------------DDMR----WLNYLVEWQQE-SANFF--E 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    553 FVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSK 632
Cdd:TIGR00691 349 FIENLKSDLFNEEIYVFTPKGDVVELPSGSTPVDFAYAVHTDVGNKCTGAKVNGKIVPLDKELENGDVVEIITGKNSNPS 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    633 SAfqrhkqWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDFVADSDSDVEDLTEDSRKSLqwwekilvNVKQFQSQ 712
Cdd:TIGR00691 429 VI------WLNFVVTSKARNKIRQWLKKLRREVAISEGKNILEKELGRSGLKLEDLTQYIQKRL--------NRLRFKKL 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    713 DksrDTTPAPQNGSVWAPKV-------NGKHNKAIKNSSSDEPEFLLPGDGIARILPANI----------PAYKEVLPGL 775
Cdd:TIGR00691 495 S---ELLAEIGKGNFSSKEVakllaqnNSKWQALTKPLKFAFSPKVFENSSFESIEGIEItkiviakccsPIPGDPIIGI 571
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    776 DSwrDSKIATWHH-----LEGQ------SIEW-----------LCVVSMDRKGIIAEVTTVLAAEGIALCSCVAEIdRGR 833
Cdd:TIGR00691 572 VT--KGKGLSVHHkdcknLKNYkqekiiEVEWnaskprrfivdINIEAVDRKGVLSDLTTAISENDSNIVSISTKT-YGK 648
                         730       740       750
                  ....*....|....*....|....*....|...
gi 7141304    834 GLAVMLFQIE-ANIESLVSVCAKVDLVLGVLGW 865
Cdd:TIGR00691 649 REAILNITVEiKNYKHLLKIMLKIKTKNDVIVV 681
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
131-659 3.02e-113

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


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 362.13  E-value: 3.02e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   131 LWEDLFPSIS-YLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfIT 209
Cdd:PRK11092   3 LFESLNQLIQtYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMRLDYETLMAALLHDVIEDTP-AT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   210 FEKIEEEFGATVRHIVEGetkVSKLGKLKCKTESETiqdvKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHK 289
Cdd:PRK11092  82 YQDMEQLFGKSVAELVEG---VSKLDKLKFRDKKEA----QAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   290 QSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYdRVTSRIANLYKEHEKELTeaNRILVkkiEDDQFLDLVT 369
Cdd:PRK11092 155 RRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRY-RVIKEVVKAARGNRKEMI--QKILS---EIEGRLQEAG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   370 VNTDVRSVCKETYSIY-KAALKSK--GSINDynqIAQLRIVVKPKpsvgvgplcspqQICYHVLGLVHEIWKPIPRTVKD 446
Cdd:PRK11092 229 IPCRVSGREKHLYSIYcKMVLKEQrfHSIMD---IYAFRVIVDDS------------DTCYRVLGQMHSLYKPRPGRVKD 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   447 YIATPKPNGYQSLHTTVI-----PflyesmfrLEVQIRTEEMDLIAERGIAVYY----NGKSLSTGLVgnavplgRNSRg 517
Cdd:PRK11092 294 YIAIPKANGYQSLHTSMIgphgvP--------VEVQIRTEDMDQMAEMGVAAHWaykeHGETGTTAQI-------RAQR- 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   518 ktgclnnadfalrvgWLNAIREWQEEfvgNMSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGN 597
Cdd:PRK11092 358 ---------------WMQSLLELQQS---AGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGH 419
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7141304   598 KMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSKSAfqrhkqWLQHAKTRSARHKIMRFLR 659
Cdd:PRK11092 420 ACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAA------WLNFVVSSKARAKIRQLLK 475
HD_4 pfam13328
HD domain; HD domains are metal dependent phosphohydrolases.
154-310 5.22e-47

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433119 [Multi-domain]  Cd Length: 157  Bit Score: 164.74  E-value: 5.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    154 LKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfITFEKIEEEFGATVRHIVEGETKVSK 233
Cdd:pfam13328   2 LALAAPLHAGQRKGTGEPYLSHALGVAAILAELGLDADTVIAALLHDVVEDTG-GSLEEIEERFGDEVARLVEGVSRLDR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7141304    234 LGKLKCKTESETIQdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGM 310
Cdd:pfam13328  81 IQKLAARDWAERKA-AQAENLRKMLLAMVEDIRVVLVKLADRLQTLRSLAAAPPEKQRAIARETLDIYAPLANRLGI 156
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
379-499 4.47e-34

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: 126.14  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304     379 KETYSIY-KAALKSKGSINDYNQIAQLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQ 457
Cdd:smart00954   4 KHLYSIYkKMRRKGEISFDEITDLAGVRIIVDFVDD------------CYRVLGILHSLFDPIPGRFKDYIANPKPNGYR 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 7141304     458 SLHTTVIpflYESMFRLEVQIRTEEMDLIAERGIAVYYNGKS 499
Cdd:smart00954  72 SLHTTVI---GPEGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
TGS_RSH cd01668
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ...
567-625 2.65e-33

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: 122.25  E-value: 2.65e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7141304  567 FVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVT 625
Cdd:cd01668   1 FVFTPKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT 59
 
Name Accession Description Interval E-value
SpoT COG0317
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
127-863 0e+00

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


Pssm-ID: 440086 [Multi-domain]  Cd Length: 722  Bit Score: 587.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  127 TVETLWEDLFPSI-SYLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDT 205
Cdd:COG0317   8 AIEARLEELLERLkAYLPPADIALIRRAYEFAEEAHEGQKRKSGEPYITHPLAVAEILAELGLDAETIAAALLHDVVEDT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  206 NfITFEKIEEEFGATVRHIVEGetkVSKLGKLKCKTESEtiqdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHM 285
Cdd:COG0317  88 D-VTLEEIEEEFGEEVAELVDG---VTKLSKIEFGSKEE----AQAENFRKMLLAMAKDIRVILIKLADRLHNMRTLKAM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  286 PPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQfl 365
Cdd:COG0317 160 PPEKQRRIARETLEIYAPLAHRLGINQIKWELEDLSFRYLEPERYKEIAKLLKEKRGEREEYIEEIIEELKEELAEAG-- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  366 dlvtVNTDVRSVCKETYSIYKAALKSKGSIND-YNQIAqLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTV 444
Cdd:COG0317 238 ----IKAEVSGRPKHIYSIYRKMQRKGLSFEEiYDLYA-FRIIVDTVDD------------CYAALGIVHSLWKPIPGRF 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  445 KDYIATPKPNGYQSLHTTVI-PflyESMfRLEVQIRTEEMDLIAERGIA---VYYNGKSLStglvgnavplgrnsrgktg 520
Cdd:COG0317 301 KDYIAIPKPNGYQSLHTTVIgP---DGK-PVEVQIRTEEMHEIAEYGVAahwKYKEGGGSG------------------- 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  521 clnNADFALRVGWLNAIREWQEEFVgnmSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMV 600
Cdd:COG0317 358 ---DSSYDEKIAWLRQLLEWQEEAG---DSGEFLESLKLDLFPDEVYVFTPKGDVIELPRGATPLDFAYAIHTEVGHRCV 431
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  601 AAKVNGNLVSPTHVLENAEVVEIVTynalSSKSAFQRhkQWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDF--- 677
Cdd:COG0317 432 GAKVNGRLVPLSTPLKNGDTVEIIT----SKNAGPSR--DWLNFVKTSRARSKIRQWFKKQRREENIELGRELLEKElkr 505
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  678 --VADSDSDVEDLTEDSR-KSLqwwEKILVNV-----------KQFqsQDKSRDTTPAPQNGSVWAPKVNGKHNKAIKNS 743
Cdd:COG0317 506 lgLTLDDENLEKLAKKLGfKSL---DDLLAAIglgeislrqvvNRL--LPELEKEEPEEEDEELLKKSKKKKSDSGVLID 580
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  744 SSDEPEFLL-------PGDGIA------------RILPANIPAYKEVLPglDSWRDskiATWH-HLEGQSIEWLCVVSMD 803
Cdd:COG0317 581 GVDGLLVKLakccnpiPGDPIVgfvtrgrgvsvhRKDCPNLAELREREP--ERLID---VEWGeDSSGVFPVDIRIEALD 655
                       730       740       750       760       770       780
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7141304  804 RKGIIAEVTTVLAAEGIALCScVAEIDRGRGLAVMLFQIE-ANIESLVSVCAKVDLVLGVL 863
Cdd:COG0317 656 RPGLLADITSVIAEEKINILS-VNTRSRDDGTATIRFTVEvRDLDHLARVLRKLRKVPGVI 715
spoT_relA TIGR00691
(p)ppGpp synthetase, RelA/SpoT family; The functions of E. coli RelA and SpoT differ somewhat. ...
154-865 8.83e-147

(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: 449.53  E-value: 8.83e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    154 LKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfITFEKIEEEFGATVRHIVEGetkVSK 233
Cdd:TIGR00691   2 LEIAKDLHEGQKRKSGEPYIIHPLAVALILAELGMDEETVCAALLHDVIEDTP-VTEEEIEEEFGEEVAELVDG---VTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    234 LGKLKCKTESEtiqdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGMYSI 313
Cdd:TIGR00691  78 ITKLKKKSRQE----LQAENFRKMILAMAQDIRVIVIKLADRLHNMRTLDFLPPEKQKRIAKETLEIYAPLAHRLGMSSI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    314 KSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQFLDLVTvntdVRSvcKETYSIYKaALKSKG 393
Cdd:TIGR00691 154 KTELEDLSFKYLYPKEYENIKSLVNEQKVNRENKLEKFKSELEKRLEDSGIEAELE----GRS--KHLYSIYQ-KMTRKG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    394 S-INDYNQIAQLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQSLHTTVIpfLYESMF 472
Cdd:TIGR00691 227 QnFDEIHDLLAIRIIVKSELD------------CYRVLGIIHLLFKPIPGRFKDYIASPKENGYQSLHTTVR--GPKGLP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    473 rLEVQIRTEEMDLIAERGIAVYYNGKSLSTGLVGNAvplgrnsrgktgclnnADFAlrvgWLNAIREWQEEfVGNMSsrE 552
Cdd:TIGR00691 293 -VEIQIRTEDMDRVAEYGIAAHWIYKEGNPQKEALI----------------DDMR----WLNYLVEWQQE-SANFF--E 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    553 FVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSK 632
Cdd:TIGR00691 349 FIENLKSDLFNEEIYVFTPKGDVVELPSGSTPVDFAYAVHTDVGNKCTGAKVNGKIVPLDKELENGDVVEIITGKNSNPS 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    633 SAfqrhkqWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDFVADSDSDVEDLTEDSRKSLqwwekilvNVKQFQSQ 712
Cdd:TIGR00691 429 VI------WLNFVVTSKARNKIRQWLKKLRREVAISEGKNILEKELGRSGLKLEDLTQYIQKRL--------NRLRFKKL 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    713 DksrDTTPAPQNGSVWAPKV-------NGKHNKAIKNSSSDEPEFLLPGDGIARILPANI----------PAYKEVLPGL 775
Cdd:TIGR00691 495 S---ELLAEIGKGNFSSKEVakllaqnNSKWQALTKPLKFAFSPKVFENSSFESIEGIEItkiviakccsPIPGDPIIGI 571
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    776 DSwrDSKIATWHH-----LEGQ------SIEW-----------LCVVSMDRKGIIAEVTTVLAAEGIALCSCVAEIdRGR 833
Cdd:TIGR00691 572 VT--KGKGLSVHHkdcknLKNYkqekiiEVEWnaskprrfivdINIEAVDRKGVLSDLTTAISENDSNIVSISTKT-YGK 648
                         730       740       750
                  ....*....|....*....|....*....|...
gi 7141304    834 GLAVMLFQIE-ANIESLVSVCAKVDLVLGVLGW 865
Cdd:TIGR00691 649 REAILNITVEiKNYKHLLKIMLKIKTKNDVIVV 681
PRK11092 PRK11092
bifunctional GTP diphosphokinase/guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase;
131-659 3.02e-113

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


Pssm-ID: 236843 [Multi-domain]  Cd Length: 702  Bit Score: 362.13  E-value: 3.02e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   131 LWEDLFPSIS-YLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfIT 209
Cdd:PRK11092   3 LFESLNQLIQtYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMRLDYETLMAALLHDVIEDTP-AT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   210 FEKIEEEFGATVRHIVEGetkVSKLGKLKCKTESETiqdvKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHK 289
Cdd:PRK11092  82 YQDMEQLFGKSVAELVEG---VSKLDKLKFRDKKEA----QAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   290 QSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYdRVTSRIANLYKEHEKELTeaNRILVkkiEDDQFLDLVT 369
Cdd:PRK11092 155 RRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRY-RVIKEVVKAARGNRKEMI--QKILS---EIEGRLQEAG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   370 VNTDVRSVCKETYSIY-KAALKSK--GSINDynqIAQLRIVVKPKpsvgvgplcspqQICYHVLGLVHEIWKPIPRTVKD 446
Cdd:PRK11092 229 IPCRVSGREKHLYSIYcKMVLKEQrfHSIMD---IYAFRVIVDDS------------DTCYRVLGQMHSLYKPRPGRVKD 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   447 YIATPKPNGYQSLHTTVI-----PflyesmfrLEVQIRTEEMDLIAERGIAVYY----NGKSLSTGLVgnavplgRNSRg 517
Cdd:PRK11092 294 YIAIPKANGYQSLHTSMIgphgvP--------VEVQIRTEDMDQMAEMGVAAHWaykeHGETGTTAQI-------RAQR- 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   518 ktgclnnadfalrvgWLNAIREWQEEfvgNMSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGN 597
Cdd:PRK11092 358 ---------------WMQSLLELQQS---AGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGH 419
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7141304   598 KMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSKSAfqrhkqWLQHAKTRSARHKIMRFLR 659
Cdd:PRK11092 420 ACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAA------WLNFVVSSKARAKIRQLLK 475
relA PRK10872
(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional
177-661 1.04e-65

(p)ppGpp synthetase I/GTP pyrophosphokinase; Provisional


Pssm-ID: 182797 [Multi-domain]  Cd Length: 743  Bit Score: 234.30  E-value: 1.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   177 VAVARILGELELDWESIVAGLLHDTVeDTNFITFEKIEEEFGATVRHIVEGETKVSKLGKLKCkTESETIQDVKADDLRQ 256
Cdd:PRK10872  60 VEMVEILSTLSMDIDTLRAALLFPLA-DANVVSEDVLRESVGKSIVNLIHGVRDMDAIRQLKA-THNDSVSSEQVDNVRR 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   257 MFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYdrvtSR 336
Cdd:PRK10872 138 MLLAMVEDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPDEY----KR 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   337 IANLYKEhekelteanrilvKKIEDDQFLD-LVT----------VNTDVRSVCKETYSIYKAALKSKGSINDYNQIAQLR 405
Cdd:PRK10872 214 IAKLLHE-------------RRIDREHYIEeFVGhlraemkaegVKAEVYGRPKHIYSIWRKMQKKSLAFDELFDVRAVR 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   406 IVVKPkpsvgvgplcspQQICYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQSLHTTVipfLYESMFRLEVQIRTEEMDL 485
Cdd:PRK10872 281 IVAER------------LQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVV---LGPGGKTVEIQIRTRQMHE 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   486 IAERGIAVYYNGKSLSTGlvgnavplgrnSRGKTGCLNnadfalRVGWLNAIREWQEEFVgnmSSREFVDTITRDLLGSR 565
Cdd:PRK10872 346 DAELGVAAHWKYKEGAAA-----------GGGRSGHED------RIAWLRKLIAWQEEMA---DSGEMLDEVRSQVFDDR 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   566 VFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTynalssksafQRH----KQW 641
Cdd:PRK10872 406 VYVFTPKGDVVDLPAGSTPLDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIIT----------QKQpnpsRDW 475
                        490       500
                 ....*....|....*....|....
gi 7141304   642 LQ----HAKTRSARHKIMRFLREQ 661
Cdd:PRK10872 476 LNpnlgYVTTSRGRSKIHAWFRKQ 499
HD_4 pfam13328
HD domain; HD domains are metal dependent phosphohydrolases.
154-310 5.22e-47

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433119 [Multi-domain]  Cd Length: 157  Bit Score: 164.74  E-value: 5.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    154 LKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNfITFEKIEEEFGATVRHIVEGETKVSK 233
Cdd:pfam13328   2 LALAAPLHAGQRKGTGEPYLSHALGVAAILAELGLDADTVIAALLHDVVEDTG-GSLEEIEERFGDEVARLVEGVSRLDR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7141304    234 LGKLKCKTESETIQdVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGM 310
Cdd:pfam13328  81 IQKLAARDWAERKA-AQAENLRKMLLAMVEDIRVVLVKLADRLQTLRSLAAAPPEKQRAIARETLDIYAPLANRLGI 156
RelA_SpoT pfam04607
Region found in RelA / SpoT proteins; This region of unknown function is found in RelA and ...
379-492 7.46e-35

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: 128.44  E-value: 7.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    379 KETYSIYKAALKSKGSINDYNQIAQLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQS 458
Cdd:pfam04607   4 KSPYSIYEKMQRKGLLFEEIYDLIGIRIIVQFVDD------------CYRVLGIIHSLWDPIPGRFKDYIAIPKPNGYRS 71
                          90       100       110
                  ....*....|....*....|....*....|....
gi 7141304    459 LHTTVIPFlyESMFRLEVQIRTEEMDLIAERGIA 492
Cdd:pfam04607  72 LHTTVIIG--PEGVPVEIQIRTIAMHFWAEYGIA 103
RelA_SpoT smart00954
Region found in RelA / SpoT proteins; The functions of Escherichia coli RelA and SpoT differ ...
379-499 4.47e-34

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: 126.14  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304     379 KETYSIY-KAALKSKGSINDYNQIAQLRIVVKPKPSvgvgplcspqqiCYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQ 457
Cdd:smart00954   4 KHLYSIYkKMRRKGEISFDEITDLAGVRIIVDFVDD------------CYRVLGILHSLFDPIPGRFKDYIANPKPNGYR 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 7141304     458 SLHTTVIpflYESMFRLEVQIRTEEMDLIAERGIAVYYNGKS 499
Cdd:smart00954  72 SLHTTVI---GPEGRPVEIQIRTILMHAWAELGHAAHYKYKE 110
TGS_RSH cd01668
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ...
567-625 2.65e-33

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: 122.25  E-value: 2.65e-33
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7141304  567 FVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVT 625
Cdd:cd01668   1 FVFTPKGDVVSLPKGATPIDFAYAIHTDVGNKCVGAKVNGKIVPLDYVLKNGDVVEIIT 59
NT_Rel-Spo_like cd05399
Nucleotidyltransferase (NT) domain of RelA- and SpoT-like ppGpp synthetases and hydrolases; ...
368-489 5.20e-31

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: 118.22  E-value: 5.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  368 VTVNTDVRSVCKETYSIY-KAALKSK--GSINDYNQIAQLRIVVKPKpsvgvgplcspqQICYHVLGLVHEIWKPIPRTV 444
Cdd:cd05399  17 IGRVASVSGRVKSPYSIYeKLRRKGKdlPILDEITDLVGVRVVLLFV------------DDCYRVLDLLHSLFKVIPGRV 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7141304  445 KDYIATPKPNGYQSLHTTVIPFLYESMFRLEVQIRTEEMDLIAER 489
Cdd:cd05399  85 KDYIAEPKENGYQSLHLVVRGPEDKAGVLIEIQIRTILMHAWAEL 129
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
566-625 2.60e-24

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: 96.46  E-value: 2.60e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    566 VFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVT 625
Cdd:pfam02824   1 IRVYTPDGKVPDLPRGATPEDFAYAIHTSLAKKFIYAKVNGQLVGLDHPLEDGDVVEIVT 60
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
173-279 3.17e-11

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 61.10  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304    173 IIHPVAVARILGELELDWES------IVAGLLHDTVEDTnfitFEKIEEEFGATVRHIVEGETKVSKLGKLKCKTESETI 246
Cdd:pfam01966   2 LEHSLRVALLARELAEELGEldrellLLAALLHDIGKGP----FGDEKPEFEIFLGHAVVGAEILRELEKRLGLEDVLKL 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 7141304    247 QDVKADDLRQMFLAMTDEVRVIIVKLADRLHNM 279
Cdd:pfam01966  78 ILEHHESWEGAGYPEEISLEARIVKLADRLDAL 110
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
170-301 3.13e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 56.19  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304  170 EPFIIHPVAVARI-------LGELELDWESI-VAGLLHDTVEDTnfITFEKIEEEFGATVRHIVEGETKVSKLGKLKC-K 240
Cdd:cd00077   1 EHRFEHSLRVAQLarrlaeeLGLSEEDIELLrLAALLHDIGKPG--TPDAITEEESELEKDHAIVGAEILRELLLEEViK 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7141304  241 TESETIQDV------KADDLRQMFLAMTDE--VRVIIVKLADRLHNMRTLCHmppHKQSSIAGETLQVF 301
Cdd:cd00077  79 LIDELILAVdashheRLDGLGYPDGLKGEEitLEARIVKLADRLDALRRDSR---EKRRRIAEEDLEEL 144
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
168-284 6.82e-08

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 51.91  E-value: 6.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304     168 SGEPFIIHPVAVARILGEL-----ELDWESI-VAGLLHDTVEDTnfiTFEKIEEEFGATVRHIVEGETKVSKLGKLKCKT 241
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALaeelgLLDIELLlLAALLHDIGKPG---TPDSFLVKTSVLEDHHFIGAEILLEEEEPRILE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 7141304     242 ESEtIQDVKAddlRQMFLAMTDE----VRVIIVKLADRLHNMRTLCH 284
Cdd:smart00471  78 EIL-RTAILS---HHERPDGLRGepitLEARIVKVADRLDALRADRR 120
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
578-625 2.37e-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: 48.85  E-value: 2.37e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 7141304  578 LPKGATVVDYAYLIHTEIGNKMVAAK--VNGNLVSPTHVLENAEVVEIVT 625
Cdd:cd01669  29 LKRGSTPRDLAYKIHTDLGKGFLYAIdaRTKMRLGEDYELKHGDVVKIVS 78
TGS cd01616
TGS (ThrRS, GTPase and SpoT) domain structurally similar to a beta-grasp ubiquitin-like fold; ...
568-623 5.00e-07

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: 47.60  E-value: 5.00e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7141304  568 VFTPK---GEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEI 623
Cdd:cd01616   2 VFTVGktpGTVFVMNKGATAYSCAMHLHEDYCRKSILALVDGQLWDMYYPLTKGDEIKF 60
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
568-625 6.31e-07

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: 47.62  E-value: 6.31e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7141304  568 VFT-PKGEIKN------LPKGATVVDYAYLIHTEIGNKMVAAKV-------NGNLVSPTHVLENAEVVEIVT 625
Cdd:cd01666   6 VYTkPPGKKPDfdepfiLRRGSTVEDVAEKIHKDLAENFKYARVwgksvkfDGQRVGLDHVLEDGDIVEIHK 77
YjbM COG2357
ppGpp synthetase catalytic domain (RelA/SpoT-type nucleotidyltranferase) [Nucleotide transport ...
444-488 1.40e-06

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: 50.93  E-value: 1.40e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 7141304  444 VKDYIATPKPNGYQSLHTTV-IP-FLYESM--FRLEVQIRTEEMDLIAE 488
Cdd:COG2357 115 EKDYIKNPKPNGYRSLHLIVrVPvFLSDGPkgVPVEIQIRTIAMDFWAE 163
PRK09602 PRK09602
translation-associated GTPase; Reviewed
534-625 6.55e-06

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 49.42  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   534 LNAIREWQEEFvGNMSSREFVDTITRDLLGsRVFVFTPKGEIK------N-------LPKGATVVDYAYLIHTEIGNKMV 600
Cdd:PRK09602 290 LEYIREVLKKY-GGTGVQEAINTAVFDLLD-MIVVYPVEDENKltdkkgNvlpdaflLPKGSTARDLAYKIHTDIGEGFL 367
                         90       100
                 ....*....|....*....|....*...
gi 7141304   601 AAkVN---GNLVSPTHVLENAEVVEIVT 625
Cdd:PRK09602 368 YA-IDartKRRIGEDYELKDGDVIKIVS 394
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
571-638 1.06e-05

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 49.36  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7141304   571 PKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTynaLSSKSAFQ--RH 638
Cdd:PRK12444  11 PDGSVKEFVKGITLEEIAGSISSSLKKKAVAGKVNDKLYDLRRNLEEDAEVEIIT---IDSNEGVEiaRH 77
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
571-625 2.12e-05

Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 48.10  E-value: 2.12e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7141304  571 PKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVT 625
Cdd:COG0441   7 PDGSVREFEAGVTVLDVAKSISPGLAKAAVAAKVNGELVDLSTPIEEDAELEIVT 61
ACT_RelA-SpoT cd04876
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ...
797-863 1.59e-04

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: 40.51  E-value: 1.59e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7141304  797 LCVVSMDRKGIIAEVTTVLAAEGIALCSCVAEiDRGRGLAVMLFQIEA-NIESLVSVCAKVDLVLGVL 863
Cdd:cd04876   1 IRVEAIDRPGLLADITTVIAEEKINILSVNTR-TDDDGLATIRLTLEVrDLEHLARIMRKLRQIPGVI 67
TGS_ThrRS cd01667
TGS (ThrRS, GTPase and SpoT) domain found in threonyl-tRNA synthetase (ThrRS) and similar ...
571-625 9.32e-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: 9.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7141304  571 PKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVT 625
Cdd:cd01667   6 PDGSVKEFPKGTTPLDIAKSISPGLAKKAVAAKVNGELVDLSRPLEEDAELEILT 60
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
799-846 2.49e-03

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


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 39.82  E-value: 2.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 7141304  799 VVSMDRKGIIAEVTTVLAAEGIALCSCVAEIDRGRGLAVMLFQIEANI 846
Cdd:COG2716  95 VVGNDRPGIVAEVTQFLAERGINIEDLSTKTYPAPMSGTPLFSAQITV 142
 
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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