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Conserved domains on  [gi|298265167|gb|EFI06831|]
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ThiF family protein, ubiquitin-activating enzyme [Bacteroides sp. 3_1_19]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 320623)

ubiquitin-activating E1 family protein is an activating enzyme similar to Osphranter rufus ubiquitin-activating enzyme E1 Y that activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_enzyme_family super family cl22428
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 5-263 1.32e-77

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


The actual alignment was detected with superfamily member TIGR03736:

Pssm-ID: 451392  Cd Length: 244  Bit Score: 234.95  E-value: 1.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167    5 HFTDKYLLSpyHPVTVLVAGAGGTGYQVITSLARMSVALQALGHP-GLHLTAFDPDTVTEANIGRQLFSETELGLNKATA 83
Cdd:TIGR03736   1 HKIPPALLS--RPVSVVLVGAGGTGSQVIAGLARLHHALKALGHPgGLAVTVYDDDTVSEANVGRQAFYPADVGQNKAIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167   84 LVTRVNRFFGYAWEARECRYpiitkEGDKSVPLANIIITCTDNTRSRLDLWRFLKkyreyknNDEKAPIYWMDFGNAQTT 163
Cdd:TIGR03736  79 LVNRLNQAMGTDWTAHPERV-----ERSSTLHRPDIVIGCVDNRAARLAILRAFE-------GGYSGYAYWLDLGNRADD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  164 GQVMVGNIRS------KISQPASSEYLPmprmnviteEVSYSTIREEDSGPSCSLAEALRKQDLFINSMLAQIGCDILWR 237
Cdd:TIGR03736 147 GQVILGQVPSrakgenRLRLPHVGELFP---------ELIDPSVDPDDDRPSCSLAEALAKQSLFINQAIAVFAMNLLWK 217

                         250       260
                  ....*....|....*....|....*.
gi 298265167  238 MFREGRTFYRGAYLNLGTLRVNPIPV 263
Cdd:TIGR03736 218 LFRKGRLEFHGVFVNLATGRTNPLPV 243
 
Name Accession Description Interval E-value
PRTRC_ThiF TIGR03736
PRTRC system ThiF family protein; A novel genetic system characterized by six major proteins, ...
 5-263 1.32e-77

PRTRC system ThiF family protein; A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. This family is the PRTRC system ThiF family protein.


Pssm-ID: 163448  Cd Length: 244  Bit Score: 234.95  E-value: 1.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167    5 HFTDKYLLSpyHPVTVLVAGAGGTGYQVITSLARMSVALQALGHP-GLHLTAFDPDTVTEANIGRQLFSETELGLNKATA 83
Cdd:TIGR03736   1 HKIPPALLS--RPVSVVLVGAGGTGSQVIAGLARLHHALKALGHPgGLAVTVYDDDTVSEANVGRQAFYPADVGQNKAIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167   84 LVTRVNRFFGYAWEARECRYpiitkEGDKSVPLANIIITCTDNTRSRLDLWRFLKkyreyknNDEKAPIYWMDFGNAQTT 163
Cdd:TIGR03736  79 LVNRLNQAMGTDWTAHPERV-----ERSSTLHRPDIVIGCVDNRAARLAILRAFE-------GGYSGYAYWLDLGNRADD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  164 GQVMVGNIRS------KISQPASSEYLPmprmnviteEVSYSTIREEDSGPSCSLAEALRKQDLFINSMLAQIGCDILWR 237
Cdd:TIGR03736 147 GQVILGQVPSrakgenRLRLPHVGELFP---------ELIDPSVDPDDDRPSCSLAEALAKQSLFINQAIAVFAMNLLWK 217

                         250       260
                  ....*....|....*....|....*.
gi 298265167  238 MFREGRTFYRGAYLNLGTLRVNPIPV 263
Cdd:TIGR03736 218 LFRKGRLEFHGVFVNLATGRTNPLPV 243
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 19-173 1.72e-23

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 92.72  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSValqalghpgLHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGY-AW 96
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGV---------GKITLIDFDTVELSNLNRQfLARQADIGKPKAEVAARRLNELNPGvNV 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298265167  97 EARECRYPIITKEGDKSVPlaNIIITCTDNTRSRLDLWRFLKKYReyknndekapIYWMDFGNAQTTGQVMVGNIRS 173
Cdd:cd01483   72 TAVPEGISEDNLDDFLDGV--DLVIDAIDNIAVRRALNRACKELG----------IPVIDAGGLGLGGDIQVIDIGS 136
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-168 2.08e-15

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 73.45  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167   19 TVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGYAwE 97
Cdd:pfam00899  22 RVLIVGAGGLGSEAAKYLARAGVG---------KITLVDFDTVELSNLNRQfLFREADIGKPKAEVAAERLREINPDV-E 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298265167   98 ARECRYPIITKEGDKSVPLANIIITCTDNTRSRLDLWRFLKKYReyknndekapIYWMDFGNAQTTGQVMV 168
Cdd:pfam00899  92 VEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLG----------KPLIEAGVLGFKGQVTV 152
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 19-168 1.49e-10

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 59.76  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSValqalGhpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGYAW- 96
Cdd:COG0476   29 RVLVVGAGGLGSPVALYLAAAGV-----G----TLTLVDDDVVELSNLQRQiLYTEADVGRPKVEAAAERLRALNPDVEv 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298265167  97 EARECRypiITKE-GDKSVPLANIIITCTDNTRSRLDLwrflkkyreyknND--EKAPIYWMDFGNAQTTGQVMV 168
Cdd:COG0476  100 EAIPER---LTEEnALELLAGADLVLDCTDNFATRYLL------------NDacVKLGIPLVSGAVIGFEGQVTV 159
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 16-90 5.33e-05

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 43.72  E-value: 5.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298265167  16 HPVTVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNR 90
Cdd:PRK05600  40 HNARVLVIGAGGLGCPAMQSLASAGVG---------TITLIDDDTVDVSNIHRQiLFGASDVGRPKVEVAAERLKE 106
 
Name Accession Description Interval E-value
PRTRC_ThiF TIGR03736
PRTRC system ThiF family protein; A novel genetic system characterized by six major proteins, ...
 5-263 1.32e-77

PRTRC system ThiF family protein; A novel genetic system characterized by six major proteins, included a ParB homolog and a ThiF homolog, is designated PRTRC, or ParB-Related,ThiF-Related Cassette. This family is the PRTRC system ThiF family protein.


Pssm-ID: 163448  Cd Length: 244  Bit Score: 234.95  E-value: 1.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167    5 HFTDKYLLSpyHPVTVLVAGAGGTGYQVITSLARMSVALQALGHP-GLHLTAFDPDTVTEANIGRQLFSETELGLNKATA 83
Cdd:TIGR03736   1 HKIPPALLS--RPVSVVLVGAGGTGSQVIAGLARLHHALKALGHPgGLAVTVYDDDTVSEANVGRQAFYPADVGQNKAIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167   84 LVTRVNRFFGYAWEARECRYpiitkEGDKSVPLANIIITCTDNTRSRLDLWRFLKkyreyknNDEKAPIYWMDFGNAQTT 163
Cdd:TIGR03736  79 LVNRLNQAMGTDWTAHPERV-----ERSSTLHRPDIVIGCVDNRAARLAILRAFE-------GGYSGYAYWLDLGNRADD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  164 GQVMVGNIRS------KISQPASSEYLPmprmnviteEVSYSTIREEDSGPSCSLAEALRKQDLFINSMLAQIGCDILWR 237
Cdd:TIGR03736 147 GQVILGQVPSrakgenRLRLPHVGELFP---------ELIDPSVDPDDDRPSCSLAEALAKQSLFINQAIAVFAMNLLWK 217

                         250       260
                  ....*....|....*....|....*.
gi 298265167  238 MFREGRTFYRGAYLNLGTLRVNPIPV 263
Cdd:TIGR03736 218 LFRKGRLEFHGVFVNLATGRTNPLPV 243
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 19-173 1.72e-23

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 92.72  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSValqalghpgLHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGY-AW 96
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGV---------GKITLIDFDTVELSNLNRQfLARQADIGKPKAEVAARRLNELNPGvNV 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298265167  97 EARECRYPIITKEGDKSVPlaNIIITCTDNTRSRLDLWRFLKKYReyknndekapIYWMDFGNAQTTGQVMVGNIRS 173
Cdd:cd01483   72 TAVPEGISEDNLDDFLDGV--DLVIDAIDNIAVRRALNRACKELG----------IPVIDAGGLGLGGDIQVIDIGS 136
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-168 2.08e-15

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 73.45  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167   19 TVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGYAwE 97
Cdd:pfam00899  22 RVLIVGAGGLGSEAAKYLARAGVG---------KITLVDFDTVELSNLNRQfLFREADIGKPKAEVAAERLREINPDV-E 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298265167   98 ARECRYPIITKEGDKSVPLANIIITCTDNTRSRLDLWRFLKKYReyknndekapIYWMDFGNAQTTGQVMV 168
Cdd:pfam00899  92 VEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLG----------KPLIEAGVLGFKGQVTV 152
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 19-168 1.49e-10

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 59.76  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSValqalGhpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGYAW- 96
Cdd:COG0476   29 RVLVVGAGGLGSPVALYLAAAGV-----G----TLTLVDDDVVELSNLQRQiLYTEADVGRPKVEAAAERLRALNPDVEv 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298265167  97 EARECRypiITKE-GDKSVPLANIIITCTDNTRSRLDLwrflkkyreyknND--EKAPIYWMDFGNAQTTGQVMV 168
Cdd:COG0476  100 EAIPER---LTEEnALELLAGADLVLDCTDNFATRYLL------------NDacVKLGIPLVSGAVIGFEGQVTV 159
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 19-131 1.12e-09

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 57.10  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNRFFGY--- 94
Cdd:cd00757   23 RVLVVGAGGLGSPAAEYLAAAGVG---------KLGLVDDDVVELSNLQRQiLHTEADVGQPKAEAAAERLRAINPDvei 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 298265167  95 -AWEARecrypiITKEG-DKSVPLANIIITCTDNTRSRL 131
Cdd:cd00757   94 eAYNER------LDAENaEELIAGYDLVLDCTDNFATRY 126
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 20-133 3.34e-06

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 46.83  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298265167  20 VLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQLFSETE-LGLNKATAL------------VT 86
Cdd:cd00755   14 VAVVGLGGVGSWAAEALARSGVG---------KLTLIDFDVVCVSNLNRQIHALLStVGKPKVEVMaerirdinpeceVD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 298265167  87 RVNRFFgyaweARECRYPIITKEGDksvplanIIITCTDNTRSRLDL 133
Cdd:cd00755   85 AVEEFL-----TPDNSEDLLGGDPD-------FVVDAIDSIRAKVAL 119
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 19-91 5.09e-05

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 42.75  E-value: 5.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQLFSETELGLNKATALVTRVNRF 91
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVG---------NLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREI 64
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 16-90 5.33e-05

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 43.72  E-value: 5.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298265167  16 HPVTVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNR 90
Cdd:PRK05600  40 HNARVLVIGAGGLGCPAMQSLASAGVG---------TITLIDDDTVDVSNIHRQiLFGASDVGRPKVEVAAERLKE 106
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 19-88 1.41e-04

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 41.99  E-value: 1.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298265167  19 TVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQLFS-ETELGLNKATALVTRV 88
Cdd:COG1179   26 HVAVVGLGGVGSWAAEALARSGVG---------RLTLVDLDDVCESNINRQLHAlDSTVGRPKVEVMAERI 87
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 20-90 3.91e-04

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 40.80  E-value: 3.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298265167  20 VLVAGAGGTGYQVITSLArmsvalqALGHPGLHLtaFDPDTVTEANIGRQ-LFSETELGLNKATALVTRVNR 90
Cdd:cd01488    2 ILVIGAGGLGCELLKNLA-------LSGFRNIHV--IDMDTIDVSNLNRQfLFREKDIGKPKAEVAAKFVND 64
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
18-84 8.83e-04

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 39.45  E-value: 8.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298265167  18 VTVLVAGAGGTGYQVITSLARMSVAlqalghpglHLTAFDPDTVTEANIGRQLFSETELGLNKATAL 84
Cdd:PRK08644  29 AKVGIAGAGGLGSNIAVALARSGVG---------NLKLVDFDVVEPSNLNRQQYFISQIGMPKVEAL 86
 
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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