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Conserved domains on  [gi|1239957366|ref|XP_022264351|]
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ubiquitin-like modifier-activating enzyme 5 isoform X3 [Canis lupus familiaris]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 10091534)

HesA/MoeB/ThiF family protein similar to eukaryotic ubiquitin-activating enzyme 5 (UBA5), a UFM1 (ubiquitin-fold modifier 1) E1-activating enzyme, and to bacterial protein HesA that may be required for efficient nitrogen fixation

CATH:  3.40.50.720
Gene Ontology:  GO:0008641
PubMed:  12660720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 1-207 3.81e-66

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: 206.94  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggl 79
Cdd:cd00757    39 YLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGV 159
Cdd:cd00757   110 ---AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCA 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1239957366 160 CAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSM 207
Cdd:cd00757   179 EAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFRTLKL 228
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 1-207 3.81e-66

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: 206.94  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggl 79
Cdd:cd00757    39 YLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGV 159
Cdd:cd00757   110 ---AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCA 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1239957366 160 CAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSM 207
Cdd:cd00757   179 EAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-213 5.60e-49

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: 163.20  E-value: 5.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggl 79
Cdd:pfam00899  38 YLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTP-ENAEELI-------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGV 159
Cdd:pfam00899 109 ---KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCT 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366 160 CAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFFPTMSMK-PNPQC 213
Cdd:pfam00899 179 VAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-213 6.68e-35

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: 126.78  E-value: 6.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggl 79
Cdd:COG0476    45 YLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL-------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregv 159
Cdd:COG0476   116 ---AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE------ 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239957366 160 cAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 213
Cdd:COG0476   185 -AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
1-109 1.96e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.91  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggle 80
Cdd:PRK08644   46 ALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF--------- 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 1239957366  81 egKPVDLVLSCVDNFEA-RMTINTACNELG 109
Cdd:PRK08644  116 --KDCDIVVEAFDNAETkAMLVETVLEHPG 143
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 2-103 1.31e-09

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 56.80  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisngglee 81
Cdd:TIGR02354  40 LARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAYDEKITE-ENIDKFF---------- 108

                          90       100
                  ....*....|....*....|...
gi 1239957366  82 gKPVDLVLSCVDNFEAR-MTINT 103
Cdd:TIGR02354 109 -KDADIVCEAFDNAEAKaMLVNA 130
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 1-207 3.81e-66

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: 206.94  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggl 79
Cdd:cd00757    39 YLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGV 159
Cdd:cd00757   110 ---AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCA 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1239957366 160 CAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSM 207
Cdd:cd00757   179 EAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-213 5.60e-49

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: 163.20  E-value: 5.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggl 79
Cdd:pfam00899  38 YLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTP-ENAEELI-------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGV 159
Cdd:pfam00899 109 ---KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCT 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366 160 CAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFFPTMSMK-PNPQC 213
Cdd:pfam00899 179 VAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-213 6.68e-35

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: 126.78  E-value: 6.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggl 79
Cdd:COG0476    45 YLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL-------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 eegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregv 159
Cdd:COG0476   116 ---AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE------ 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239957366 160 cAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 213
Cdd:COG0476   185 -AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
1-109 1.96e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.91  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggle 80
Cdd:PRK08644   46 ALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF--------- 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 1239957366  81 egKPVDLVLSCVDNFEA-RMTINTACNELG 109
Cdd:PRK08644  116 --KDCDIVVEAFDNAETkAMLVETVLEHPG 143
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-136 9.78e-18

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: 78.46  E-value: 9.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVlfevhnyNITTVEnfqhfmDRISNGGL 79
Cdd:cd01483    17 NLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAVP------EGISEDNL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366  80 EE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 136
Cdd:cd01483    84 DDfLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-139 7.13e-17

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 79.65  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtVENFQHFMDRisng 77
Cdd:PRK07688   42 MLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAVAAKKRLEEINSDVRVEAIVQDVT-AEELEELVTG---- 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239957366  78 gleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGvsenAVS--GHIQLIIPGESACFAC 139
Cdd:PRK07688  117 -------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGKTPCLRC 169
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 6-141 1.58e-15

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO 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 by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 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: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 75.49  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   6 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITT----VENFQHFmdrisnggle 80
Cdd:cd01489    22 GFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEFFKQF---------- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239957366  81 egkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 141
Cdd:cd01489    92 -----DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-213 7.03e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 74.28  E-value: 7.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQAAEYTLRNINPDVlfevhnynitTVENFQhfmDRISNGG 78
Cdd:PRK08762  154 LAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVDSAAQRLAALNPDV----------QVEAVQ---ERVTSDN 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  79 LEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESA----CFAC----APPLVVAANI 149
Cdd:PRK08762  219 VEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSC 296

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239957366 150 DEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 213
Cdd:PRK08762  297 AEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDPHC 353
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 2-213 1.09e-12

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 66.41  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtvenfQHFMDRISNGgle 80
Cdd:PRK05690   51 LAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESARAALARINPHIAIETINARLD-----DDELAALIAG--- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  81 egkpVDLVLSCVDNFEARMTINTACNELGQTWmesgVSENAV--SGHIQLIIPGESA-CFACAPPLVVAANIdekTLKRE 157
Cdd:PRK05690  123 ----HDLVLDCTDNVATRNQLNRACFAAKKPL----VSGAAIrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEA 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366 158 GVCAAsLPttmGVVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 213
Cdd:PRK05690  192 GVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLLLYDAMTMQFREMKLKRDPGC 245
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 2-139 1.24e-12

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 67.45  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEYTLRNINPDVlfEVHNYNI-TTVENFQHFMdrisng 77
Cdd:PRK12475   43 LVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAIAAKEHLRKINSEV--EIVPVVTdVTVEELEELV------ 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239957366  78 gleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESG-VSENAVSghiQLIIPGESACFAC 139
Cdd:PRK12475  115 -----KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVGSYGVT---YTIIPGKTPCLRC 169
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 1-104 3.13e-12

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: 63.94  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTVENFQHFMDrisnggle 80
Cdd:cd01487    17 LLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGD-------- 88

                          90       100
                  ....*....|....*....|....*
gi 1239957366  81 egkpVDLVLSCVDNFEA-RMTINTA 104
Cdd:cd01487    89 ----CDIVVEAFDNAETkAMLAESL 109
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 6-142 3.85e-12

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 64.91  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   6 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPdvlfevhNYNITTvenFQHFMDRISNGGLEEGKP 84
Cdd:cd01484    22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNP-------NCKVVP---YQNKVGPEQDFNDTFFEQ 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  85 VDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 142
Cdd:cd01484    92 FHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 1-97 2.56e-10

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: 59.54  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisn 76
Cdd:cd00755    29 ALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEVDAVEEFLTP-DNSEDLL----- 99

                          90       100
                  ....*....|....*....|.
gi 1239957366  77 ggleeGKPVDLVLSCVDNFEA 97
Cdd:cd00755   100 -----GGDPDFVVDAIDSIRA 115
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 1-109 7.25e-10

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: 58.17  E-value: 7.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   1 MLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEYTLRNINPDVlfevhnyNITTVENFqhfmdrIS 75
Cdd:COG1179    42 ALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDC-------EVTAIDEF------VT 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1239957366  76 NGGLEE--GKPVDLVLSCVDNFEARMTINTACNELG 109
Cdd:COG1179   105 PENADEllSEDYDYVIDAIDSVSAKAALIAWCRRRG 140
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 2-103 1.31e-09

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 56.80  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisngglee 81
Cdd:TIGR02354  40 LARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAYDEKITE-ENIDKFF---------- 108

                          90       100
                  ....*....|....*....|...
gi 1239957366  82 gKPVDLVLSCVDNFEAR-MTINT 103
Cdd:TIGR02354 109 -KDADIVCEAFDNAEAKaMLVNA 130
PRK08328 PRK08328
hypothetical protein; Provisional
 2-187 1.68e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 57.11  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVhnynittvenfqhFMDRISNGGL 79
Cdd:PRK08328   46 LAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET-------------FVGRLSEENI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  80 EEG-KPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREG 158
Cdd:PRK08328  113 DEVlKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTKRLREIFP-----KVKKKKGKFPI 185

                         170       180
                  ....*....|....*....|....*....
gi 1239957366 159 VCAaslptTMGVVAGILVQNVLKFLLNFG 187
Cdd:PRK08328  186 LGA-----TAGVIGSIQAMEVIKLITGYG 209
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 2-144 1.04e-07

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: 52.36  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQ-AAEYTLRNInPDVLFEVHNYNITT--VENFQHFmdrisng 77
Cdd:cd01488    18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEvAAKFVNDRV-PGVNVTPHFGKIQDkdEEFYRQF------- 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366  78 gleegkpvDLVLSCVDNFEARMTIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 144
Cdd:cd01488    90 --------NIIICGLDSIEARRWINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 2-211 1.68e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 52.19  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLE 80
Cdd:PRK05600   60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  81 EGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAvsGHIQLIIPGESAC-------FACAPPLVVAANidekt 153
Cdd:PRK05600  128 LLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFH--GELAVFNSGPDHRgvglrdlFPEQPSGDSIPD----- 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239957366 154 lkregvCAAS--LPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNP 211
Cdd:PRK05600  201 ------CATAgvLGATTAVIGALMATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 2-109 2.49e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 51.41  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEYTLRNINPDVLFEVHNYNITTvenfqhfmdrisNGGLE 80
Cdd:PRK05597   47 LAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQPKAESAREAMLALNPDVKVTVSVRRLTW------------SNALD 114

                          90       100
                  ....*....|....*....|....*....
gi 1239957366  81 EGKPVDLVLSCVDNFEARMTINTACNELG 109
Cdd:PRK05597  115 ELRDADVILDGSDNFDTRHLASWAAARLG 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-131 2.92e-07

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 51.81  E-value: 2.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366    8 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPV 85
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKL 519

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1239957366   86 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 131
Cdd:TIGR01408  520 DVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
PRK08223 PRK08223
hypothetical protein; Validated
 2-109 2.59e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 48.14  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMDrisnggle 80
Cdd:PRK08223   46 LARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFLD-------- 116

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1239957366  81 egkPVDLVLSCVDNFE--ARMTINTACNELG 109
Cdd:PRK08223  117 ---GVDVYVDGLDFFEfdARRLVFAACQQRG 144
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 8-131 2.89e-06

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 48.44  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   8 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNI-TTVENFqhFMDRISNGgleegkpV 85
Cdd:cd01490    29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgPETEHI--FNDEFWEK-------L 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1239957366  86 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 131
Cdd:cd01490   100 DGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 2-213 2.92e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 48.17  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITT---VENFQHFmdrisng 77
Cdd:PRK07878   61 LAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPsnaVELFSQY------- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  78 gleegkpvDLVLSCVDNFEARMTINTACNELGQ--TW-----MESGVS---ENAVSGHiqliipgeSACFAC-----APP 142
Cdd:PRK07878  134 --------DLILDGTDNFATRYLVNDAAVLAGKpyVWgsiyrFEGQASvfwEDAPDGL--------GLNYRDlypepPPP 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239957366 143 LVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 213
Cdd:PRK07878  198 GMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
2-213 1.92e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.88  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLE 80
Cdd:PRK07411   57 LAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLS------------SENALD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239957366  81 EGKPVDLVLSCVDNFEARMTINTACNELGQTwmesgvsenAVSGHIqLIIPGESACF-------------ACAPPLVVAA 147
Cdd:PRK07411  125 ILAPYDVVVDGTDNFPTRYLVNDACVLLNKP---------NVYGSI-FRFEGQATVFnyeggpnyrdlypEPPPPGMVPS 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239957366 148 NidektlkREGVCAASLPttmGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSMKPNPQC 213
Cdd:PRK07411  195 C-------AEGGVLGILP---GIIGVIQATETIKIILGAGNTlsGRLLLYNALDMKFRELKLRPNPER 252
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 2-72 8.34e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 37.09  E-value: 8.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239957366   2 LTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEYTLRNINPDVLFEVHNyNITTVENFQHFMD 72
Cdd:PRK15116   49 LARTGIGAITLIDMDDVCVTNTNR---QIHalrdNVGLAKAEVMAERIRQINPECRVTVVD-DFITPDNVAEYMS 119
 
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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