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Conserved domains on  [gi|500821|gb|AAB68430|]
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Yhr003cp [Saccharomyces cerevisiae]

Protein Classification

tRNA threonylcarbamoyladenosine dehydratase( domain architecture ID 10091512)

tRNA threonylcarbamoyladenosine dehydratase catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine to form cyclic t(6)A in tRNA

CATH:  2.40.30.180
EC:  6.1.-.-
Gene Ontology:  GO:0008641|GO:0061503|GO:0016887|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 64-298 4.34e-112

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: 328.41  E-value: 4.34e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPW 143
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   144 SEIKARAKAWTKENSHDLIFADgesPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTEFDP 223
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD---PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500821   224 ISRCVRRKLRKRGIATGISVVFSNEMLDPRRDDILSPIDcEHRAINAVRDEALRHLPELGTMPGIFGLSIATWIL 298
Cdd:cd00755 158 LARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGD-EVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 64-298 4.34e-112

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: 328.41  E-value: 4.34e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPW 143
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   144 SEIKARAKAWTKENSHDLIFADgesPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTEFDP 223
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD---PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500821   224 ISRCVRRKLRKRGIATGISVVFSNEMLDPRRDDILSPIDcEHRAINAVRDEALRHLPELGTMPGIFGLSIATWIL 298
Cdd:cd00755 158 LARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGD-EVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 57-337 5.65e-59

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: 192.86  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821      57 LARNYAF--LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLK 134
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     135 EHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVsin 214
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELI----KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     215 disMTEFDPISRCV-----RRKLRKRGIATGIsvvfsnemldprrddilspidcehrainavrdealrhlpeLGTMPGIF 289
Cdd:pfam00899 154 ---IPGKTPCYRCLfpedpPPKLVPSCTVAGV----------------------------------------LGPTTAVV 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 500821     290 GLSIATWILTKVSGYPmkENEVKNRLKFYDSIleTFQKQMARLNENKE 337
Cdd:pfam00899 191 AGLQALEALKLLLGKG--EPNLAGRLLQFDAL--TMTFRELRLALKNP 234
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 64-298 5.73e-51

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: 172.19  E-value: 5.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLN--THccAVLSDIGKPKVQCLKEHLSKIA 141
Cdd:COG1179  14 YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINrqLH--ALDSTVGRPKVEVMAERIRDIN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   142 PWSEIKARAKAWTKENSHDLIFADgesPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTEF 221
Cdd:COG1179  92 PDCEVTAIDEFVTPENADELLSED---YDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   222 DPISRCVRRKLRKRGIATGISVVFSNEMLDPRRddilspidcEHRAINAVRDEALRHLPeLGT---MPGIFGLSIATWIL 298
Cdd:COG1179 169 CPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQ---------ADGTVCDTGGTGLKCAG-PGSisfVPAVFGLIAAGEVI 238
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 58-250 3.22e-21

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 92.56  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     58 ARNYaflGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHL 137
Cdd:PRK15116  17 ARLY---GEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    138 SKIAPWSEIKARAKAWTKENSHDLIFADGespTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDIS 217
Cdd:PRK15116  94 RQINPECRVTVVDDFITPDNVAEYMSAGF---SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500821    218 MTEFDPISRCVRRKLRK--------RGiATGISVVFSNEML 250
Cdd:PRK15116 171 KTIQDPLAAKLRERLKSdfgvvknsKG-KLGVDCVFSTEAL 210
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-199 9.59e-06

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: 47.96  E-value: 9.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821       49 DDHLFREQLArnyaFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKP 128
Cdd:TIGR01408    3 DEALYSRQLY----VLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500821      129 KVQCLKEHLSKIAPWSEIKARAKAWTKEnshdliFADGESPTFIVDCLDNLESKVDLLEYAHHNKIDVISS 199
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVPFNEE------FLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAFISA 143
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 64-298 4.34e-112

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: 328.41  E-value: 4.34e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPW 143
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   144 SEIKARAKAWTKENSHDLIFADgesPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTEFDP 223
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD---PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDP 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500821   224 ISRCVRRKLRKRGIATGISVVFSNEMLDPRRDDILSPIDcEHRAINAVRDEALRHLPELGTMPGIFGLSIATWIL 298
Cdd:cd00755 158 LARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGD-EVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 57-337 5.65e-59

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: 192.86  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821      57 LARNYAF--LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLK 134
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     135 EHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVsin 214
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELI----KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     215 disMTEFDPISRCV-----RRKLRKRGIATGIsvvfsnemldprrddilspidcehrainavrdealrhlpeLGTMPGIF 289
Cdd:pfam00899 154 ---IPGKTPCYRCLfpedpPPKLVPSCTVAGV----------------------------------------LGPTTAVV 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 500821     290 GLSIATWILTKVSGYPmkENEVKNRLKFYDSIleTFQKQMARLNENKE 337
Cdd:pfam00899 191 AGLQALEALKLLLGKG--EPNLAGRLLQFDAL--TMTFRELRLALKNP 234
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 64-298 5.73e-51

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: 172.19  E-value: 5.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLN--THccAVLSDIGKPKVQCLKEHLSKIA 141
Cdd:COG1179  14 YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINrqLH--ALDSTVGRPKVEVMAERIRDIN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   142 PWSEIKARAKAWTKENSHDLIFADgesPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTEF 221
Cdd:COG1179  92 PDCEVTAIDEFVTPENADELLSED---YDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   222 DPISRCVRRKLRKRGIATGISVVFSNEMLDPRRddilspidcEHRAINAVRDEALRHLPeLGT---MPGIFGLSIATWIL 298
Cdd:COG1179 169 CPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQ---------ADGTVCDTGGTGLKCAG-PGSisfVPAVFGLIAAGEVI 238
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 77-220 2.43e-25

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: 100.42  E-value: 2.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    77 IVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPWseIKARAKAWTKE 156
Cdd:cd01483   2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPG--VNVTAVPEGIS 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500821   157 NshDLIFADGESPTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDISMTE 220
Cdd:cd01483  80 E--DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAAE 141
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 58-250 3.22e-21

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 92.56  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     58 ARNYaflGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHL 137
Cdd:PRK15116  17 ARLY---GEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    138 SKIAPWSEIKARAKAWTKENSHDLIFADGespTFIVDCLDNLESKVDLLEYAHHNKIDVISSMGVATKSDPTRVSINDIS 217
Cdd:PRK15116  94 RQINPECRVTVVDDFITPDNVAEYMSAGF---SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500821    218 MTEFDPISRCVRRKLRK--------RGiATGISVVFSNEML 250
Cdd:PRK15116 171 KTIQDPLAAKLRERLKSdfgvvknsKG-KLGVDCVFSTEAL 210
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 54-198 7.87e-20

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: 88.26  E-value: 7.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    54 REQLARNYAF--LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHccaVL---SDIGKP 128
Cdd:COG0476   5 LERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQ---ILyteADVGRP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821   129 KVQCLKEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKIDVIS 198
Cdd:COG0476  82 KVEAAAERLRALNPDVEVEAIPERLTEENALELL----AGADLVLDCTDNFATRYLLNDACVKLGIPLVS 147
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
52-203 3.72e-18

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 82.60  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     52 LFREQLArnyAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCcAVLSDIGKPKVQ 131
Cdd:PRK08644   9 EFEAMLA---SRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQ-YFISQIGMPKVE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500821    132 CLKEHLSKIAPWSEIKARAKAWTKENSHDlIFADGEsptFIVDCLDNLESKVDLLEYAH-HNKIDVISSMGVA 203
Cdd:PRK08644  85 ALKENLLEINPFVEIEAHNEKIDEDNIEE-LFKDCD---IVVEAFDNAETKAMLVETVLeHPGKKLVAASGMA 153
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 64-182 1.58e-17

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: 80.98  E-value: 1.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHccaVL---SDIGKPKVQCLKEHLSKI 140
Cdd:cd00757  11 IGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQ---ILhteADVGQPKAEAAAERLRAI 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 500821   141 APWSEIKARAKAWTKENSHDLIF-ADgesptFIVDCLDNLESK 182
Cdd:cd00757  88 NPDVEIEAYNERLDAENAEELIAgYD-----LVLDCTDNFATR 125
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 77-218 5.82e-15

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: 72.41  E-value: 5.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    77 IVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCcAVLSDIGKPKVQCLKEHLSKIAPWSEIKARAKAWTKE 156
Cdd:cd01487   2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500821   157 NShDLIFADGEsptFIVDCLDNLESKVDLLEYA--HHNKIdVISSMGVATKSDPTRVSINDISM 218
Cdd:cd01487  81 NL-EGLFGDCD---IVVEAFDNAETKAMLAESLlgNKNKP-VVCASGMAGFGDSNNIKTKKISD 139
PRK08328 PRK08328
hypothetical protein; Provisional
 55-197 1.65e-11

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 63.66  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     55 EQLARNYAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGK-PKVQCL 133
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSA 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500821    134 KEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKIDVI 197
Cdd:PRK08328  88 KWKLERFNSDIKIETFVGRLSEENIDEVL----KGVDVIVDCLDNFETRYLLDDYAHKKGIPLV 147
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 55-202 4.95e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 60.51  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     55 EQLARNYAF--LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIG--KPKV 130
Cdd:PRK12475   3 ERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500821    131 QCLKEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKI-----DVISSMGV 202
Cdd:PRK12475  83 IAAKEHLRKINSEVEIVPVVTDVTVEELEELV----KEVDLIIDATDNFDTRLLINDLSQKYNIpwiygGCVGSYGV 155
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 54-182 1.45e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 56.15  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     54 REQLarnYAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGK--PKVQ 131
Cdd:PRK07688   7 RQEL---FSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlPKAV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500821    132 CLKEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESK 182
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELV----TGVDLIIDATDNFETR 130
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 43-182 4.75e-08

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 54.50  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     43 SRPRQYDDHLFREQLARNYAF--LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCA 120
Cdd:PRK05600   8 LSPFMQLPTSELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILF 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500821    121 VLSDIGKPKVQCLKEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESK 182
Cdd:PRK05600  88 GASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELL----NGVDLVLDGSDSFATK 145
PRK08223 PRK08223
hypothetical protein; Validated
 52-177 3.29e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 51.61  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     52 LFREQLARNYAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQ 131
Cdd:PRK08223   5 DYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 500821    132 CLKEHLSKIAPWSEIKARAKAWTKENSHDliFADGESptFIVDCLD 177
Cdd:PRK08223  85 VLAEMVRDINPELEIRAFPEGIGKENADA--FLDGVD--VYVDGLD 126
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 49-199 9.59e-06

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: 47.96  E-value: 9.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821       49 DDHLFREQLArnyaFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKP 128
Cdd:TIGR01408    3 DEALYSRQLY----VLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500821      129 KVQCLKEHLSKIAPWSEIKARAKAWTKEnshdliFADGESPTFIVDCLDNLESKVDLLEYAHHNKIDVISS 199
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVPFNEE------FLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIAFISA 143
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
64-182 2.15e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 46.27  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPW 143
Cdd:PRK07411  28 VGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPY 107

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500821    144 SEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESK 182
Cdd:PRK07411 108 CQVDLYETRLSSENALDIL----APYDVVVDGTDNFPTR 142
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 67-198 3.02e-05

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 45.22  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     67 EGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLN---THCCAvlsDIGKPKVQCLKEHLSKIAPW 143
Cdd:PRK05690  25 DGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQrqvLHDDA---TIGQPKVESARAALARINPH 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500821    144 SEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESKVDLLEYAHHNKIDVIS 198
Cdd:PRK05690 102 IAIETINARLDDDELAALI----AGHDLVLDCTDNVATRNQLNRACFAAKKPLVS 152
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 41-178 3.90e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 45.47  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     41 TVSRPRQYDDHLFREQLarnyaflGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCA 120
Cdd:PRK07878  16 TRDEVARYSRHLIIPDV-------GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIH 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500821    121 VLSDIGKPKVQCLKEHLSKIAPWSEIKARAKAWTKENSHDlIFADGEsptFIVDCLDN 178
Cdd:PRK07878  89 GQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVE-LFSQYD---LILDGTDN 142
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 64-182 6.71e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 44.86  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPW 143
Cdd:PRK05597  18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500821    144 SEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNLESK 182
Cdd:PRK05597  98 VKVTVSVRRLTWSNALDEL----RDADVILDGSDNFDTR 132
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 77-182 1.35e-04

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: 43.34  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    77 IVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPWSEIKARAKAWTKE 156
Cdd:cd01484   2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                        90       100
                ....*....|....*....|....*.
gi 500821   157 NSHDLIFAdgESPTFIVDCLDNLESK 182
Cdd:cd01484  82 QDFNDTFF--EQFHIIVNALDNIIAR 105
PRK14851 PRK14851
hypothetical protein; Provisional
 53-199 1.64e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 44.08  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     53 FREQLARNYAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQC 132
Cdd:PRK14851  22 REAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAV 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500821    133 LKEHLSKIAPWSEIKARAKAWTKENSHdlIFADGESptFIVDCLDNLESKV--DLLEYAHHNKIDVISS 199
Cdd:PRK14851 102 MKEQALSINPFLEITPFPAGINADNMD--AFLDGVD--VVLDGLDFFQFEIrrTLFNMAREKGIPVITA 166
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 62-182 1.99e-04

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: 43.72  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821       62 AFLGEEGMRKIKEQYIVIVGAGEVGswvCTML-------IRSGCQ-KIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCL 133
Cdd:TIGR01408  407 AVFGDTFQQKLQNLNIFLVGCGAIG---CEMLknfalmgVGTGKKgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTA 483

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 500821      134 KEHLSKIAPWSEIKARAKAWTKENSHdlIFADG--ESPTFIVDCLDNLESK 182
Cdd:TIGR01408  484 ADATLKINPQIKIDAHQNRVGPETET--IFNDEfyEKLDVVINALDNVEAR 532
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 77-182 3.77e-04

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: 42.37  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    77 IVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPWSEIKARaKAWTKE 156
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAY-HANIKD 80

                        90       100
                ....*....|....*....|....*.
gi 500821   157 NSHDLIFAdgESPTFIVDCLDNLESK 182
Cdd:cd01489  81 PDFNVEFF--KQFDLVFNALDNLAAR 104
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
42-179 3.92e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 42.31  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821     42 VSRPRQYDDhlfrEQLARnYAF------LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLN 115
Cdd:PRK08762 102 LERPRLLTD----EQDER-YSRhlrlpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQ 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500821    116 THCCAVLSDIGKPKVQCLKEHLSKIAPWSEIKARAKAWTKENSHDLIfadgESPTFIVDCLDNL 179
Cdd:PRK08762 177 RQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALL----QDVDVVVDGADNF 236
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 59-200 6.44e-04

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 41.48  E-value: 6.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    59 RNYAFLGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLS 138
Cdd:cd01491   4 RQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLA 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500821   139 KIAPWSEIKArakawtkenSHDLIFADGESPTFIVDCLD-NLESKVDLLEYAHHNKIDVISSM 200
Cdd:cd01491  84 ELNPYVPVTV---------STGPLTTDELLKFQVVVLTDaSLEDQLKINEFCHSPGIKFISAD 137
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 64-142 1.07e-03

Ubiquitin activating enzyme (E1), repeat 1-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. The 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 first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 40.10  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500821    64 LGEEGMRKIKEQYIVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSL--NTHCCAVLSDIGKPKVQCLKEHLSKIA 141
Cdd:cd01485   9 WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLgsNFFLDAEVSNSGMNRAAASYEFLQELN 88


                .
gi 500821   142 P 142
Cdd:cd01485  89 P 89
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 77-104 3.26e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 39.40  E-value: 3.26e-03
                         10        20
                 ....*....|....*....|....*...
gi 500821     77 IVIVGAGEVGSWVCTMLIRSGCQKIMII 104
Cdd:PRK00045 185 VLVIGAGEMGELVAKHLAEKGVRKITVA 212
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 77-148 4.70e-03

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: 38.88  E-value: 4.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500821    77 IVIVGAGEVGSWVCTMLIRSGCQKIMIIDPENISIDSLNTHCCAVLSDIGKPKVQCLKEHLSKIAPWSEIKA 148
Cdd:cd01488   2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTP 73
 
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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