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Conserved domains on  [gi|515598585|ref|WP_017031185|]
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MULTISPECIES: tRNA cyclic N6-threonylcarbamoyladenosine(37) synthase TcdA [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15116 super family cl30839
sulfur acceptor protein CsdL; Provisional
4-266 5.04e-155

sulfur acceptor protein CsdL; Provisional


The actual alignment was detected with superfamily member PRK15116:

Pssm-ID: 185071  Cd Length: 268  Bit Score: 432.30  E-value: 5.04e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   4 LTTPASESYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGT 83
Cdd:PRK15116   1 MSVVISDAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  84 VGKSKIEVMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVD 163
Cdd:PRK15116  81 VGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 164 PTQICVADLSKTVQDPLAKKIKDQLRRFHNFSKNPKRKFAIDCVFSTEQLKYPQADGSVCAVKSTAEGPKRMDCATGFGA 243
Cdd:PRK15116 161 PTQIQVVDLAKTIQDPLAAKLRERLKSDFGVVKNSKGKLGVDCVFSTEALVYPQADGSVCAMKSTAEGPKRMDCASGFGA 240
                        250       260
                 ....*....|....*....|...
gi 515598585 244 ATVVTATFGFVAVSRIIEKLIQK 266
Cdd:PRK15116 241 ATMVTATFGFVAVSHALKKMMAK 263
 
Name Accession Description Interval E-value
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
4-266 5.04e-155

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 432.30  E-value: 5.04e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   4 LTTPASESYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGT 83
Cdd:PRK15116   1 MSVVISDAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  84 VGKSKIEVMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVD 163
Cdd:PRK15116  81 VGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 164 PTQICVADLSKTVQDPLAKKIKDQLRRFHNFSKNPKRKFAIDCVFSTEQLKYPQADGSVCAVKSTAEGPKRMDCATGFGA 243
Cdd:PRK15116 161 PTQIQVVDLAKTIQDPLAAKLRERLKSDFGVVKNSKGKLGVDCVFSTEALVYPQADGSVCAMKSTAEGPKRMDCASGFGA 240
                        250       260
                 ....*....|....*....|...
gi 515598585 244 ATVVTATFGFVAVSRIIEKLIQK 266
Cdd:PRK15116 241 ATMVTATFGFVAVSHALKKMMAK 263
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
11-268 1.18e-150

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: 420.26  E-value: 1.18e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  11 SYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIE 90
Cdd:COG1179    2 DMERRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  91 VMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVDPTQICVA 170
Cdd:COG1179   82 VMAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 171 DLSKTVQDPLAKKIKDQLRRfHNFSKNpkrkfaIDCVFSTEQLKYPQADGSVCAVkstaeGPKRMDCAtGFGAATVVTAT 250
Cdd:COG1179  162 DLSKTSNCPLAAKVRKRLRK-RGIPKG------VKVVYSTEQPRKPQADGTVCDT-----GGTGLKCA-GPGSISFVPAV 228
                        250
                 ....*....|....*...
gi 515598585 251 FGFVAVSRIIEKLIQKHS 268
Cdd:COG1179  229 FGLIAAGEVIRDLLGKAA 246
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
23-260 1.53e-114

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: 1.53e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  23 YGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPD 102
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 103 CKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVDPTQICVADLSKTVQDPLAK 182
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515598585 183 KIKDQLRRFHNFsknpkrkFAIDCVFSTEQLKYPQADGSVCAVKSTAEGPKRMDCATGFGAATVVTATFGFVAVSRII 260
Cdd:cd00755  161 KVRKRLRKRGIF-------FGVPVVYSTEPPDPPKADELVCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
31-162 4.13e-40

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: 138.93  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515598585  111 FIDQDNQAEYLsKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAG--GQV 162
Cdd:pfam00899  98 RLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGfkGQV 150
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
31-181 2.88e-27

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; 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 the Escherichia. 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 more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 104.36  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:TIGR02356  19 LLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSDIQVTALKE 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515598585  111 FIDQDNqAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVI--TIGGAGGQV-----DPTQICVADLSKTVQDPLA 181
Cdd:TIGR02356  99 RVTAEN-LELLINNVDLVLDCTDNFATRYLINDACVALGTPLIsaAVVGFGGQLmvfdpGGEGPCLRCLFPDIADTGP 175
 
Name Accession Description Interval E-value
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
4-266 5.04e-155

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 432.30  E-value: 5.04e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   4 LTTPASESYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGT 83
Cdd:PRK15116   1 MSVVISDAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  84 VGKSKIEVMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVD 163
Cdd:PRK15116  81 VGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 164 PTQICVADLSKTVQDPLAKKIKDQLRRFHNFSKNPKRKFAIDCVFSTEQLKYPQADGSVCAVKSTAEGPKRMDCATGFGA 243
Cdd:PRK15116 161 PTQIQVVDLAKTIQDPLAAKLRERLKSDFGVVKNSKGKLGVDCVFSTEALVYPQADGSVCAMKSTAEGPKRMDCASGFGA 240
                        250       260
                 ....*....|....*....|...
gi 515598585 244 ATVVTATFGFVAVSRIIEKLIQK 266
Cdd:PRK15116 241 ATMVTATFGFVAVSHALKKMMAK 263
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
11-268 1.18e-150

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: 420.26  E-value: 1.18e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  11 SYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIE 90
Cdd:COG1179    2 DMERRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  91 VMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVDPTQICVA 170
Cdd:COG1179   82 VMAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 171 DLSKTVQDPLAKKIKDQLRRfHNFSKNpkrkfaIDCVFSTEQLKYPQADGSVCAVkstaeGPKRMDCAtGFGAATVVTAT 250
Cdd:COG1179  162 DLSKTSNCPLAAKVRKRLRK-RGIPKG------VKVVYSTEQPRKPQADGTVCDT-----GGTGLKCA-GPGSISFVPAV 228
                        250
                 ....*....|....*...
gi 515598585 251 FGFVAVSRIIEKLIQKHS 268
Cdd:COG1179  229 FGLIAAGEVIRDLLGKAA 246
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
23-260 1.53e-114

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: 1.53e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  23 YGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPD 102
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585 103 CKVNLIDDFIDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVDPTQICVADLSKTVQDPLAK 182
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515598585 183 KIKDQLRRFHNFsknpkrkFAIDCVFSTEQLKYPQADGSVCAVKSTAEGPKRMDCATGFGAATVVTATFGFVAVSRII 260
Cdd:cd00755  161 KVRKRLRKRGIF-------FGVPVVYSTEPPDPPKADELVCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
31-162 4.13e-40

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: 138.93  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515598585  111 FIDQDNQAEYLsKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAG--GQV 162
Cdd:pfam00899  98 RLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGfkGQV 150
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
24-162 3.59e-39

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: 136.80  E-value: 3.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  24 GNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDC 103
Cdd:COG0476   18 GEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDV 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515598585 104 KVNLIDDFIDQDNqAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVIT--IGGAGGQV 162
Cdd:COG0476   98 EVEAIPERLTEEN-ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSgaVIGFEGQV 157
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
31-162 1.06e-33

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: 121.82  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:cd00757   19 LKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNE 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515598585 111 FIDQDNqAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVIT--IGGAGGQV 162
Cdd:cd00757   99 RLDAEN-AEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSgaVLGFEGQV 151
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
35-163 1.72e-33

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: 118.91  E-value: 1.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  35 HVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDDFIDQ 114
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515598585 115 DNQAEYLsKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVD 163
Cdd:cd01483   81 DNLDDFL-DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGD 128
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
31-181 2.88e-27

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; 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 the Escherichia. 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 more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 104.36  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:TIGR02356  19 LLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSDIQVTALKE 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515598585  111 FIDQDNqAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVI--TIGGAGGQV-----DPTQICVADLSKTVQDPLA 181
Cdd:TIGR02356  99 RVTAEN-LELLINNVDLVLDCTDNFATRYLINDACVALGTPLIsaAVVGFGGQLmvfdpGGEGPCLRCLFPDIADTGP 175
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
29-174 1.13e-25

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 100.32  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  29 EILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQiHAMTGTVGKSKIEVMAERVALINPDCKVNLI 108
Cdd:PRK08644  24 EKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMPKVEALKENLLEINPFVEIEAH 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515598585 109 DDFIDQDNQAEyLSKEFDYVLDAIDSVKAKASLLAYCRSN-KIKVITIGGAGGQVDPTQICVADLSK 174
Cdd:PRK08644 103 NEKIDEDNIEE-LFKDCDIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMAGYGDSNSIKTRRIGK 168
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
35-167 7.94e-24

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: 94.76  E-value: 7.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  35 HVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQiHAMTGTVGKSKIEVMAERVALINPDCKVNLIDDFIDQ 114
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515598585 115 DNqAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIK-VITIGGAGGQVDPTQI 167
Cdd:cd01487   80 NN-LEGLFGDCDIVVEAFDNAETKAMLAESLLGNKNKpVVCASGMAGFGDSNNI 132
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
23-138 1.30e-23

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 98.03  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  23 YGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPD 102
Cdd:PRK05600  31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPD 110
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515598585 103 CKVNLIDDFIDQDNQAEyLSKEFDYVLDAIDSVKAK 138
Cdd:PRK05600 111 IRVNALRERLTAENAVE-LLNGVDLVLDGSDSFATK 145
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
29-174 6.30e-23

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 94.14  E-value: 6.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  29 EILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLI 108
Cdd:PRK05690  28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETI 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515598585 109 DDFIDQDNQAEYLSKeFDYVLDAIDSVKAKASLLAYCRSNKIKVITiGGAG---GQV-----DPTQICVADLSK 174
Cdd:PRK05690 108 NARLDDDELAALIAG-HDLVLDCTDNVATRNQLNRACFAAKKPLVS-GAAIrmeGQVtvftyQDDEPCYRCLSR 179
PRK08223 PRK08223
hypothetical protein; Validated
11-159 8.47e-23

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 94.75  E-value: 8.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  11 SYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIE 90
Cdd:PRK08223   5 DYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAE 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515598585  91 VMAERVALINPDCKVNLIDDFIDQDNQAEYLSKEFDYVlDAID--SVKAKASLLAYCRSNKIKVITIGGAG 159
Cdd:PRK08223  85 VLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYV-DGLDffEFDARRLVFAACQQRGIPALTAAPLG 154
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
23-133 8.43e-21

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 90.32  E-value: 8.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  23 YGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPD 102
Cdd:PRK05597  18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97
                         90       100       110
                 ....*....|....*....|....*....|.
gi 515598585 103 CKVNLIDDFIDQDNQAEYLsKEFDYVLDAID 133
Cdd:PRK05597  98 VKVTVSVRRLTWSNALDEL-RDADVILDGSD 127
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-133 4.19e-17

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 80.06  E-value: 4.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:PRK08762 133 LLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQE 212
                         90       100
                 ....*....|....*....|...
gi 515598585 111 FIDQDNqAEYLSKEFDYVLDAID 133
Cdd:PRK08762 213 RVTSDN-VEALLQDVDVVVDGAD 234
PRK14851 PRK14851
hypothetical protein; Provisional
8-159 3.75e-16

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 77.98  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   8 ASESYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKS 87
Cdd:PRK14851  18 AAEYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRP 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515598585  88 KIEVMAERVALINPDCKVNLIDDFIDQDNQAEYLSkEFDYVLDAID--SVKAKASLLAYCRSNKIKVITIGGAG 159
Cdd:PRK14851  98 KLAVMKEQALSINPFLEITPFPAGINADNMDAFLD-GVDVVLDGLDffQFEIRRTLFNMAREKGIPVITAGPLG 170
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
31-133 4.34e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 77.08  E-value: 4.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:PRK07411  36 LKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYET 115
                         90       100
                 ....*....|....*....|...
gi 515598585 111 FIDQDNQAEYLsKEFDYVLDAID 133
Cdd:PRK07411 116 RLSSENALDIL-APYDVVVDGTD 137
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
31-133 7.70e-15

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 73.59  E-value: 7.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLIDD 110
Cdd:PRK07878  40 LKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEF 119
                         90       100
                 ....*....|....*....|...
gi 515598585 111 FIDQDNQAEyLSKEFDYVLDAID 133
Cdd:PRK07878 120 RLDPSNAVE-LFSQYDLILDGTD 141
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
36-164 1.30e-13

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: 69.33  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  36 VCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDckVNLI---DDFI 112
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPN--VKIVayhANIK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515598585 113 DQDNQAEYLsKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAG--GQVDP 164
Cdd:cd01489   80 DPDFNVEFF-KQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGflGQVQV 132
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
19-212 1.83e-13

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: 67.45  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  19 TRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQ--IHAMTGTVGKSKIEVMAERV 96
Cdd:cd01485    5 QIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAASYEFL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  97 ALINPDCKVNLIDDF-IDQDNQAEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVI--TIGGAGGQVDPTQICVADLS 173
Cdd:cd01485   85 QELNPNVKLSIVEEDsLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFIscATYGLIGYAFFDFPIAAFLG 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515598585 174 KTVQDPLAKKIKDQLRRFHNFsknpkrkFAIDCVFSTEQ 212
Cdd:cd01485  165 GVVAQEAIKSISGKFTPLNNL-------YIYDGFESTGP 196
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
35-160 5.50e-13

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: 67.38  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  35 HVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKV----NLIDD 110
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVtphfGKIQD 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515598585 111 FidqdNQAEYlsKEFDYVLDAIDSVKAK-------ASLLAYCRSNKIKVITIGGAGG 160
Cdd:cd01488   81 K----DEEFY--RQFNIIICGLDSIEARrwingtlVSLLLYEDPESIIPLIDGGTEG 131
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
36-159 9.37e-13

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: 66.06  E-value: 9.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  36 VCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCK-------VNLI 108
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKvvpyqnkVGPE 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515598585 109 DDFIDQdnqaeyLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAG 159
Cdd:cd01484   82 QDFNDT------FFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEG 126
PRK14852 PRK14852
hypothetical protein; Provisional
16-159 1.52e-12

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 67.41  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  16 FGGTRRLygnseveiLRAaHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAER 95
Cdd:PRK14852 324 YAGQRRL--------LRS-RVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515598585  96 VALINPDCKVNLIDDFIDQDNQAEYLsKEFDYVLDAID--SVKAKASLLAYCRSNKIKVITIGGAG 159
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETIDAFL-KDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLG 459
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
21-156 8.58e-11

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 59.61  E-value: 8.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  21 RLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALIN 100
Cdd:cd01492    9 RLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALN 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515598585 101 PDCKVNLIDDFIDQDNQaEYLSKeFDYVLDAIDSVKAKASLLAYCRSNKIKVITIG 156
Cdd:cd01492   89 PRVKVSVDTDDISEKPE-EFFSQ-FDVVVATELSRAELVKINELCRKLGVKFYATG 142
PRK08328 PRK08328
hypothetical protein; Provisional
9-162 8.63e-11

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 60.19  E-value: 8.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585   9 SESYDQRFGGTRRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSK 88
Cdd:PRK08328   3 SERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNP 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515598585  89 IEVMAE-RVALINPDCKVNLIDDFIDQDNQAEYLsKEFDYVLDAIDSVKAKASLLAYCRSNKIKVI--TIGGAGGQV 162
Cdd:PRK08328  83 KPLSAKwKLERFNSDIKIETFVGRLSEENIDEVL-KGVDVIVDCLDNFETRYLLDDYAHKKGIPLVhgAVEGTYGQV 158
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
35-138 5.74e-10

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: 59.23  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  35 HVCVIGIGGVG-----SWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALINPDCKVNLID 109
Cdd:cd01490    1 KVFLVGAGAIGcellkNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515598585 110 DFIDQDNQAEYlSKEF----DYVLDAIDSVKAK 138
Cdd:cd01490   81 NRVGPETEHIF-NDEFweklDGVANALDNVDAR 112
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
11-133 9.40e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 58.20  E-value: 9.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  11 SYDQRFGGTrrlyGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIE 90
Cdd:PRK12475   6 SRQILFSGI----GEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKPK 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515598585  91 VMA--ERVALINPDCKVN-LIDDFIDQDnqAEYLSKEFDYVLDAID 133
Cdd:PRK12475  82 AIAakEHLRKINSEVEIVpVVTDVTVEE--LEELVKEVDLIIDATD 125
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
15-184 1.54e-09

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: 58.36  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585    15 RFGGTRRLYGNSEVEILRAAHVCVIGIGGVG-----SWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKI 89
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGcemlkNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585    90 EVMAERVALINPDCKVNLIDDFIDQDNQAEYlSKEF----DYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVDpT 165
Cdd:TIGR01408  481 YTAADATLKINPQIKIDAHQNRVGPETETIF-NDEFyeklDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGN-T 558
                          170       180
                   ....*....|....*....|..
gi 515598585   166 QICVADLSKTV---QDPLAKKI 184
Cdd:TIGR01408  559 QVVVPHLTESYgssRDPPEKEI 580
PRK07877 PRK07877
Rv1355c family protein;
26-163 4.50e-09

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 56.92  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  26 SEVEILRAAHVCVIGIGgVGSWAVEALARSGV-GELTLIDMDDVCVTNINRqIHAMTGTVGKSKIEVMAERVALINPDCK 104
Cdd:PRK07877 100 EEQERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDPYLP 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515598585 105 VNLIDDFIDQDNQAEYLSkEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIGGAGGQVD 163
Cdd:PRK07877 178 VEVFTDGLTEDNVDAFLD-GLDVVVEECDSLDVKVLLREAARARRIPVLMATSDRGLLD 235
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
31-76 1.91e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 54.23  E-value: 1.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQ 76
Cdd:PRK07688  22 LREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQ 67
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
20-153 1.11e-07

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: 51.88  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  20 RRLY--GNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVA 97
Cdd:cd01491    4 RQLYvlGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLA 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515598585  98 LINPDCKVNLIDDFIDQDnqaeYLSKEFDYVLDAIDSVKAKaSLLAYCRSNKIKVI 153
Cdd:cd01491   84 ELNPYVPVTVSTGPLTTD----ELLKFQVVVLTDASLEDQL-KINEFCHSPGIKFI 134
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
21-159 3.22e-06

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 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. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 47.68  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  21 RLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLID-----MDDVCVtniNRQIHAmtGTVGKSKIEVMAER 95
Cdd:cd01493    8 RLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDgskvdEEDLGN---NFFLDA--SSLGKSRAEATCEL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515598585  96 VALINPDckVNliDDFIDQ------DNQAEYLSKeFDYVLDAIDSVKAKASLLAYCRSNKIKVI---TIGGAG 159
Cdd:cd01493   83 LQELNPD--VN--GSAVEEspeallDNDPSFFSQ-FTVVIATNLPESTLLRLADVLWSANIPLLyvrSYGLYG 150
PRK06153 PRK06153
hypothetical protein; Provisional
31-156 9.65e-06

hypothetical protein; Provisional


Pssm-ID: 235717 [Multi-domain]  Cd Length: 393  Bit Score: 46.12  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585  31 LRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINR---QIHAMTGTVGKSKIEVMAERVAliNPDCKVNL 107
Cdd:PRK06153 174 LEGQRIAIIGLGGTGSYILDLVAKTPVREIHLFDGDDFLQHNAFRspgAASIEELREAPKKVDYFKSRYS--NMRRGIVP 251
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515598585 108 IDDFIDQDNqaEYLSKEFDYVLDAIDSVKAKASLLAYCRSNKIKVITIG 156
Cdd:PRK06153 252 HPEYIDEDN--VDELDGFTFVFVCVDKGSSRKLIVDYLEALGIPFIDVG 298
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
20-148 9.99e-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: 40.26  E-value: 9.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515598585    20 RRLYGNSEVEILRAAHVCVIGIGGVGSWAVEALARSGVGELTLIDMDDVCVTNINRQIHAMTGTVGKSKIEVMAERVALI 99
Cdd:TIGR01408   11 LYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAEL 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 515598585   100 NPDCKVNLIDDFIDQdnqaEYLSKeFDYVLDAIDSVKAKASLLAYCRSN 148
Cdd:TIGR01408   91 NPYVHVSSSSVPFNE----EFLDK-FQCVVLTEMSLPLQKEINDFCHSQ 134
 
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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