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Conserved domains on  [gi|299788289|gb|AAS54424|]
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AGL066Wp [Eremothecium gossypii ATCC 10895]

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 ...
 76-317 1.49e-111

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: 328.03  E-value: 1.49e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 156 CEIEAVNELWHIDSAERLIFGNdgqdkPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTRINVGDLSTTEE 235
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGD-----PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 236 DSLSRSVRRRLKQRGITKGIPVVFSAEKPDPKKAKLLPLPEEqylmgkVDELSALKDFRVRVLPVLGTMPGVFGLTIATW 315
Cdd:cd00755  156 DPLARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASE 229


                 ..
gi 299788289 316 VL 317
Cdd:cd00755  230 VI 231
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 76-317 1.49e-111

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: 328.03  E-value: 1.49e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 156 CEIEAVNELWHIDSAERLIFGNdgqdkPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTRINVGDLSTTEE 235
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGD-----PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 236 DSLSRSVRRRLKQRGITKGIPVVFSAEKPDPKKAKLLPLPEEqylmgkVDELSALKDFRVRVLPVLGTMPGVFGLTIATW 315
Cdd:cd00755  156 DPLARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASE 229


                 ..
gi 299788289 316 VL 317
Cdd:cd00755  230 VI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 65-322 3.82e-76

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: 238.06  E-value: 3.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  65 YREQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEV 144
Cdd:COG1179    3 MERRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 145 LKSHLLKIAPWCEIEAVNELWHIDSAERLIFgndgqDKPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTR 224
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLS-----EDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 225 INVGDLSTTEEDSLSRSVRRRLKQRGITKGIPVVFSAEKPDPkkakllPLPEEQYLMGKVDELSAlkdfrvrvlPVLGT- 303
Cdd:COG1179  158 IRVADLSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRK------PQADGTVCDTGGTGLKC---------AGPGSi 222

                        250       260
                 ....*....|....*....|.
gi 299788289 304 --MPGVFGLTIATWVLCSIAG 322
Cdd:COG1179  223 sfVPAVFGLIAAGEVIRDLLG 243
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 65-339 4.73e-56

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: 185.54  E-value: 4.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289   65 YREQLArnYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEV 144
Cdd:pfam00899   1 YSRQLA--LPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  145 LKSHLLKIAPWCEIEAVNELWHIDSAERLIFgndgqdKPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTR 224
Cdd:pfam00899  79 AAERLREINPDVEVEAYTERLTPENAEELIK------SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  225 INVGDlSTTEEDSLSRSVRRRLKQRGITKGIpvvfsaekpdpkkakllplpeeqylmgkvdelsalkdfrvrvlpvLGTM 304
Cdd:pfam00899 153 VIPGK-TPCYRCLFPEDPPPKLVPSCTVAGV---------------------------------------------LGPT 186

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 299788289  305 PGVFGLTIATWVLCSIAGYPMEPIegKNRIKLYDG 339
Cdd:pfam00899 187 TAVVAGLQALEALKLLLGKGEPNL--AGRLLQFDA 219
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 63-262 3.39e-37

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 136.86  E-value: 3.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  63 ELYREQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKV 142
Cdd:PRK15116   7 DAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 143 EVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkpTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDP 222
Cdd:PRK15116  87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF-----SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 299788289 223 TRINVGDLSTTEEDSLSRSVRRRLKQR-GITK------GIPVVFSAE 262
Cdd:PRK15116 162 TQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVDCVFSTE 208
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 76-212 2.95e-23

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: 97.04  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289   76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:TIGR02356  11 IGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289  156 CEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLIS 212
Cdd:TIGR02356  91 IQVTALKERVTAENLELLINNVD------LVLDCTDNFATRYLINDACVALGTPLIS 141
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 76-317 1.49e-111

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: 328.03  E-value: 1.49e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 156 CEIEAVNELWHIDSAERLIFGNdgqdkPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTRINVGDLSTTEE 235
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGD-----PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 236 DSLSRSVRRRLKQRGITKGIPVVFSAEKPDPKKAKLLPLPEEqylmgkVDELSALKDFRVRVLPVLGTMPGVFGLTIATW 315
Cdd:cd00755  156 DPLARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASE 229


                 ..
gi 299788289 316 VL 317
Cdd:cd00755  230 VI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 65-322 3.82e-76

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: 238.06  E-value: 3.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  65 YREQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEV 144
Cdd:COG1179    3 MERRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 145 LKSHLLKIAPWCEIEAVNELWHIDSAERLIFgndgqDKPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTR 224
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLS-----EDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 225 INVGDLSTTEEDSLSRSVRRRLKQRGITKGIPVVFSAEKPDPkkakllPLPEEQYLMGKVDELSAlkdfrvrvlPVLGT- 303
Cdd:COG1179  158 IRVADLSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRK------PQADGTVCDTGGTGLKC---------AGPGSi 222

                        250       260
                 ....*....|....*....|.
gi 299788289 304 --MPGVFGLTIATWVLCSIAG 322
Cdd:COG1179  223 sfVPAVFGLIAAGEVIRDLLG 243
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 65-339 4.73e-56

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: 185.54  E-value: 4.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289   65 YREQLArnYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEV 144
Cdd:pfam00899   1 YSRQLA--LPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  145 LKSHLLKIAPWCEIEAVNELWHIDSAERLIFgndgqdKPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTR 224
Cdd:pfam00899  79 AAERLREINPDVEVEAYTERLTPENAEELIK------SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  225 INVGDlSTTEEDSLSRSVRRRLKQRGITKGIpvvfsaekpdpkkakllplpeeqylmgkvdelsalkdfrvrvlpvLGTM 304
Cdd:pfam00899 153 VIPGK-TPCYRCLFPEDPPPKLVPSCTVAGV---------------------------------------------LGPT 186

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 299788289  305 PGVFGLTIATWVLCSIAGYPMEPIegKNRIKLYDG 339
Cdd:pfam00899 187 TAVVAGLQALEALKLLLGKGEPNL--AGRLLQFDA 219
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 89-234 5.20e-38

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: 135.09  E-value: 5.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  89 FIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPWCEIEAVNElwHID 168
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPE--GIS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299788289 169 SAERLIFGndgqDKPTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDPTRINVGDLSTTE 234
Cdd:cd01483   80 EDNLDDFL----DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAAE 141
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 63-262 3.39e-37

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 136.86  E-value: 3.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  63 ELYREQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKV 142
Cdd:PRK15116   7 DAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 143 EVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkpTFVIDCIDNISTKVDLLEYVYRKGIPLISSMGAATKSDP 222
Cdd:PRK15116  87 EVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF-----SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 299788289 223 TRINVGDLSTTEEDSLSRSVRRRLKQR-GITK------GIPVVFSAE 262
Cdd:PRK15116 162 TQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVDCVFSTE 208
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 61-217 1.19e-34

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: 129.09  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  61 DEELYReqLARNYAF--LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVG 138
Cdd:COG0476    2 DEELER--YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299788289 139 HSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLISsmGAA 217
Cdd:COG0476   80 RPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGAD------LVLDCTDNFATRYLLNDACVKLGIPLVS--GAV 150
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 76-217 6.38e-29

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: 113.34  E-value: 6.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:cd00757   11 IGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPD 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299788289 156 CEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLISsmGAA 217
Cdd:cd00757   91 VEIEAYNERLDAENAEELIAGYD------LVLDCTDNFATRYLINDACVKLGKPLVS--GAV 144
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 76-212 2.95e-23

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: 97.04  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289   76 LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPW 155
Cdd:TIGR02356  11 IGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289  156 CEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLIS 212
Cdd:TIGR02356  91 IQVTALKERVTAENLELLINNVD------LVLDCTDNFATRYLINDACVALGTPLIS 141
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
62-217 7.58e-23

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 96.08  E-value: 7.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  62 EELYREQLARnyafLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHScATLNDVGHSK 141
Cdd:PRK08644   8 EEFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQ-YFISQIGMPK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 142 VEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRK-GIPLISSMGAA 217
Cdd:PRK08644  83 VEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDCD------IVVEAFDNAETKAMLVETVLEHpGKKLVAASGMA 153
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 91-225 5.36e-20

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: 87.05  E-value: 5.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  91 VVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHScATLNDVGHSKVEVLKSHLLKIAPWCEIEAVNELWHIDSA 170
Cdd:cd01487    4 IAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299788289 171 ERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYR-KGIPLISSMGAATKSDPTRI 225
Cdd:cd01487   83 EGLFGDCD------IVVEAFDNAETKAMLAESLLGnKNKPVVCASGMAGFGDSNNI 132
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 61-217 4.49e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 80.27  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  61 DEEL--YREQ-LARNYAFlgeDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDV 137
Cdd:PRK05690   7 DEEMlrYNRQiILRGFDF---DGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 138 GHSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLISsmGAA 217
Cdd:PRK05690  84 GQPKVESARAALARINPHIAIETINARLDDDELAALIAGHD------LVLDCTDNVATRNQLNRACFAAKKPLVS--GAA 155
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 62-225 3.11e-13

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 68.36  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289   62 EELYREQLARNyaflGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHScATLNDVGHSK 141
Cdd:TIGR02354   1 EEFRRALVARH----TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQ-YKASQVGEPK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  142 VEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYR--KGIPLISSMGAATK 219
Cdd:TIGR02354  76 TEALKENISEINPYTEIEAYDEKITEENIDKFFKDAD------IVCEAFDNAEAKAMLVNAVLEkyKDKYLIAASGLAGY 149


                  ....*.
gi 299788289  220 SDPTRI 225
Cdd:TIGR02354 150 DDANSI 155
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 66-220 1.09e-12

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 68.87  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  66 REQLarnYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDV--GHSKVE 143
Cdd:PRK07688   7 RQEL---FSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKAV 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 144 VLKSHLLKIAPWCEIEAVNELWHIDSAERLIfgnDGQDkptFVIDCIDNISTKVDLLEYVYRKGIPLIssMGAATKS 220
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELV---TGVD---LIIDATDNFETRFIVNDAAQKYGIPWI--YGACVGS 152
PRK08223 PRK08223
hypothetical protein; Validated
 64-217 1.10e-12

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 68.17  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  64 LYREQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVE 143
Cdd:PRK08223   5 DYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 144 VLKSHLLKIAPWCEIEAVNELWHIDSAERLIfgnDGQDkptFVIDCIDNIStkVDLLEYVY----RKGIPLISS----MG 215
Cdd:PRK08223  85 VLAEMVRDINPELEIRAFPEGIGKENADAFL---DGVD---VYVDGLDFFE--FDARRLVFaacqQRGIPALTAaplgMG 156


                 ..
gi 299788289 216 AA 217
Cdd:PRK08223 157 TA 158
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 63-211 1.14e-12

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 69.14  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  63 ELYREQLARNYAF--LGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHS 140
Cdd:PRK05600  16 TSELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRP 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299788289 141 KVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:PRK05600  96 KVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVD------LVLDGSDSFATKFLVADAAEITGTPLV 160
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
77-213 1.87e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.42  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  77 GEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPWC 156
Cdd:PRK08762 126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDV 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 157 EIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLISS 213
Cdd:PRK08762 206 QVEAVQERVTSDNVEALLQDVD------VVVDGADNFPTRYLLNDACVKLGKPLVYG 256
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 65-209 1.92e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 65.28  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  65 YREQLArnYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNR---HSCATlndVGHSK 141
Cdd:PRK05597   9 YRRQIM--LGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRqviHSTAG---VGQPK 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299788289 142 VEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIP 209
Cdd:PRK05597  84 AESAREAMLALNPDVKVTVSVRRLTWSNALDELRDAD------VILDGSDNFDTRHLASWAAARLGIP 145
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 90-211 1.44e-10

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: 61.99  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  90 IVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPWCEIEAVNelwhids 169
Cdd:cd01488    3 LVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHF------- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 170 aerlifgNDGQDKP-------TFVIDCIDNI-------STKVDLLEYV-YRKGIPLI 211
Cdd:cd01488   76 -------GKIQDKDeefyrqfNIIICGLDSIearrwinGTLVSLLLYEdPESIIPLI 125
PRK08328 PRK08328
hypothetical protein; Provisional
 67-211 1.69e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 60.97  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  67 EQLARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVG-HSKVEVL 145
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGkNPKPLSA 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299788289 146 KSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:PRK08328  88 KWKLERFNSDIKIETFVGRLSEENIDEVLKGVD------VIVDCLDNFETRYLLDDYAHKKGIPLV 147
PRK14851 PRK14851
hypothetical protein; Provisional
 54-213 4.91e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 61.80  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  54 IRESRAYDEELYreqlARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCAT 133
Cdd:PRK14851  15 ISSAAEYREAAF----SRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGAR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 134 LNDVGHSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKV--DLLEYVYRKGIPLI 211
Cdd:PRK14851  91 VPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGVD------VVLDGLDFFQFEIrrTLFNMAREKGIPVI 164


                 ..
gi 299788289 212 SS 213
Cdd:PRK14851 165 TA 166
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 62-196 1.35e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 59.72  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  62 EELYREQLARNYAFL-----GEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLND 136
Cdd:PRK07878  13 AELTRDEVARYSRHLiipdvGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 137 VGHSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTK 196
Cdd:PRK07878  93 VGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYD------LILDGTDNFATR 146
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 62-211 1.48e-09

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 59.36  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  62 EELY-REQLarnYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHS 140
Cdd:PRK12475   2 QERYsRQIL---FSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQK 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299788289 141 KVEVL--KSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:PRK12475  79 KPKAIaaKEHLRKINSEVEIVPVVTDVTVEELEELVKEVD------LIIDATDNFDTRLLINDLSQKYNIPWI 145
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 90-213 5.65e-09

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: 57.39  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  90 IVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPWCEIEAvnelwHIDS 169
Cdd:cd01489    3 LVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVA-----YHAN 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 299788289 170 AERLIFGNDGQDKPTFVIDCIDNISTKvdllEYVYR----KGIPLISS 213
Cdd:cd01489   78 IKDPDFNVEFFKQFDLVFNALDNLAAR----RHVNKmclaADVPLIES 121
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
63-196 1.98e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 55.90  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  63 ELYREQLARNYAFL-----GEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDV 137
Cdd:PRK07411  10 QLSKDEYERYSRHLilpevGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299788289 138 GHSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCIDNISTK 196
Cdd:PRK07411  90 GKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYD------VVVDGTDNFPTR 142
PRK14852 PRK14852
hypothetical protein; Provisional
 69-213 4.48e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 52.39  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  69 LARNYAFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSH 148
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 149 LLKIAPWCEIEAVNELWHIDSAERLIFGNDgqdkptFVIDCID--NISTKVDLLEYVYRKGIPLISS 213
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETIDAFLKDVD------LLVDGIDffALDIRRRLFNRALELGIPVITA 455
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 90-219 4.85e-07

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: 50.65  E-value: 4.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  90 IVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSHLLKIAPWCEIEAVNELWHIDS 169
Cdd:cd01484    3 LLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQ 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299788289 170 aerlIFGNDGQDKPTFVIDCIDNISTKvdllEYVYRKGI----PLISSMGAATK 219
Cdd:cd01484   83 ----DFNDTFFEQFHIIVNALDNIIAR----RYVNGMLIflivPLIESGTEGFK 128
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 60-212 5.35e-05

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: 43.95  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  60 YDEELYreqlarnyaFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVS---LSS---LNRHScat 133
Cdd:cd01485    2 YDRQIR---------LWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVStedLGSnffLDAEV--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289 134 lNDVGHSKVEVLKSHLLKIAPWCEIEAVNELwhidsaERLIFGNDGQ--DKPTFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:cd01485   70 -SNSGMNRAAASYEFLQELNPNVKLSIVEED------SLSNDSNIEEylQKFTLVIATEENYERTAKVNDVCRKHHIPFI 142


                 .
gi 299788289 212 S 212
Cdd:cd01485  143 S 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 74-219 7.84e-05

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: 45.26  E-value: 7.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289    74 AFLGEDGMARLQEQYFIVVGAGGVG-----SWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVEVLKSH 148
Cdd:TIGR01408  407 AVFGDTFQQKLQNLNIFLVGCGAIGcemlkNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADA 486

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299788289   149 LLKIAPWCEIEAVNElwHIDSAERLIFGNDGQDKPTFVIDCIDNISTKVdlleYVYRKGI----PLISSMGAATK 219
Cdd:TIGR01408  487 TLKINPQIKIDAHQN--RVGPETETIFNDEFYEKLDVVINALDNVEARR----YVDSRCLaflkPLLESGTLGTK 555
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 61-164 9.32e-05

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: 44.88  E-value: 9.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289    61 DEELYREQLArnyaFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHS 140
Cdd:TIGR01408    3 DEALYSRQLY----VLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRN 78

                           90       100
                   ....*....|....*....|....
gi 299788289   141 KVEVLKSHLLKIAPWCEIEAVNEL 164
Cdd:TIGR01408   79 RAEAVVKKLAELNPYVHVSSSSVP 102
PRK06153 PRK06153
hypothetical protein; Provisional
 82-211 1.27e-03

hypothetical protein; Provisional


Pssm-ID: 235717 [Multi-domain]  Cd Length: 393  Bit Score: 40.72  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  82 ARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRH-SCATLNDVG--HSKVEVLKSHLLKiapwcei 158
Cdd:PRK06153 172 AKLEGQRIAIIGLGGTGSYILDLVAKTPVREIHLFDGDDFLQHNAFRSpGAASIEELReaPKKVDYFKSRYSN------- 244

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299788289 159 eavnelWH---IDSAERLIFGNDGQ-DKPTFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:PRK06153 245 ------MRrgiVPHPEYIDEDNVDElDGFTFVFVCVDKGSSRKLIVDYLEALGIPFI 295
PRK07877 PRK07877
Rv1355c family protein;
61-211 1.46e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 41.13  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  61 DEELYRE-QLARNYAFLGEDGMARLQEQYFIVVGAGgVGSWVVTMLVRSG-CRKIKVIDFDQVSLSSLNRHScATLNDVG 138
Cdd:PRK07877  81 GPREFRAvRLDRNRNKITAEEQERLGRLRIGVVGLS-VGHAIAHTLAAEGlCGELRLADFDTLELSNLNRVP-AGVFDLG 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299788289 139 HSKVEVLKSHLLKIAPWCEIEAVNELWHIDSAERLIfgnDGQDkptFVIDCIDNISTKVDLLEYVYRKGIPLI 211
Cdd:PRK07877 159 VNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFL---DGLD---VVVEECDSLDVKVLLREAARARRIPVL 225
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 64-149 1.68e-03

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: 40.33  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299788289  64 LYREQLArnyaFLGEDGMARLQEQYFIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDVGHSKVE 143
Cdd:cd01491    1 LYSRQLY----VLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76


                 ....*.
gi 299788289 144 VLKSHL 149
Cdd:cd01491   77 ASQARL 82
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 89-162 2.14e-03

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 40.05  E-value: 2.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299788289  89 FIVVGAGGVGSWVVTMLVRSGCRKIKVIDFDQVSLSSLNRHSCATLNDV--GHSKVEVLKSHLLKIAPWCEIEAVN 162
Cdd:cd01486    2 CLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIV 77
 
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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