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Conserved domains on  [gi|767924523|ref|XP_011532512|]
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NEDD8-activating enzyme E1 catalytic subunit isoform X1 [Homo sapiens]

Protein Classification

NEDD8-activating enzyme E1 catalytic subunit( domain architecture ID 10107293)

NEDD8-activating enzyme E1 catalytic subunit activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP

CATH:  3.10.20.260|1.10.10.520|3.40.50.720
EC:  6.2.1.64
Gene Ontology:  GO:0005524|GO:0005515|GO:0019781|GO:0019788|GO:0006508|GO:0045116
SCOP:  4000345|4004110

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 62-341 0e+00

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: 575.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 141
Cdd:cd01488   19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 142 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 221
Cdd:cd01488   99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 222 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 301
Cdd:cd01488  175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767924523 302 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 341
Cdd:cd01488  252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 349-434 4.05e-32

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


:

Pssm-ID: 462611  Cd Length: 81  Bit Score: 116.84  E-value: 4.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  349 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 428
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 767924523  429 LFKLHF 434
Cdd:pfam08825  76 SLRLRF 81
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 62-341 0e+00

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: 575.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 141
Cdd:cd01488   19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 142 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 221
Cdd:cd01488   99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 222 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 301
Cdd:cd01488  175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767924523 302 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 341
Cdd:cd01488  252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 62-214 7.39e-46

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: 158.57  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-QDFNDTFYRQFHIIVCGLD 140
Cdd:pfam00899  40 ARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATD 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924523  141 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIAS 214
Cdd:pfam00899 120 NFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLFPEDPPPKLVPSCTVAG 181
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-342 1.59e-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: 128.71  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:COG0476   47 AAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLDCTD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 141 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYPpqvnfpmctiasmprlpe 220
Cdd:COG0476  127 NFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP------------------ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 221 hcieyvrmlqwpkeqpfgegvpldgDDPEhiqwifqkslerasqynirgvtyrltQGVVKRIIPAVASTNAVIAAVCATE 300
Cdd:COG0476  174 -------------------------EPPE--------------------------PGPSCAEAGVLGPLVGVIGSLQATE 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767924523 301 VFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 342
Cdd:COG0476  203 AIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 349-434 4.05e-32

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


Pssm-ID: 462611  Cd Length: 81  Bit Score: 116.84  E-value: 4.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  349 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 428
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 767924523  429 LFKLHF 434
Cdd:pfam08825  76 SLRLRF 81
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 68-394 2.10e-29

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: 121.53  E-value: 2.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523    68 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSI 142
Cdd:TIGR01408  450 MITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNV 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   143 IARRWINGMLISLLNyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 217
Cdd:TIGR01408  530 EARRYVDSRCLAFLK------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPA 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   218 LPEHCIEYVR-MLQWPKEQPFGEgVPLDGDDPEHiqwiFQKSLERASQYNIRGVTYRLTQGVVKRiipavastnaviaav 296
Cdd:TIGR01408  591 AIEHTIQWARdKFEGLFSHKPSL-VNKYLSSPSS----AEEVLQKIQSGHSREGLEQIIKLLSKE--------------- 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   297 cATEVFK-IATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCP---ACSQLPQNIQFSPSAKlqEVLDYLTNSASLQMKS 372
Cdd:TIGR01408  651 -KPRNFSqCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPfwsSPKRPPSPLKFDLNEP--LHLSFIQAAAKLYATV 727

                          330       340
                   ....*....|....*....|..
gi 767924523   373 PAITATLEGKNRTLYLQSVTSI 394
Cdd:TIGR01408  728 YGIPFAEEDLSADALLNILSEV 749
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
64-148 7.18e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 58.71  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  64 SGFRQIHVIDMDTIDVSNLNRQFLFrPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 142
Cdd:PRK08644  50 SGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNiEELFKDCDIVVEAFDNA 128


                 ....*.
gi 767924523 143 IARRWI 148
Cdd:PRK08644 129 ETKAML 134
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 62-341 0e+00

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: 575.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 141
Cdd:cd01488   19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 142 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 221
Cdd:cd01488   99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 222 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 301
Cdd:cd01488  175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767924523 302 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 341
Cdd:cd01488  252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 62-302 4.41e-131

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: 377.30  E-value: 4.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI---QDFNDTFYRQFHIIVCG 138
Cdd:cd01484   19 ALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVgpeQDFNDTFFEQFHIIVNA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 139 LDSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTleLYPPQVNFPMCTIASMPRL 218
Cdd:cd01484   99 LDNIIARRYVNGMLIFL------------IVPLIESGTEGFKGNAQVILPGMTECIECT--LYPPQKNFPMCTIASMPRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 219 PEHCIEYVRMLQWpkeqpfgegvpldgDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCA 298
Cdd:cd01484  165 PEHCIEWARMLQW--------------DDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCA 230


                 ....
gi 767924523 299 TEVF 302
Cdd:cd01484  231 LEVF 234
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 62-304 8.90e-60

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: 197.60  E-value: 8.90e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD--FNDTFYRQFHIIVCGL 139
Cdd:cd01489   19 VLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdFNVEFFKQFDLVFNAL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 140 DSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTLElyPPQVNFPMCTIASMPRLP 219
Cdd:cd01489   99 DNLAARRHVNKMCLAA------------DVPLIESGTTGFLGQVQVIKKGKTECYECQPK--ETPKTFPVCTIRSTPSQP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 220 EHC------------------IEYVRMLQ--WPKEQPfgeGVPL-------DGDDPEHIQWIFQKSLERASQYNIRGVTY 272
Cdd:cd01489  165 IHCivwakslfflfnkvfkddIERLLSMEelWKTRKP---PVPLswkeltfDKDDQDALDFVAAAANLRSHVFGIPMKSR 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767924523 273 RLTQGVVKRIIPAVASTNAVIAAVCATEVFKI 304
Cdd:cd01489  242 FDIKQMAGNIIPAIATTNAIIAGLIVLEALKV 273
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 62-214 7.39e-46

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: 158.57  E-value: 7.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-QDFNDTFYRQFHIIVCGLD 140
Cdd:pfam00899  40 ARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATD 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924523  141 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIAS 214
Cdd:pfam00899 120 NFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLFPEDPPPKLVPSCTVAG 181
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 68-304 5.87e-39

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: 145.51  E-value: 5.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  68 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-----QDFNDTFYRQFHIIVCGLDSI 142
Cdd:cd01490   30 EITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpeteHIFNDEFWEKLDGVANALDNV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 143 IARRWINGMLISllnYEDgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 217
Cdd:cd01490  110 DARMYVDRRCVY---YRK---------PLLESGTLGTKGNTQVVIPHLT-------ESYsssrdPPEKSIPLCTLKNFPN 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 218 LPEHCIEYVR---------------MLQW--------------------------PKE------QPFGEG-----VPL-- 243
Cdd:cd01490  171 AIEHTIQWARdefeglfkqppenvnQYLFedcvrwarllfekyfnnnikqllhnfPPDavtsdgAPFWSGpkrcpTPLef 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 244 DGDDPEHIQWI---------------FQK--------------SLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIA 294
Cdd:cd01490  251 DVNNPLHLDFVlaaanlyaevygipgFEKdddtnfhmdfitaaSNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVT 330

                        330
                 ....*....|
gi 767924523 295 AVCATEVFKI 304
Cdd:cd01490  331 GLVCLELYKV 340
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 62-196 6.08e-36

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: 129.31  E-value: 6.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:cd01483   19 ARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNlDDFLDGVDLVIDAID 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767924523 141 SIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIEC 196
Cdd:cd01483   99 NIAVRRALNRACKEL------------GIPVIDAGGLGLGGDIQVIDIGSLSAAEA 142
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-342 1.59e-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: 128.71  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:COG0476   47 AAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLDCTD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 141 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYPpqvnfpmctiasmprlpe 220
Cdd:COG0476  127 NFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP------------------ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 221 hcieyvrmlqwpkeqpfgegvpldgDDPEhiqwifqkslerasqynirgvtyrltQGVVKRIIPAVASTNAVIAAVCATE 300
Cdd:COG0476  174 -------------------------EPPE--------------------------PGPSCAEAGVLGPLVGVIGSLQATE 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 767924523 301 VFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 342
Cdd:COG0476  203 AIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 349-434 4.05e-32

E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like protein transfer cascades. This is an E2 binding domain that is found on NEDD8 activating E1 enzyme. The domain resembles ubiquitin, and recruits the catalytic core of the E2 enzyme Ubc12 in a similar manner to that in which ubiquitin interacts with ubiquitin binding domains.


Pssm-ID: 462611  Cd Length: 81  Bit Score: 116.84  E-value: 4.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  349 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 428
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 767924523  429 LFKLHF 434
Cdd:pfam08825  76 SLRLRF 81
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 68-394 2.10e-29

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: 121.53  E-value: 2.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523    68 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSI 142
Cdd:TIGR01408  450 MITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNV 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   143 IARRWINGMLISLLNyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 217
Cdd:TIGR01408  530 EARRYVDSRCLAFLK------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPA 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   218 LPEHCIEYVR-MLQWPKEQPFGEgVPLDGDDPEHiqwiFQKSLERASQYNIRGVTYRLTQGVVKRiipavastnaviaav 296
Cdd:TIGR01408  591 AIEHTIQWARdKFEGLFSHKPSL-VNKYLSSPSS----AEEVLQKIQSGHSREGLEQIIKLLSKE--------------- 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523   297 cATEVFK-IATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCP---ACSQLPQNIQFSPSAKlqEVLDYLTNSASLQMKS 372
Cdd:TIGR01408  651 -KPRNFSqCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPfwsSPKRPPSPLKFDLNEP--LHLSFIQAAAKLYATV 727

                          330       340
                   ....*....|....*....|..
gi 767924523   373 PAITATLEGKNRTLYLQSVTSI 394
Cdd:TIGR01408  728 YGIPFAEEDLSADALLNILSEV 749
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 64-213 5.10e-26

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: 105.25  E-value: 5.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  64 SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 142
Cdd:cd00757   43 AGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENaEELIAGYDLVLDCTDNF 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924523 143 IARRWINgMLISLLNyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELyPPQVNFPMCTIA 213
Cdd:cd00757  123 ATRYLIN-DACVKLG-----------KPLVSGAVLGFEGQVTVFIPGEGPCYRCLFPE-PPPPGVPSCAEA 180
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 61-144 6.17e-14

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: 70.71  E-value: 6.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  61 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN--DTFYRQFHIIV 136
Cdd:cd00755   28 EALarSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTPDNseDLLGGDPDFVV 107


                 ....*...
gi 767924523 137 CGLDSIIA 144
Cdd:cd00755  108 DAIDSIRA 115
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 61-124 1.86e-10

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


Pssm-ID: 440792  Cd Length: 247  Bit Score: 60.87  E-value: 1.86e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  61 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEflndRV----PNCNVvphfNKIQDF 124
Cdd:COG1179   41 EALarSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAE----RIrdinPDCEV----TAIDEF 102
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
64-148 7.18e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 58.71  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  64 SGFRQIHVIDMDTIDVSNLNRQFLFrPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 142
Cdd:PRK08644  50 SGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNiEELFKDCDIVVEAFDNA 128


                 ....*.
gi 767924523 143 IARRWI 148
Cdd:PRK08644 129 ETKAML 134
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 62-121 7.70e-10

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 60.28  E-value: 7.70e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI 121
Cdd:PRK05600  61 ASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERL 120
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 62-149 1.43e-08

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 55.24  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:PRK05690  52 AAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDElAALIAGHDLVLDCTD 131


                 ....*....
gi 767924523 141 SIIARRWIN 149
Cdd:PRK05690 132 NVATRNQLN 140
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 62-149 2.86e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 55.48  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN--DTFyRQFHIIVCGL 139
Cdd:PRK07878  62 AAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNavELF-SQYDLILDGT 140

                         90
                 ....*....|
gi 767924523 140 DSIIARRWIN 149
Cdd:PRK07878 141 DNFATRYLVN 150
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 62-145 4.23e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 54.88  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFND-TFYRQFHIIVCGLD 140
Cdd:PRK05597  48 AGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVSVRRLTWSNAlDELRDADVILDGSD 127


                 ....*
gi 767924523 141 SIIAR 145
Cdd:PRK05597 128 NFDTR 132
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 62-148 6.00e-08

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: 52.38  E-value: 6.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:cd01487   19 ARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNlEGLFGDCDIVVEAFD 97


                 ....*...
gi 767924523 141 SIIARRWI 148
Cdd:cd01487   98 NAETKAML 105
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
62-202 7.96e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 53.86  E-value: 7.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 140
Cdd:PRK08762 155 AAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNvEALLQDVDVVVDGAD 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924523 141 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTA----CIECtleLYP 202
Cdd:PRK08762 235 NFPTRYLLNDACVKLG------------KPLVYGAVFRFEGQVSVFDAGRQRgqapCYRC---LFP 285
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 61-124 1.63e-05

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 46.33  E-value: 1.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924523  61 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPhfnkIQDF 124
Cdd:PRK15116  47 EALarTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTV----VDDF 108
PRK08223 PRK08223
hypothetical protein; Validated
 60-146 1.71e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 46.21  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  60 TEALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCG 138
Cdd:PRK08223  45 TLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENaDAFLDGVDVYVDG 124

                         90
                 ....*....|
gi 767924523 139 LD--SIIARR 146
Cdd:PRK08223 125 LDffEFDARR 134
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 63-254 1.83e-05

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: 46.91  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  63 LSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCN---VVPHFNKIQDFNDTFYRQFHIIVCGl 139
Cdd:cd01493   41 LPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVNgsaVEESPEALLDNDPSFFSQFTVVIAT- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 140 dSIIARrwingmliSLLNYEDGVLDPSsiVPLIDGGTEGFKGNARVILPgmtaciectlELyppqvnfpmCTIASMprlP 219
Cdd:cd01493  120 -NLPES--------TLLRLADVLWSAN--IPLLYVRSYGLYGYIRIQLK----------EH---------TIVESH---P 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767924523 220 EHCIEYVRMLQ-WPKEQPFGEGVPLDGDDPE---HIQWI 254
Cdd:cd01493  167 DNALEDLRLDNpFPELREHADSIDLDDMDPAehsHTPYI 205
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 63-138 4.09e-05

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: 44.20  E-value: 4.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924523  63 LSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCG 138
Cdd:cd01492   42 LSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVAT 117
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
62-197 5.47e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.11  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFND-TFYRQFHIIVCGLD 140
Cdd:PRK07411  58 AAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENAlDILAPYDVVVDGTD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523 141 SIIARRWINGMLI------------------SLLNYEDG--VLD------PSSIVP-LIDGGTEGfkgnarvILPGMTAC 193
Cdd:PRK07411 138 NFPTRYLVNDACVllnkpnvygsifrfegqaTVFNYEGGpnYRDlypeppPPGMVPsCAEGGVLG-------ILPGIIGV 210


                 ....
gi 767924523 194 IECT 197
Cdd:PRK07411 211 IQAT 214
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 62-194 6.84e-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: 43.56  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPK--DIGRPKAEVAAEFLNDRVPNCNV--VPHFNKIQDFNDTFYRQFHIIVC 137
Cdd:cd01485   39 VLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAASYEFLQELNPNVKLsiVEEDSLSNDSNIEEYLQKFTLVI 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767924523 138 GLDSIIARrwiNGMLISLLNYEDgvldpssiVPLIDGGTEGFKGNARVILPgMTACI 194
Cdd:cd01485  119 ATEENYER---TAKVNDVCRKHH--------IPFISCATYGLIGYAFFDFP-IAAFL 163
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 65-114 1.20e-04

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: 43.90  E-value: 1.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767924523  65 GFRQIHVIDMDTIDVSNLNRQFLFRPKDI--GRPKAEVAAEFLNDRVPNCNV 114
Cdd:cd01486   22 GVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDA 73
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 62-137 1.84e-04

Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 43.02  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVA----AEfLNDRVPncnVVPHFNKIqdfNDTFYRQFHIIVC 137
Cdd:cd01491   39 ILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASqarlAE-LNPYVP---VTVSTGPL---TTDELLKFQVVVL 111
PRK08328 PRK08328
hypothetical protein; Provisional
 62-202 1.88e-04

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 42.86  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924523  62 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGR-PKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGL 139
Cdd:PRK08328  47 AAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIKIETFVGRLSEENiDEVLKGVDVIVDCL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924523 140 DSIIARrwingMLISLLNYEDGvldpssiVPLIDGGTEGFKGNARVILPGMTACIEctlELYP 202
Cdd:PRK08328 127 DNFETR-----YLLDDYAHKKG-------IPLVHGAVEGTYGQVTTIVPGKTKRLR---EIFP 174
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 367-421 7.65e-04

Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein.


Pssm-ID: 464286  Cd Length: 88  Bit Score: 38.33  E-value: 7.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767924523  367 SLQMKSPAITatLEGKNRTLYLQSvTSIEERTrPNLSKTLKELGLVDGQELAVAD 421
Cdd:pfam14732  21 KLGMVAPDVS--LSGGGTILYLSS-EEDETED-DNLPKKLSELGIKNGSILTVDD 71
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 288-322 6.02e-03

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: 38.82  E-value: 6.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767924523 288 STNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVD 322
Cdd:cd01493  385 NISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGIR 419
 
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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