NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1394533323|ref|NP_001350790|]
View 

NEDD8-activating enzyme E1 catalytic subunit isoform 3 [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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 48-327 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: 575.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 127
Cdd:cd01488    19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 128 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 207
Cdd:cd01488    99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 208 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 287
Cdd:cd01488   175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1394533323 288 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 327
Cdd:cd01488   252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 335-420 3.25e-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: 3.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 335 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 414
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 1394533323 415 LFKLHF 420
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 ...
 48-327 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: 575.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 127
Cdd:cd01488    19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 128 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 207
Cdd:cd01488    99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 208 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 287
Cdd:cd01488   175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1394533323 288 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 327
Cdd:cd01488   252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 48-200 5.45e-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: 5.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-QDFNDTFYRQFHIIVCGLD 126
Cdd:pfam00899  40 ARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATD 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533323 127 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIAS 200
Cdd:pfam00899 120 NFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLFPEDPPPKLVPSCTVAG 181
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 48-328 1.26e-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: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:COG0476    47 AAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLDCTD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 127 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYPpqvnfpmctiasmprlpe 206
Cdd:COG0476   127 NFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP------------------ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 207 hcieyvrmlqwpkeqpfgegvpldgDDPEhiqwifqkslerasqynirgvtyrltQGVVKRIIPAVASTNAVIAAVCATE 286
Cdd:COG0476   174 -------------------------EPPE--------------------------PGPSCAEAGVLGPLVGVIGSLQATE 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1394533323 287 VFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 328
Cdd:COG0476   203 AIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 335-420 3.25e-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: 3.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 335 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 414
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 1394533323 415 LFKLHF 420
Cdd:pfam08825  76 SLRLRF 81
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 54-380 1.44e-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: 1.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323   54 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSI 128
Cdd:TIGR01408  450 MITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNV 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  129 IARRWINGMLISLLNyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 203
Cdd:TIGR01408  530 EARRYVDSRCLAFLK------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPA 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  204 LPEHCIEYVR-MLQWPKEQPFGEgVPLDGDDPEHiqwiFQKSLERASQYNIRGVTYRLTQGVVKRiipavastnaviaav 282
Cdd:TIGR01408  591 AIEHTIQWARdKFEGLFSHKPSL-VNKYLSSPSS----AEEVLQKIQSGHSREGLEQIIKLLSKE--------------- 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  283 cATEVFK-IATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCP---ACSQLPQNIQFSPSAKlqEVLDYLTNSASLQMKS 358
Cdd:TIGR01408  651 -KPRNFSqCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPfwsSPKRPPSPLKFDLNEP--LHLSFIQAAAKLYATV 727

                          330       340
                   ....*....|....*....|..
gi 1394533323  359 PAITATLEGKNRTLYLQSVTSI 380
Cdd:TIGR01408  728 YGIPFAEEDLSADALLNILSEV 749
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
50-134 6.72e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 58.71  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  50 SGFRQIHVIDMDTIDVSNLNRQFLFrPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 128
Cdd:PRK08644   50 SGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNiEELFKDCDIVVEAFDNA 128


                  ....*.
gi 1394533323 129 IARRWI 134
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 ...
 48-327 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: 575.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDS 127
Cdd:cd01488    19 ALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKDEEFYRQFNIIICGLDS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 128 IIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEH 207
Cdd:cd01488    99 IEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVTFPLCTIANTPRLPEH 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 208 CIEYVRMLQWPKEQPFgegVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEV 287
Cdd:cd01488   175 CIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRIIPAVASTNAIIAAACCLEA 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1394533323 288 FKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 327
Cdd:cd01488   252 LKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 48-288 6.99e-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: 376.15  E-value: 6.99e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI---QDFNDTFYRQFHIIVCG 124
Cdd:cd01484    19 ALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVgpeQDFNDTFFEQFHIIVNA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 125 LDSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTleLYPPQVNFPMCTIASMPRL 204
Cdd:cd01484    99 LDNIIARRYVNGMLIFL------------IVPLIESGTEGFKGNAQVILPGMTECIECT--LYPPQKNFPMCTIASMPRL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 205 PEHCIEYVRMLQWpkeqpfgegvpldgDDPEHIQWIFQKSLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCA 284
Cdd:cd01484   165 PEHCIEWARMLQW--------------DDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAGRIIPAVATTNAVVAGVCA 230


                  ....
gi 1394533323 285 TEVF 288
Cdd:cd01484   231 LEVF 234
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 48-290 7.39e-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: 197.22  E-value: 7.39e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD--FNDTFYRQFHIIVCGL 125
Cdd:cd01489    19 VLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdFNVEFFKQFDLVFNAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 126 DSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTLElyPPQVNFPMCTIASMPRLP 205
Cdd:cd01489    99 DNLAARRHVNKMCLAA------------DVPLIESGTTGFLGQVQVIKKGKTECYECQPK--ETPKTFPVCTIRSTPSQP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 206 EHC------------------IEYVRMLQ--WPKEQPfgeGVPL-------DGDDPEHIQWIFQKSLERASQYNIRGVTY 258
Cdd:cd01489   165 IHCivwakslfflfnkvfkddIERLLSMEelWKTRKP---PVPLswkeltfDKDDQDALDFVAAAANLRSHVFGIPMKSR 241

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1394533323 259 RLTQGVVKRIIPAVASTNAVIAAVCATEVFKI 290
Cdd:cd01489   242 FDIKQMAGNIIPAIATTNAIIAGLIVLEALKV 273
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 48-200 5.45e-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: 5.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-QDFNDTFYRQFHIIVCGLD 126
Cdd:pfam00899  40 ARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLtPENAEELIKSFDIVVDATD 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533323 127 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIAS 200
Cdd:pfam00899 120 NFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLFPEDPPPKLVPSCTVAG 181
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 54-290 4.92e-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: 4.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  54 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI-----QDFNDTFYRQFHIIVCGLDSI 128
Cdd:cd01490    30 EITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpeteHIFNDEFWEKLDGVANALDNV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 129 IARRWINGMLISllnYEDgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 203
Cdd:cd01490   110 DARMYVDRRCVY---YRK---------PLLESGTLGTKGNTQVVIPHLT-------ESYsssrdPPEKSIPLCTLKNFPN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 204 LPEHCIEYVR---------------MLQW--------------------------PKE------QPFGEG-----VPL-- 229
Cdd:cd01490   171 AIEHTIQWARdefeglfkqppenvnQYLFedcvrwarllfekyfnnnikqllhnfPPDavtsdgAPFWSGpkrcpTPLef 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 230 DGDDPEHIQWI---------------FQK--------------SLERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIA 280
Cdd:cd01490   251 DVNNPLHLDFVlaaanlyaevygipgFEKdddtnfhmdfitaaSNLRARNYSIPPADRHKTKRIAGKIIPAIATTTAAVT 330

                         330
                  ....*....|
gi 1394533323 281 AVCATEVFKI 290
Cdd:cd01490   331 GLVCLELYKV 340
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 48-182 5.99e-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: 128.93  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:cd01483    19 ARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNlDDFLDGVDLVIDAID 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533323 127 SIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIEC 182
Cdd:cd01483    99 NIAVRRALNRACKEL------------GIPVIDAGGLGLGGDIQVIDIGSLSAAEA 142
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 48-328 1.26e-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: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:COG0476    47 AAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLDCTD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 127 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYPpqvnfpmctiasmprlpe 206
Cdd:COG0476   127 NFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP------------------ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 207 hcieyvrmlqwpkeqpfgegvpldgDDPEhiqwifqkslerasqynirgvtyrltQGVVKRIIPAVASTNAVIAAVCATE 286
Cdd:COG0476   174 -------------------------EPPE--------------------------PGPSCAEAGVLGPLVGVIGSLQATE 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1394533323 287 VFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 328
Cdd:COG0476   203 AIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 335-420 3.25e-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: 3.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 335 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 414
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 1394533323 415 LFKLHF 420
Cdd:pfam08825  76 SLRLRF 81
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 54-380 1.44e-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: 1.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323   54 QIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSI 128
Cdd:TIGR01408  450 MITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNV 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  129 IARRWINGMLISLLNyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPR 203
Cdd:TIGR01408  530 EARRYVDSRCLAFLK------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPA 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  204 LPEHCIEYVR-MLQWPKEQPFGEgVPLDGDDPEHiqwiFQKSLERASQYNIRGVTYRLTQGVVKRiipavastnaviaav 282
Cdd:TIGR01408  591 AIEHTIQWARdKFEGLFSHKPSL-VNKYLSSPSS----AEEVLQKIQSGHSREGLEQIIKLLSKE--------------- 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  283 cATEVFK-IATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCP---ACSQLPQNIQFSPSAKlqEVLDYLTNSASLQMKS 358
Cdd:TIGR01408  651 -KPRNFSqCVEWARLKFEKYFNNKALQLLHCFPLDIRTSTGSPfwsSPKRPPSPLKFDLNEP--LHLSFIQAAAKLYATV 727

                          330       340
                   ....*....|....*....|..
gi 1394533323  359 PAITATLEGKNRTLYLQSVTSI 380
Cdd:TIGR01408  728 YGIPFAEEDLSADALLNILSEV 749
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 50-199 4.61e-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: 104.87  E-value: 4.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  50 SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 128
Cdd:cd00757    43 AGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENaEELIAGYDLVLDCTDNF 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533323 129 IARRWINgMLISLLNyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELyPPQVNFPMCTIA 199
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 ...
 47-130 5.43e-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: 71.10  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  47 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN--DTFYRQFHIIV 122
Cdd:cd00755    28 EALarSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTPDNseDLLGGDPDFVV 107


                  ....*...
gi 1394533323 123 CGLDSIIA 130
Cdd:cd00755   108 DAIDSIRA 115
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 47-110 1.76e-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: 1.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  47 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEflndRV----PNCNVvphfNKIQDF 110
Cdd:COG1179    41 EALarSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAE----RIrdinPDCEV----TAIDEF 102
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
50-134 6.72e-10

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 58.71  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  50 SGFRQIHVIDMDTIDVSNLNRQFLFrPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLDSI 128
Cdd:PRK08644   50 SGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNiEELFKDCDIVVEAFDNA 128


                  ....*.
gi 1394533323 129 IARRWI 134
Cdd:PRK08644  129 ETKAML 134
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 48-107 7.29e-10

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 60.28  E-value: 7.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKI 107
Cdd:PRK05600   61 ASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERL 120
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 48-135 1.36e-08

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 55.24  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:PRK05690   52 AAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDElAALIAGHDLVLDCTD 131


                  ....*....
gi 1394533323 127 SIIARRWIN 135
Cdd:PRK05690  132 NVATRNQLN 140
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 48-135 2.69e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 55.48  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN--DTFyRQFHIIVCGL 125
Cdd:PRK07878   62 AAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNavELF-SQYDLILDGT 140

                          90
                  ....*....|
gi 1394533323 126 DSIIARRWIN 135
Cdd:PRK07878  141 DNFATRYLVN 150
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 48-131 3.99e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 54.88  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFND-TFYRQFHIIVCGLD 126
Cdd:PRK05597   48 AGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVSVRRLTWSNAlDELRDADVILDGSD 127


                  ....*
gi 1394533323 127 SIIAR 131
Cdd:PRK05597  128 NFDTR 132
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 48-134 5.74e-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: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:cd01487    19 ARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNlEGLFGDCDIVVEAFD 97


                  ....*...
gi 1394533323 127 SIIARRWI 134
Cdd:cd01487    98 NAETKAML 105
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
48-188 7.50e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 53.86  E-value: 7.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGLD 126
Cdd:PRK08762  155 AAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNvEALLQDVDVVVDGAD 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533323 127 SIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTA----CIECtleLYP 188
Cdd:PRK08762  235 NFPTRYLLNDACVKLG------------KPLVYGAVFRFEGQVSVFDAGRQRgqapCYRC---LFP 285
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 47-110 1.55e-05

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 46.33  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533323  47 EAL--SGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPhfnkIQDF 110
Cdd:PRK15116   47 EALarTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTV----VDDF 108
PRK08223 PRK08223
hypothetical protein; Validated
 46-132 1.63e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 46.21  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  46 TEALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCG 124
Cdd:PRK08223   45 TLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENaDAFLDGVDVYVDG 124

                          90
                  ....*....|
gi 1394533323 125 LD--SIIARR 132
Cdd:PRK08223  125 LDffEFDARR 134
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 49-240 1.74e-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: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  49 LSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCN---VVPHFNKIQDFNDTFYRQFHIIVCGl 125
Cdd:cd01493    41 LPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVNgsaVEESPEALLDNDPSFFSQFTVVIAT- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 126 dSIIARrwingmliSLLNYEDGVLDPSsiVPLIDGGTEGFKGNARVILPgmtaciectlELyppqvnfpmCTIASMprlP 205
Cdd:cd01493   120 -NLPES--------TLLRLADVLWSAN--IPLLYVRSYGLYGYIRIQLK----------EH---------TIVESH---P 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1394533323 206 EHCIEYVRMLQ-WPKEQPFGEGVPLDGDDPE---HIQWI 240
Cdd:cd01493   167 DNALEDLRLDNpFPELREHADSIDLDDMDPAehsHTPYI 205
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 49-124 3.91e-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: 3.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533323  49 LSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCG 124
Cdd:cd01492    42 LSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVAT 117
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
48-183 4.93e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.11  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFND-TFYRQFHIIVCGLD 126
Cdd:PRK07411   58 AAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENAlDILAPYDVVVDGTD 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323 127 SIIARRWINGMLI------------------SLLNYEDG--VLD------PSSIVP-LIDGGTEGfkgnarvILPGMTAC 179
Cdd:PRK07411  138 NFPTRYLVNDACVllnkpnvygsifrfegqaTVFNYEGGpnYRDlypeppPPGMVPsCAEGGVLG-------ILPGIIGV 210


                  ....
gi 1394533323 180 IECT 183
Cdd:PRK07411  211 IQAT 214
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 48-180 7.05e-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: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPK--DIGRPKAEVAAEFLNDRVPNCNV--VPHFNKIQDFNDTFYRQFHIIVC 123
Cdd:cd01485    39 VLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAASYEFLQELNPNVKLsiVEEDSLSNDSNIEEYLQKFTLVI 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533323 124 GLDSIIARrwiNGMLISLLNYEDgvldpssiVPLIDGGTEGFKGNARVILPgMTACI 180
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 ...
 51-100 1.14e-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: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533323  51 GFRQIHVIDMDTIDVSNLNRQFLFRPKDI--GRPKAEVAAEFLNDRVPNCNV 100
Cdd:cd01486    22 GVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDA 73
PRK08328 PRK08328
hypothetical protein; Provisional
 48-188 1.39e-04

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 42.86  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGR-PKAEVAAEFLNDRVPNCNVVPHFNKIQDFN-DTFYRQFHIIVCGL 125
Cdd:PRK08328   47 AAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIKIETFVGRLSEENiDEVLKGVDVIVDCL 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533323 126 DSIIARrwingMLISLLNYEDGvldpssiVPLIDGGTEGFKGNARVILPGMTACIEctlELYP 188
Cdd:PRK08328  127 DNFETR-----YLLDDYAHKKG-------IPLVHGAVEGTYGQVTTIVPGKTKRLR---EIFP 174
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 48-123 1.88e-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: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533323  48 ALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKAEVA----AEfLNDRVPncnVVPHFNKIqdfNDTFYRQFHIIVC 123
Cdd:cd01491    39 ILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASqarlAE-LNPYVP---VTVSTGPL---TTDELLKFQVVVL 111
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 353-407 6.19e-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: 38.71  E-value: 6.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533323 353 SLQMKSPAITatLEGKNRTLYLQSvTSIEERTrPNLSKTLKELGLVDGQELAVAD 407
Cdd:pfam14732  21 KLGMVAPDVS--LSGGGTILYLSS-EEDETED-DNLPKKLSELGIKNGSILTVDD 71
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 274-308 5.74e-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: 5.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1394533323 274 STNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVD 308
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH