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Conserved domains on  [gi|162135936|ref|NP_035796|]
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NEDD8-activating enzyme E1 catalytic subunit isoform 1 [Mus musculus]

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 ...
 71-368 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: 618.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 FNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPP 230
Cdd:cd01488   81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 231 QVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFgdgVPLDGDDPEHIQWIFQKSIERASQYNIRGVTYRLTQGVVKRII 310
Cdd:cd01488  157 QVTFPLCTIANTPRLPEHCIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRII 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162135936 311 PAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 368
Cdd:cd01488  234 PAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 376-461 6.02e-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: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  376 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 455
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 162135936  456 LFKLHF 461
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 ...
 71-368 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: 618.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 FNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPP 230
Cdd:cd01488   81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 231 QVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFgdgVPLDGDDPEHIQWIFQKSIERASQYNIRGVTYRLTQGVVKRII 310
Cdd:cd01488  157 QVTFPLCTIANTPRLPEHCIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRII 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162135936 311 PAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 368
Cdd:cd01488  234 PAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 67-241 1.37e-59

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 195.17  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  147 KI-QDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTL 225
Cdd:pfam00899  98 RLtPENAEELIKSFDIVVDATDNFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLF 165

                         170
                  ....*....|....*.
gi 162135936  226 ELYPPQVNFPMCTIAS 241
Cdd:pfam00899 166 PEDPPPKLVPSCTVAG 181
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 71-369 1.08e-45

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: 159.14  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:COG0476   29 RVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 FN-DTFYRQFHIIVCGLDSIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYP 229
Cdd:COG0476  109 ENaLELLAGADLVLDCTDNFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 230 pqvnfpmctiasmprlpehcieyvrmlqwpkeqpfgdgvpldgDDPEhiqwifqksierasqynirgvtyrltQGVVKRI 309
Cdd:COG0476  174 -------------------------------------------EPPE--------------------------PGPSCAE 184

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 310 IPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 369
Cdd:COG0476  185 AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 45-254 1.79e-38

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: 149.27  E-value: 1.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936    45 LERSGPFTHPDFEPST-----------ESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFR-----QIHVIDMDTIDVSN 108
Cdd:TIGR01408  384 LPSLGKPECEEFLPRGdrydaqiavfgDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSN 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   109 LNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSIIARRWINGMLISLL 183
Cdd:TIGR01408  464 LNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFL 543

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135936   184 NyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPRLPEHCIEYVR 254
Cdd:TIGR01408  544 K------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPAAIEHTIQWAR 600
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 376-461 6.02e-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: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  376 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 455
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 162135936  456 LFKLHF 461
Cdd:pfam08825  76 SLRLRF 81
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 67-148 1.09e-19

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 90.32  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:PRK05600  39 LHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRE 118


                 ..
gi 162135936 147 KI 148
Cdd:PRK05600 119 RL 120
 
Name Accession Description Interval E-value
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 71-368 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: 618.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 FNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEdgvlDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPP 230
Cdd:cd01488   81 KDEEFYRQFNIIICGLDSIEARRWINGTLVSLLLYE----DPESIIPLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 231 QVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFgdgVPLDGDDPEHIQWIFQKSIERASQYNIRGVTYRLTQGVVKRII 310
Cdd:cd01488  157 QVTFPLCTIANTPRLPEHCIEYASLIQWPKEFPF---VPLDGDDPEHIEWLYQKALERAAQFNISGVTYSLTQGVVKRII 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 162135936 311 PAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACS 368
Cdd:cd01488  234 PAVASTNAIIAAACCLEALKIATDCYENLNNYLMYNGVDGCYTYTFEHERKEDCPVCS 291
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 71-329 1.27e-143

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: 410.05  E-value: 1.27e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKI-- 148
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVgp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 149 -QDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTleL 227
Cdd:cd01484   81 eQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFL------------IVPLIESGTEGFKGNAQVILPGMTECIECT--L 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 228 YPPQVNFPMCTIASMPRLPEHCIEYVRMLQWpkeqpfgdgvpldgDDPEHIQWIFQKSIERASQYNIRGVTYRLTQGVVK 307
Cdd:cd01484  147 YPPQKNFPMCTIASMPRLPEHCIEWARMLQW--------------DDPEHIQFIFQASNERASQYNIRGVTYFLTKGVAG 212

                        250       260
                 ....*....|....*....|..
gi 162135936 308 RIIPAVASTNAVIAAVCATEVF 329
Cdd:cd01484  213 RIIPAVATTNAVVAGVCALEVF 234
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 71-331 1.15e-74

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: 236.89  E-value: 1.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 --FNDTFYRQFHIIVCGLDSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIECTLEly 228
Cdd:cd01489   81 pdFNVEFFKQFDLVFNALDNLAARRHVNKMCLAA------------DVPLIESGTTGFLGQVQVIKKGKTECYECQPK-- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 229 PPQVNFPMCTIASMPRLPEHC------------------IEYVRMLQ--WPKEQPfgdGVPL-------DGDDPEHIQWI 281
Cdd:cd01489  147 ETPKTFPVCTIRSTPSQPIHCivwakslfflfnkvfkddIERLLSMEelWKTRKP---PVPLswkeltfDKDDQDALDFV 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 162135936 282 FQKSIERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKI 331
Cdd:cd01489  224 AAAANLRSHVFGIPMKSRFDIKQMAGNIIPAIATTNAIIAGLIVLEALKV 273
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 67-241 1.37e-59

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 195.17  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:pfam00899  18 LRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  147 KI-QDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTL 225
Cdd:pfam00899  98 RLtPENAEELIKSFDIVVDATDNFAARYLVNDACVKLG------------KPLIEAGVLGFKGQVTVVIPGKTPCYRCLF 165

                         170
                  ....*....|....*.
gi 162135936  226 ELYPPQVNFPMCTIAS 241
Cdd:pfam00899 166 PEDPPPKLVPSCTVAG 181
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 71-331 1.80e-51

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: 179.79  E-value: 1.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFR-----QIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHF 145
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 146 NKI-----QDFNDTFYRQFHIIVCGLDSIIARRWINGMLISllnYEDgvldpssivPLIDGGTEGFKGNARVILPGMTac 220
Cdd:cd01490   81 NRVgpeteHIFNDEFWEKLDGVANALDNVDARMYVDRRCVY---YRK---------PLLESGTLGTKGNTQVVIPHLT-- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 221 iectlELY-----PPQVNFPMCTIASMPRLPEHCIEYVR---------------MLQW---------------------- 258
Cdd:cd01490  147 -----ESYsssrdPPEKSIPLCTLKNFPNAIEHTIQWARdefeglfkqppenvnQYLFedcvrwarllfekyfnnnikql 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 259 ----PKEQPFGDGVP-------------LDGDDPEHIQWI---------------FQK--------------SIERASQY 292
Cdd:cd01490  222 lhnfPPDAVTSDGAPfwsgpkrcptpleFDVNNPLHLDFVlaaanlyaevygipgFEKdddtnfhmdfitaaSNLRARNY 301

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 162135936 293 NIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKI 331
Cdd:cd01490  302 SIPPADRHKTKRIAGKIIPAIATTTAAVTGLVCLELYKV 340
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 71-223 3.73e-47

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: 159.36  E-value: 3.73e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162135936 151 FN-DTFYRQFHIIVCGLDSIIARRWINGMLISLlnyedgvldpssIVPLIDGGTEGFKGNARVILPGMTACIEC 223
Cdd:cd01483   81 DNlDDFLDGVDLVIDAIDNIAVRRALNRACKEL------------GIPVIDAGGLGLGGDIQVIDIGSLSAAEA 142
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 71-369 1.08e-45

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: 159.14  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:COG0476   29 RVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 151 FN-DTFYRQFHIIVCGLDSIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECtleLYP 229
Cdd:COG0476  109 ENaLELLAGADLVLDCTDNFATRYLLNDACVKLG------------IPLVSGAVIGFEGQVTVFIPGDTPCYRC---LFP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 230 pqvnfpmctiasmprlpehcieyvrmlqwpkeqpfgdgvpldgDDPEhiqwifqksierasqynirgvtyrltQGVVKRI 309
Cdd:COG0476  174 -------------------------------------------EPPE--------------------------PGPSCAE 184

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 310 IPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQ 369
Cdd:COG0476  185 AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDCPVCGE 244
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 45-254 1.79e-38

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: 149.27  E-value: 1.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936    45 LERSGPFTHPDFEPST-----------ESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFR-----QIHVIDMDTIDVSN 108
Cdd:TIGR01408  384 LPSLGKPECEEFLPRGdrydaqiavfgDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSN 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   109 LNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD-----FNDTFYRQFHIIVCGLDSIIARRWINGMLISLL 183
Cdd:TIGR01408  464 LNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPetetiFNDEFYEKLDVVINALDNVEARRYVDSRCLAFL 543

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135936   184 NyedgvldpssivPLIDGGTEGFKGNARVILPGMTaciectlELY-----PPQVNFPMCTIASMPRLPEHCIEYVR 254
Cdd:TIGR01408  544 K------------PLLESGTLGTKGNTQVVVPHLT-------ESYgssrdPPEKEIPFCTLKSFPAAIEHTIQWAR 600
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 67-240 2.42e-36

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: 133.76  E-value: 2.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:cd00757   19 LKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 147 KIQDFN-DTFYRQFHIIVCGLDSIIARRWINgMLISLLNyedgvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTL 225
Cdd:cd00757   99 RLDAENaEELIAGYDLVLDCTDNFATRYLIN-DACVKLG-----------KPLVSGAVLGFEGQVTVFIPGEGPCYRCLF 166

                        170
                 ....*....|....*
gi 162135936 226 ELyPPQVNFPMCTIA 240
Cdd:cd00757  167 PE-PPPPGVPSCAEA 180
E2_bind pfam08825
E2 binding domain; E1 and E2 enzymes play a central role in ubiquitin and ubiquitin-like ...
 376-461 6.02e-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: 6.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  376 FSPSAKLQEVLDYLTNSASLQMKSPAITatleGKNRTLYLQSVTSIEERTRPNLSKTLKELgLVDGQELAVADVTTPQTV 455
Cdd:pfam08825   1 VSPSWTLQELIDSLAERPELQLKKPSLS----TEGKTLYMQSPPSLEEATRPNLSKKLKEL-VEDGEEITVTDPTLPSTI 75


                  ....*.
gi 162135936  456 LFKLHF 461
Cdd:pfam08825  76 SLRLRF 81
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 67-148 1.09e-19

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 90.32  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:PRK05600  39 LHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRE 118


                 ..
gi 162135936 147 KI 148
Cdd:PRK05600 119 RL 120
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 67-171 1.15e-18

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: 84.58  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:cd00755    9 LRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEE 88

                         90       100
                 ....*....|....*....|....*..
gi 162135936 147 KIQDFN--DTFYRQFHIIVCGLDSIIA 171
Cdd:cd00755   89 FLTPDNseDLLGGDPDFVVDAIDSIRA 115
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 71-176 1.19e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 82.20  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:PRK05690  34 RVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDD 113

                         90       100
                 ....*....|....*....|....*..
gi 162135936 151 FN-DTFYRQFHIIVCGLDSIIARRWIN 176
Cdd:PRK05690 114 DElAALIAGHDLVLDCTDNVATRNQLN 140
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 64-176 2.67e-16

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 80.52  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  64 QFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVP 143
Cdd:PRK07878  37 QKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRL 116

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 162135936 144 HFNKIQDFN--DTFyRQFHIIVCGLDSIIARRWIN 176
Cdd:PRK07878 117 HEFRLDPSNavELF-SQYDLILDGTDNFATRYLVN 150
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
60-175 8.42e-16

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 76.05  E-value: 8.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  60 TESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFrPKDVGRPKAEVAAEFLNDRVPNC 139
Cdd:PRK08644  19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYF-ISQIGMPKVEALKENLLEINPFV 97

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 162135936 140 NVVPHFNKIQDFN-DTFYRQFHIIVCGLDSIIARRWI 175
Cdd:PRK08644  98 EIEAHNEKIDEDNiEELFKDCDIVVEAFDNAETKAML 134
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-229 1.94e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 77.74  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  64 QFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVP 143
Cdd:PRK08762 130 QRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEA 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 144 HFNKIQDFN-DTFYRQFHIIVCGLDSIIARRWINGMLISLLnyedgvldpssiVPLIDGGTEGFKGNARVILPGMTA--- 219
Cdd:PRK08762 210 VQERVTSDNvEALLQDVDVVVDGADNFPTRYLLNDACVKLG------------KPLVYGAVFRFEGQVSVFDAGRQRgqa 277

                        170
                 ....*....|.
gi 162135936 220 -CIECtleLYP 229
Cdd:PRK08762 278 pCYRC---LFP 285
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 64-172 3.66e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 76.45  E-value: 3.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  64 QFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVP 143
Cdd:PRK05597  23 QQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTV 102

                         90       100       110
                 ....*....|....*....|....*....|
gi 162135936 144 HFNKIQDFND-TFYRQFHIIVCGLDSIIAR 172
Cdd:PRK05597 103 SVRRLTWSNAlDELRDADVILDGSDNFDTR 132
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 61-281 1.07e-14

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: 75.80  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  61 ESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCN 140
Cdd:cd01493   12 EHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCELLQELNPDVN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 141 ---VVPHFNKIQDFNDTFYRQFHIIVCGldSIIARrwingmliSLLNYEDGVLDPSsiVPLIDGGTEGFKGNARVILPgm 217
Cdd:cd01493   92 gsaVEESPEALLDNDPSFFSQFTVVIAT--NLPES--------TLLRLADVLWSAN--IPLLYVRSYGLYGYIRIQLK-- 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135936 218 taciectlELyppqvnfpmCTIASMprlPEHCIEYVRMLQ-WPKEQPFGDGVPLDGDDPE---HIQWI 281
Cdd:cd01493  158 --------EH---------TIVESH---PDNALEDLRLDNpFPELREHADSIDLDDMDPAehsHTPYI 205
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 71-175 1.67e-14

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: 71.26  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFlFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD 150
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90       100
                 ....*....|....*....|....*.
gi 162135936 151 FN-DTFYRQFHIIVCGLDSIIARRWI 175
Cdd:cd01487   80 NNlEGLFGDCDIVVEAFDNAETKAML 105
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 67-221 2.48e-14

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: 71.30  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDV--GRPKAEVAAEFLNDRVPNCNV--V 142
Cdd:cd01485   17 LRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASYEFLQELNPNVKLsiV 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162135936 143 PHFNKIQDFNDTFYRQFHIIVCGLDSIIARrwiNGMLISLLNYEDgvldpssiVPLIDGGTEGFKGNARVILPgMTACI 221
Cdd:cd01485   97 EEDSLSNDSNIEEYLQKFTLVIATEENYER---TAKVNDVCRKHH--------IPFISCATYGLIGYAFFDFP-IAAFL 163
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 64-165 4.82e-14

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: 70.40  E-value: 4.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  64 QFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVP 143
Cdd:cd01492   16 QKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRVKVSV 95

                         90       100
                 ....*....|....*....|..
gi 162135936 144 HFNKIQDFNDTFYRQFHIIVCG 165
Cdd:cd01492   96 DTDDISEKPEEFFSQFDVVVAT 117
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 70-151 6.05e-13

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: 68.57  E-value: 6.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  70 CKVLVIGAGGLG---CEllkNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEflndRV----PNCNVv 142
Cdd:COG1179   25 AHVAVVGLGGVGswaAE---ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAE----RIrdinPDCEV- 96


                 ....*....
gi 162135936 143 phfNKIQDF 151
Cdd:COG1179   97 ---TAIDEF 102
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 72-164 2.42e-12

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: 67.29  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  72 VLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVA----AEfLNDRVPncnVVPHFNK 147
Cdd:cd01491   22 VLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASqarlAE-LNPYVP---VTVSTGP 97

                         90
                 ....*....|....*..
gi 162135936 148 IqdfNDTFYRQFHIIVC 164
Cdd:cd01491   98 L---TTDELLKFQVVVL 111
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
67-224 4.93e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 67.45  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFN 146
Cdd:PRK07411  36 LKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYET 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 147 KIQDFND-TFYRQFHIIVCGLDSIIARRWINGMLI------------------SLLNYEDG--VLD------PSSIVP-L 198
Cdd:PRK07411 116 RLSSENAlDILAPYDVVVDGTDNFPTRYLVNDACVllnkpnvygsifrfegqaTVFNYEGGpnYRDlypeppPPGMVPsC 195

                        170       180
                 ....*....|....*....|....*.
gi 162135936 199 IDGGTEGfkgnarvILPGMTACIECT 224
Cdd:PRK07411 196 AEGGVLG-------ILPGIIGVIQAT 214
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 60-172 7.84e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 64.12  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   60 TESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQfLFRPKDVGRPKAEVAAEFLNDRVPNC 139
Cdd:TIGR02354  12 TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQ-QYKASQVGEPKTEALKENISEINPYT 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 162135936  140 NVVPHFNKIQDFN-DTFYRQFHIIVCGLDSIIAR 172
Cdd:TIGR02354  91 EIEAYDEKITEENiDKFFKDADIVCEAFDNAEAK 124
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 71-141 3.07e-11

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: 64.32  E-value: 3.07e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDV--GRPKAEVAAEFLNDRVPNCNV 141
Cdd:cd01486    1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDA 73
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 56-229 7.92e-11

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 63.09  E-value: 7.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  56 FEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDV--GRPKAeVAAEfln 133
Cdd:PRK07688  11 FSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKA-VAAK--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 134 DRVPNCNVVPHFNKI-QDFN----DTFYRQFHIIVCGLDSIIARrwingMLISLLNYEDGvldpssiVPLIDGGTEGFKG 208
Cdd:PRK07688  87 KRLEEINSDVRVEAIvQDVTaeelEELVTGVDLIIDATDNFETR-----FIVNDAAQKYG-------IPWIYGACVGSYG 154

                        170       180
                 ....*....|....*....|.
gi 162135936 209 NARVILPGMTACIECTLELYP 229
Cdd:PRK07688 155 LSYTIIPGKTPCLRCLLQSIP 175
PRK08223 PRK08223
hypothetical protein; Validated
 60-173 1.21e-09

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 59.31  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  60 TESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNC 139
Cdd:PRK08223  18 TPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPEL 97

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 162135936 140 NVVPHFNKIQDFN-DTFYRQFHIIVCGLD--SIIARR 173
Cdd:PRK08223  98 EIRAFPEGIGKENaDAFLDGVDVYVDGLDffEFDARR 134
PRK08328 PRK08328
hypothetical protein; Provisional
 67-229 1.47e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 58.27  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGR-PKAEVAAEFLNDRVPNCNVVPHF 145
Cdd:PRK08328  25 LKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKLERFNSDIKIETFV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 146 NKIQDFN-DTFYRQFHIIVCGLDSIIARrwingMLISLLNYEDGvldpssiVPLIDGGTEGFKGNARVILPGMTACIEct 224
Cdd:PRK08328 105 GRLSEENiDEVLKGVDVIVDCLDNFETR-----YLLDDYAHKKG-------IPLVHGAVEGTYGQVTTIVPGKTKRLR-- 170


                 ....*
gi 162135936 225 lELYP 229
Cdd:PRK08328 171 -EIFP 174
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 72-151 2.54e-09

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 57.89  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  72 VLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPhfnkIQDF 151
Cdd:PRK15116  33 ICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTV----VDDF 108
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 72-229 3.45e-09

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 58.20  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  72 VLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVG--RPKAEVAAEFLNDRVPNCNVVPHFNKIQ 149
Cdd:PRK12475  27 VLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAIAAKEHLRKINSEVEIVPVVTDVT 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936 150 DFN-DTFYRQFHIIVCGLDSIIARrwingMLISLLNYEDGvldpssiVPLIDGGTEGFKGNARVILPGMTACIECTLELY 228
Cdd:PRK12475 107 VEElEELVKEVDLIIDATDNFDTR-----LLINDLSQKYN-------IPWIYGGCVGSYGVTYTIIPGKTPCLRCLMEHV 174


                 .
gi 162135936 229 P 229
Cdd:PRK12475 175 P 175
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 72-163 7.63e-09

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 57.98  E-value: 7.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936    72 VLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPncnVVPHFNKIQDF 151
Cdd:TIGR01408   27 VLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLAELNP---YVHVSSSSVPF 103

                           90
                   ....*....|..
gi 162135936   152 NDTFYRQFHIIV 163
Cdd:TIGR01408  104 NEEFLDKFQCVV 115
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 71-137 1.52e-06

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 50.71  E-value: 1.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936   71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDV---GRPKAEVAAEFLNDRVP 137
Cdd:TIGR01381 340 KVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIFP 409
PRK14851 PRK14851
hypothetical protein; Provisional
 60-167 3.26e-06

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 49.47  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  60 TESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNC 139
Cdd:PRK14851  34 TPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFL 113

                         90       100
                 ....*....|....*....|....*....
gi 162135936 140 NVVPHFNKIQDFN-DTFYRQFHIIVCGLD 167
Cdd:PRK14851 114 EITPFPAGINADNmDAFLDGVDVVLDGLD 142
UAE_UbL pfam14732
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ...
 394-448 1.12e-03

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: 37.94  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162135936  394 SLQMKSPAITatLEGKNRTLYLQSvTSIEERTrPNLSKTLKELGLVDGQELAVAD 448
Cdd:pfam14732  21 KLGMVAPDVS--LSGGGTILYLSS-EEDETED-DNLPKKLSELGIKNGSILTVDD 71
PRK14852 PRK14852
hypothetical protein; Provisional
 71-216 1.54e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 41.22  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEflndRVPNCNvvpHFNKIQD 150
Cdd:PRK14852 334 RVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTE----RALSVN---PFLDIRS 406

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162135936 151 FN--------DTFYRQFHIIVCGLDSI---IARRWINGMLisllnyEDGvldpssiVPLIDGGTEGFKGNARVILPG 216
Cdd:PRK14852 407 FPegvaaetiDAFLKDVDLLVDGIDFFaldIRRRLFNRAL------ELG-------IPVITAGPLGYSCALLVFMPG 470
PRK12548 PRK12548
shikimate dehydrogenase;
71-154 2.99e-03

shikimate dehydrogenase;


Pssm-ID: 183585 [Multi-domain]  Cd Length: 289  Bit Score: 39.34  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135936  71 KVLVIGAGGLGCELLKNLALSGFRQIHVidmdtidvsnlnrqflFRPKDVGRPKAEVAAEFLNDRVPNCNVvphfnKIQD 150
Cdd:PRK12548 128 KLTVIGAGGAATAIQVQCALDGAKEITI----------------FNIKDDFYERAEQTAEKIKQEVPECIV-----NVYD 186


                 ....
gi 162135936 151 FNDT 154
Cdd:PRK12548 187 LNDT 190
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 67-99 3.03e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 37.94  E-value: 3.03e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 162135936   67 LDTCKVLVIGAGGLGCELLKNLALSGFRQIHVI 99
Cdd:pfam01488  10 LKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIA 42
 
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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