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Conserved domains on  [gi|9790247|ref|NP_062722|]
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SUMO-activating enzyme subunit 1 isoform a [Mus musculus]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 10107334)

ubiquitin-activating E1 family protein, such as SUMO1 activating enzyme subunit 1 (SAE1) which is a component of a heterodimer E1 enzyme (SAE1/SAE2) involved in small ubiquitin-like modifier (SUMO)ylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 20-345 1.98e-99

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: 291.89  E-value: 1.98e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   20 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEAS 99
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  100 LERAQNLNPMVDVKVDTEDVEKKPESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 179
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  180 eektkvakvsqgvedgpeakrakldssettmvkkkvlfcpvkealevdwsgekakaalkrtapdyfllqvllkfrtdkgr 259
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  260 dptsesykedaelllqirndvfdslgispdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 339
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 9790247  340 GSGIVE 345
Cdd:cd01492 192 SEAPIY 197
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 20-345 1.98e-99

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: 291.89  E-value: 1.98e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   20 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEAS 99
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  100 LERAQNLNPMVDVKVDTEDVEKKPESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 179
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  180 eektkvakvsqgvedgpeakrakldssettmvkkkvlfcpvkealevdwsgekakaalkrtapdyfllqvllkfrtdkgr 259
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  260 dptsesykedaelllqirndvfdslgispdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 339
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 9790247  340 GSGIVE 345
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 23-341 2.52e-51

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: 170.52  E-value: 2.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    101 ERAQNLNPMVDVKVDTEDVEKK-PESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFAnlgeheFV 179
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    180 EEKTKVAKVSQGVEDGPeakrakldssettmvkKKVLFCPVKEALevdwsgekakaalkrtapdyfllqvllkfrtdkgr 259
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPP----------------KLVPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    260 dptsesykedaelllqirndvfdslgispdllpddfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 337
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 9790247    338 MKGS 341
Cdd:pfam00899 220 LTMT 223
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 23-349 2.15e-41

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: 154.28  E-value: 2.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247      23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     103 AQNLNPMVDVKVDTEDVEkkpESFFTKFDAVCLTCCSRDVIIKVDQICHRN--SIKFFTGDVFGYHGYTFANLGEhEFV- 179
Cdd:TIGR01408   87 LAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGD-EFEv 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     180 ------EEKTK-VAKVSQ--------------GVEDG-----------PEAKRAK-------------LDSSET------ 208
Cdd:TIGR01408  163 ldtdgeEPKTGfIASITQanpgivtclenhrhKLETGdfvtfrevngmTGLNDGSprkitvispysfsIGDTTElgpylh 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     209 ----TMVK--KKVLFCPVKEALE------VDWSGEKAkaalkrtAPDYFL-LQVLLKFRTDKGRDPTSESyKEDAELLLQ 275
Cdd:TIGR01408  243 ggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPER-------PPEIHTaFQALDQFQEKYSRKPNVGC-QQDAEELLK 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9790247     276 IRNDVFDSLGISPDLLPDDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgsgIVECLGP 349
Cdd:TIGR01408  315 LATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLPSLGK 389
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 23-168 1.51e-23

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: 97.51  E-value: 1.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9790247  101 ERAQNLNPMVDV-----KVDTEDVekkpESFFTKFDAVcLTCC----SRDVIikvDQICHRNSIKFFTGDVFGYHGY 168
Cdd:COG0476  88 ERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdnfaTRYLL---NDACVKLGIPLVSGAVIGFEGQ 156
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 23-116 8.10e-14

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 70.26  E-value: 8.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:PRK05690  13 YNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                         90
                 ....*....|....*.
gi 9790247   101 ERAQNLNPmvDVKVDT 116
Cdd:PRK05690  93 AALARINP--HIAIET 106
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 20-345 1.98e-99

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: 291.89  E-value: 1.98e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   20 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEAS 99
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  100 LERAQNLNPMVDVKVDTEDVEKKPESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 179
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  180 eektkvakvsqgvedgpeakrakldssettmvkkkvlfcpvkealevdwsgekakaalkrtapdyfllqvllkfrtdkgr 259
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  260 dptsesykedaelllqirndvfdslgispdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 339
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 9790247  340 GSGIVE 345
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 23-341 2.52e-51

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: 170.52  E-value: 2.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    101 ERAQNLNPMVDVKVDTEDVEKK-PESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFAnlgeheFV 179
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    180 EEKTKVAKVSQGVEDGPeakrakldssettmvkKKVLFCPVKEALevdwsgekakaalkrtapdyfllqvllkfrtdkgr 259
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPP----------------KLVPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    260 dptsesykedaelllqirndvfdslgispdllpddfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 337
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 9790247    338 MKGS 341
Cdd:pfam00899 220 LTMT 223
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 23-170 4.15e-49

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: 163.36  E-value: 4.15e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSV--GRNRAEASL 100
Cdd:cd01485   2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASY 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790247  101 ERAQNLNPMVDVKVDTEDVEKK---PESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTF 170
Cdd:cd01485  82 EFLQELNPNVKLSIVEEDSLSNdsnIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAF 154
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 23-350 2.10e-47

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: 161.67  E-value: 2.10e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:cd01491   2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  103 AQNLNPMVDVKVDTEDVEKkpeSFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLGEhEFV--- 179
Cdd:cd01491  82 LAELNPYVPVTVSTGPLTT---DELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGD-EFTvyd 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  180 --EEKTK---VAKVSQGvEDGpeakrakldssETTMVKKKVLfcPVKEALEVDWSGEKAKAALKRTAPdyfllqvllKFR 254
Cdd:cd01491 158 pnGEEPKsgmISSISKD-NPG-----------VVTCLDETRH--GFEDGDYVTFSEVEGMTELNGCEP---------RKI 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  255 TDKGrdPTSESYKEDAELLLQIRNDVFDSLGISpdllpddfvrycfsemaPVCAVVGGILAQEIVKALSQRDPPHNNFFF 334
Cdd:cd01491 215 KVKG--PYTFSIGDTSSFSEYIRGGIVTQVKLS-----------------PMAAFFGGLAAQEVLKACSGKFTPLKQWLY 275

                       330
                ....*....|....*.
gi 9790247  335 FDGmkgsgiVECLGPQ 350
Cdd:cd01491 276 FDA------LECLPED 285
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 23-349 2.15e-41

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: 154.28  E-value: 2.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247      23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     103 AQNLNPMVDVKVDTEDVEkkpESFFTKFDAVCLTCCSRDVIIKVDQICHRN--SIKFFTGDVFGYHGYTFANLGEhEFV- 179
Cdd:TIGR01408   87 LAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGD-EFEv 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     180 ------EEKTK-VAKVSQ--------------GVEDG-----------PEAKRAK-------------LDSSET------ 208
Cdd:TIGR01408  163 ldtdgeEPKTGfIASITQanpgivtclenhrhKLETGdfvtfrevngmTGLNDGSprkitvispysfsIGDTTElgpylh 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     209 ----TMVK--KKVLFCPVKEALE------VDWSGEKAkaalkrtAPDYFL-LQVLLKFRTDKGRDPTSESyKEDAELLLQ 275
Cdd:TIGR01408  243 ggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPER-------PPEIHTaFQALDQFQEKYSRKPNVGC-QQDAEELLK 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9790247     276 IRNDVFDSLGISPDLLPDDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgsgIVECLGP 349
Cdd:TIGR01408  315 LATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLPSLGK 389
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 23-338 4.26e-33

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: 127.04  E-value: 4.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:cd01493   3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  103 AQNLNPmvdvKVDTEDVEKKPE-------SFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLGE 175
Cdd:cd01493  83 LQELNP----DVNGSAVEESPEalldndpSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  176 HEFVEEKTKvakvsQGVED------GPEAKRA-------KLDSSET-------------------------------TMV 211
Cdd:cd01493 159 HTIVESHPD-----NALEDlrldnpFPELREHadsidldDMDPAEHshtpyivilikylekwrsahngqlpstykekKEF 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  212 KKKVLFCPVKEALEVDWsgEKAKAA----LKRTAPDYFLLQVLLKFRTDK-----------------------------G 258
Cdd:cd01493 234 RDLVRSLMRSNEDEENF--EEAIKAvnkaLNRTKIPSSVEEIFNDDRCENltsqsssfwimaralkefvaeengllplpG 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247  259 RDP----TSESY-----------KEDAELLLQIRNDVFDSLGISPDLLPDD------------FVRYCFSEMAPVCAVVG 311
Cdd:cd01493 312 TLPdmtaDTEKYiklqniyrekaEKDAAEVEKYVREILKSLGRSPDSISDKeiklfcknaaflRVIRGRSLEHNISAFMG 391

                       410       420
                ....*....|....*....|....*..
gi 9790247  312 GILAQEIVKALSQRDPPHNNFFFFDGM 338
Cdd:cd01493 392 GIAAQEVIKLITKQYVPIDNTFIFDGI 418
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 23-168 1.51e-23

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: 97.51  E-value: 1.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9790247  101 ERAQNLNPMVDV-----KVDTEDVekkpESFFTKFDAVcLTCC----SRDVIikvDQICHRNSIKFFTGDVFGYHGY 168
Cdd:COG0476  88 ERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdnfaTRYLL---NDACVKLGIPLVSGAVIGFEGQ 156
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 42-168 2.89e-21

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: 88.48  E-value: 2.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPMVDVKVDTEDVEK 121
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 9790247  122 -KPESFFTKFDAVCLTCCSRDVIIKVDQICHRNSIKFFTGDVFGYHGY 168
Cdd:cd01483  81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGD 128
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 23-168 3.36e-21

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: 90.61  E-value: 3.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790247  101 ERAQNLNPMVDVKVDTEDV-EKKPESFFTKFDAVcLTCC----SRDVIikvDQICHRNSIKFFTGDVFGYHGY 168
Cdd:cd00757  82 ERLRAINPDVEIEAYNERLdAENAEELIAGYDLV-LDCTdnfaTRYLI---NDACVKLGKPLVSGAVLGFEGQ 150
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 23-116 8.10e-14

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 70.26  E-value: 8.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:PRK05690  13 YNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                         90
                 ....*....|....*.
gi 9790247   101 ERAQNLNPmvDVKVDT 116
Cdd:PRK05690  93 AALARINP--HIAIET 106
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 20-112 1.08e-13

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 70.47  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    20 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQtGSVGRNRAEAS 99
Cdd:PTZ00245   6 AVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQ-GEAGGTRGARA 84

                         90
                 ....*....|...
gi 9790247   100 LERAQNLNPMVDV 112
Cdd:PTZ00245  85 LGALQRLNPHVSV 97
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 21-117 2.64e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 69.90  E-value: 2.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    21 AQYDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEA 98
Cdd:PRK05597   7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAES 86

                         90
                 ....*....|....*....
gi 9790247    99 SLERAQNLNPMVDVKVDTE 117
Cdd:PRK05597  87 AREAMLALNPDVKVTVSVR 105
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 31-159 5.25e-13

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: 67.63  E-value: 5.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   31 GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPM- 109
Cdd:cd00755   2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPEc 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 9790247  110 -VDVKVDTEDVEKKPESFFTKFDAVcLTCCSrDVIIKVDQI--CHRNSIKFFT 159
Cdd:cd00755  82 eVDAVEEFLTPDNSEDLLGGDPDFV-VDAID-SIRAKVALIayCRKRKIPVIS 132
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 25-115 5.94e-12

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 66.06  E-value: 5.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    25 RQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:PRK05600  24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                         90
                 ....*....|...
gi 9790247   103 AQNLNPmvDVKVD 115
Cdd:PRK05600 104 LKEIQP--DIRVN 114
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
23-120 7.08e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 62.72  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    23 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASL 100
Cdd:PRK08762 116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                         90       100
                 ....*....|....*....|....*
gi 9790247   101 ERAQNLNPMVDV-----KVDTEDVE 120
Cdd:PRK08762 196 QRLAALNPDVQVeavqeRVTSDNVE 220
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 42-133 2.30e-10

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 60.83  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPMVDVKVDTEDVEK 121
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90
                ....*....|..
gi 9790247  122 KPESFFTKFDAV 133
Cdd:cd01488  81 KDEEFYRQFNII 92
PRK08328 PRK08328
hypothetical protein; Provisional
 22-167 1.75e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 57.50  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    22 QYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRN----RAE 97
Cdd:PRK08328   9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpkplSAK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    98 ASLERAQNlnpmvDVKVDTEDVEKKPESFFTKFDAVcltccsrDVIIK----------VDQICHRNSIKFFTGDVFGYHG 167
Cdd:PRK08328  89 WKLERFNS-----DIKIETFVGRLSEENIDEVLKGV-------DVIVDcldnfetrylLDDYAHKKGIPLVHGAVEGTYG 156
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 42-169 2.03e-09

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: 57.20  E-value: 2.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNP---MVDVKVDTED 118
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPnckVVPYQNKVGP 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 9790247  119 VEKKPESFFTKFDavcLTCCSRDVIIK---VDQICHRNSIKFFTGDVFGYHGYT 169
Cdd:cd01484  81 EQDFNDTFFEQFH---IIVNALDNIIArryVNGMLIFLIVPLIESGTEGFKGNA 131
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 21-120 1.00e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 56.25  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    21 AQYDRQ--IRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEA 98
Cdd:PRK07878  21 ARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQS 100

                         90       100
                 ....*....|....*....|..
gi 9790247    99 SLERAQNLNPMVDVKVDTEDVE 120
Cdd:PRK07878 101 ARDSIVEINPLVNVRLHEFRLD 122
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 42-133 2.49e-08

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: 54.69  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPMV-------DVKV 114
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVkivayhaNIKD 80

                        90
                ....*....|....*....
gi 9790247  115 DTEDVEkkpesFFTKFDAV 133
Cdd:cd01489  81 PDFNVE-----FFKQFDLV 94
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 42-134 2.82e-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: 52.77  E-value: 2.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQ--FLIQtgsVGRNRAEASLERAQNLNPMVDVKVDTEDV 119
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQqyFLSQ---IGEPKVEALKENLREINPFVKIEAINIKI 77

                        90
                ....*....|....*.
gi 9790247  120 EKKP-ESFFTKFDAVC 134
Cdd:cd01487  78 DENNlEGLFGDCDIVV 93
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
31-134 4.85e-08

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 52.94  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    31 GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQ--FLIQtgsVGRNRAEASLERAQNLNP 108
Cdd:PRK08644  19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQqyFISQ---IGMPKVEALKENLLEINP 95

                         90       100
                 ....*....|....*....|....*..
gi 9790247   109 MVDVKVDTEDVEKKP-ESFFTKFDAVC 134
Cdd:PRK08644  96 FVEIEAHNEKIDEDNiEELFKDCDIVV 122
PRK14852 PRK14852
hypothetical protein; Provisional
 23-129 1.55e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 53.16  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    23 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLER 102
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100
                 ....*....|....*....|....*..
gi 9790247   103 AQNLNPMVDVKVDTEDVEKKPESFFTK 129
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETIDAFLK 421
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 22-133 2.32e-07

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: 52.58  E-value: 2.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247      22 QYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGV----KG-LTMLDHEQVSPEDPGAQFLIQTGSVGRNRA 96
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkKGmITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 9790247      97 EASLERAQNLNPMVDVKVDTEDVEKKPES-----FFTKFDAV 133
Cdd:TIGR01408  481 YTAADATLKINPQIKIDAHQNRVGPETETifndeFYEKLDVV 522
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
21-114 2.81e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 51.66  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    21 AQYDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEA 98
Cdd:PRK07411  17 ERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIES 96

                         90
                 ....*....|....*.
gi 9790247    99 SLERAQNLNPMVDVKV 114
Cdd:PRK07411  97 AKNRILEINPYCQVDL 112
PRK14851 PRK14851
hypothetical protein; Provisional
 20-133 7.89e-07

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 50.63  E-value: 7.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    20 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEAS 99
Cdd:PRK14851  23 EAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVM 102

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 9790247   100 LERAQNLNPMVDVKVDTEDV-EKKPESFFTKFDAV 133
Cdd:PRK14851 103 KEQALSINPFLEITPFPAGInADNMDAFLDGVDVV 137
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 23-183 9.28e-07

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 49.99  E-value: 9.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    23 YDRQIRLW--GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRN--RAEA 98
Cdd:PRK07688   5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    99 SLERAQNLNPMVDVKVDTEDVekKPESFFTKFDAVcltccsrDVIIK----------VDQICHRNSIKFFTGDVFGYHGY 168
Cdd:PRK07688  85 AKKRLEEINSDVRVEAIVQDV--TAEELEELVTGV-------DLIIDatdnfetrfiVNDAAQKYGIPWIYGACVGSYGL 155

                        170
                 ....*....|....*
gi 9790247   169 TFAnlgeheFVEEKT 183
Cdd:PRK07688 156 SYT------IIPGKT 164
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 42-113 2.81e-06

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: 48.52  E-value: 2.81e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSV--GRNRAEASLERAQNLNPMVDVK 113
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDAT 74
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 22-75 1.27e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 46.65  E-value: 1.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 9790247    22 QYDRQIRLWGL--EAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQV 75
Cdd:PRK12475   4 RYSRQILFSGIgeEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYV 59
PRK08223 PRK08223
hypothetical protein; Validated
 33-122 1.99e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 45.83  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    33 EAQKRLRASRVLIVGMKGLGAeiAKNLILA--GVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPMV 110
Cdd:PRK08223  20 TEQQRLRNSRVAIAGLGGVGG--IHLLTLArlGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPEL 97

                         90
                 ....*....|..
gi 9790247   111 DVKVDTEDVEKK 122
Cdd:PRK08223  98 EIRAFPEGIGKE 109
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 42-133 2.19e-04

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: 42.66  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247   42 RVLIVGMKGLGAEIAKNLILAGVK-----GLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLNPMVDV---- 112
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKItalq 80

                        90       100
                ....*....|....*....|....
gi 9790247  113 -KV--DTEDVEKkpESFFTKFDAV 133
Cdd:cd01490  81 nRVgpETEHIFN--DEFWEKLDGV 102
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 28-114 7.15e-04

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 40.94  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247    28 RLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQTGSVGRNRAEASLERAQNLN 107
Cdd:PRK15116  18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQIN 97


                 ....*..
gi 9790247   108 PMVDVKV 114
Cdd:PRK15116  98 PECRVTV 104
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 37-141 7.83e-04

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: 41.46  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790247     37 RLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIQ-TGSVGRNR-----AEASLER-------- 102
Cdd:TIGR01381 335 RYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNfEDCLLGGRgkaetAQKALKRifpsiqat 414

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 9790247    103 AQNLN-PMVDVKVDTEDVE------KKPESFFTKFDAVCLTCCSRD 141
Cdd:TIGR01381 415 GHRLTvPMPGHPIDEKDVPelekdiARLEQLIKDHDVVFLLLDSRE 460
 
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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