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Conserved domains on  [gi|58865692|ref|NP_001012063|]
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SUMO-activating enzyme subunit 1 [Rattus norvegicus]

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 ...
 19-344 1.44e-100

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: 294.97  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  19 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEAS 98
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  99 LERAQNLNPMVDVKVDTEDIEKKPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 178
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 179 eektkvtkvsqgvedgpdakrakldssettmvkkkvlfcpvkealavdwsgekaqaalkrtapdyfllqvllkfrtdkgr 258
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 259 dptsdsysedaelllqirndvfdslgvspdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 338
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 58865692 339 GSGIVE 344
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 ...
 19-344 1.44e-100

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: 294.97  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  19 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEAS 98
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  99 LERAQNLNPMVDVKVDTEDIEKKPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 178
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 179 eektkvtkvsqgvedgpdakrakldssettmvkkkvlfcpvkealavdwsgekaqaalkrtapdyfllqvllkfrtdkgr 258
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 259 dptsdsysedaelllqirndvfdslgvspdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 338
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 58865692 339 GSGIVE 344
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 22-340 3.04e-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: 170.13  E-value: 3.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   100 ERAQNLNPMVDVKVDTEDIEKK-PESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFAnlgeheFV 178
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   179 EEKTKVTKVSQGVEDGPdakrakldssettmvkKKVLFCPVKEALavdwsgekaqaalkrtapdyfllqvllkfrtdkgr 258
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPP----------------KLVPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   259 dptsdsysedaelllqirndvfdslgvspdllpddfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 336
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 58865692   337 MKGS 340
Cdd:pfam00899 220 LTMT 223
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 22-348 2.68e-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: 2.68e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692     22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    102 AQNLNPMVDVKVDTEDIEkkpESFFTEFDAVCLTCCSKDVIIKVDQICHRN--SIKFFTGDVFGYHGYTFANLGEhEFV- 178
Cdd:TIGR01408   87 LAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGD-EFEv 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    179 ------EEKT----KVTKVSQGV-----------EDGP--------------DAKRAK----------LDSSET------ 207
Cdd:TIGR01408  163 ldtdgeEPKTgfiaSITQANPGIvtclenhrhklETGDfvtfrevngmtglnDGSPRKitvispysfsIGDTTElgpylh 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    208 ----TMVK--KKVLFCPVKEALA------VDWSGEKAqaalkrtAPDYFL-LQVLLKFRTDKGRDPTSDSySEDAELLLQ 274
Cdd:TIGR01408  243 ggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPER-------PPEIHTaFQALDQFQEKYSRKPNVGC-QQDAEELLK 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58865692    275 IRNDVFDSLGVSPDLLPDDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgsgIVECLGP 348
Cdd:TIGR01408  315 LATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLPSLGK 389
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 22-167 5.71e-26

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: 104.06  E-value: 5.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865692 100 ERAQNLNPMVDV-----KVDTEDIekkpESFFTEFDAVcLTCC-SKDVIIKVDQICHRNSIKFFTGDVFGYHGY 167
Cdd:COG0476  88 ERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdNFATRYLLNDACVKLGIPLVSGAVIGFEGQ 156
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 22-115 5.69e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.42  E-value: 5.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:PRK05690  13 YNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                         90
                 ....*....|....*.
gi 58865692  100 ERAQNLNPmvDVKVDT 115
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 ...
 19-344 1.44e-100

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: 294.97  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  19 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEAS 98
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  99 LERAQNLNPMVDVKVDTEDIEKKPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLgehefv 178
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 179 eektkvtkvsqgvedgpdakrakldssettmvkkkvlfcpvkealavdwsgekaqaalkrtapdyfllqvllkfrtdkgr 258
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 259 dptsdsysedaelllqirndvfdslgvspdllpddfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 338
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 58865692 339 GSGIVE 344
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 22-340 3.04e-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: 170.13  E-value: 3.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   100 ERAQNLNPMVDVKVDTEDIEKK-PESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFAnlgeheFV 178
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   179 EEKTKVTKVSQGVEDGPdakrakldssettmvkKKVLFCPVKEALavdwsgekaqaalkrtapdyfllqvllkfrtdkgr 258
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPP----------------KLVPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   259 dptsdsysedaelllqirndvfdslgvspdllpddfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 336
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 58865692   337 MKGS 340
Cdd:pfam00899 220 LTMT 223
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 22-169 5.80e-50

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: 165.67  E-value: 5.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSV--GQNRAEASL 99
Cdd:cd01485   2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASY 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865692 100 ERAQNLNPMVDVKVDTED---IEKKPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTF 169
Cdd:cd01485  82 EFLQELNPNVKLSIVEEDslsNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAF 154
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 22-349 1.99e-49

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: 167.06  E-value: 1.99e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:cd01491   2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 102 AQNLNPMVDVKVDTEDIEKkpeSFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLGEHEFVEEK 181
Cdd:cd01491  82 LAELNPYVPVTVSTGPLTT---DELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGDEFTVYDP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 182 T----------KVTKVSQGVEDGPDAKRAKLDSSETtmvkkkvlfcpvkealaVDWSGEKAQAALKRTAPdyfllqvllK 251
Cdd:cd01491 159 NgeepksgmisSISKDNPGVVTCLDETRHGFEDGDY-----------------VTFSEVEGMTELNGCEP---------R 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 252 FRTDKGrdPTSDSYSEDAELLLQIRNDVFDSlgvspdllpddfvrycfSEMAPVCAVVGGILAQEIVKALSQRDPPHNNF 331
Cdd:cd01491 213 KIKVKG--PYTFSIGDTSSFSEYIRGGIVTQ-----------------VKLSPMAAFFGGLAAQEVLKACSGKFTPLKQW 273

                       330
                ....*....|....*...
gi 58865692 332 FFFDGmkgsgiVECLGPQ 349
Cdd:cd01491 274 LYFDA------LECLPED 285
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 22-348 2.68e-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: 2.68e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692     22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:TIGR01408    7 YSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    102 AQNLNPMVDVKVDTEDIEkkpESFFTEFDAVCLTCCSKDVIIKVDQICHRN--SIKFFTGDVFGYHGYTFANLGEhEFV- 178
Cdd:TIGR01408   87 LAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFGD-EFEv 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    179 ------EEKT----KVTKVSQGV-----------EDGP--------------DAKRAK----------LDSSET------ 207
Cdd:TIGR01408  163 ldtdgeEPKTgfiaSITQANPGIvtclenhrhklETGDfvtfrevngmtglnDGSPRKitvispysfsIGDTTElgpylh 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692    208 ----TMVK--KKVLFCPVKEALA------VDWSGEKAqaalkrtAPDYFL-LQVLLKFRTDKGRDPTSDSySEDAELLLQ 274
Cdd:TIGR01408  243 ggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPER-------PPEIHTaFQALDQFQEKYSRKPNVGC-QQDAEELLK 314

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58865692    275 IRNDVFDSLGVSPDLLPDDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgsgIVECLGP 348
Cdd:TIGR01408  315 LATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLPSLGK 389
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 22-337 4.38e-31

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: 121.64  E-value: 4.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:cd01493   3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 102 AQNLNPMVD----VKVDTEDIEKKPeSFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGYTFANLGEHEF 177
Cdd:cd01493  83 LQELNPDVNgsavEESPEALLDNDP-SFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHTI 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 178 VE-----------------------------------------------------------------EKTKVTKV----- 187
Cdd:cd01493 162 VEshpdnaledlrldnpfpelrehadsidlddmdpaehshtpyivilikylekwrsahngqlpstykEKKEFRDLvrslm 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 188 -SQGVEDGPD-AKRAKLDSSETTMVKKKVlfcpvkEALAVDWSGEKAQ----------AALKR-------------TAPD 242
Cdd:cd01493 242 rSNEDEENFEeAIKAVNKALNRTKIPSSV------EEIFNDDRCENLTsqsssfwimaRALKEfvaeengllplpgTLPD 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692 243 -------YFLLQVLLKfrtDKGRDptsdsyseDAELLLQIRNDVFDSLGVSPDLLPDD------------FVRYCFSEMA 303
Cdd:cd01493 316 mtadtekYIKLQNIYR---EKAEK--------DAAEVEKYVREILKSLGRSPDSISDKeiklfcknaaflRVIRGRSLEH 384

                       410       420       430
                ....*....|....*....|....*....|....
gi 58865692 304 PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGM 337
Cdd:cd01493 385 NISAFMGGIAAQEVIKLITKQYVPIDNTFIFDGI 418
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 22-167 5.71e-26

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: 104.06  E-value: 5.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:COG0476   8 YSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865692 100 ERAQNLNPMVDV-----KVDTEDIekkpESFFTEFDAVcLTCC-SKDVIIKVDQICHRNSIKFFTGDVFGYHGY 167
Cdd:COG0476  88 ERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdNFATRYLLNDACVKLGIPLVSGAVIGFEGQ 156
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 22-167 7.14e-24

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: 97.93  E-value: 7.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58865692 100 ERAQNLNPmvDVKVDTEDIEKKPESFFTEFDAVcltccskDVIIK----------VDQICHRNSIKFFTGDVFGYHGY 167
Cdd:cd00757  82 ERLRAINP--DVEIEAYNERLDAENAEELIAGY-------DLVLDctdnfatrylINDACVKLGKPLVSGAVLGFEGQ 150
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 41-167 1.05e-22

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: 92.33  E-value: 1.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPMVDVKVDTEDIEK 120
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58865692 121 -KPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHGY 167
Cdd:cd01483  81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGD 128
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 22-115 5.69e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.42  E-value: 5.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:PRK05690  13 YNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                         90
                 ....*....|....*.
gi 58865692  100 ERAQNLNPmvDVKVDT 115
Cdd:PRK05690  93 AALARINP--HIAIET 106
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 20-116 1.06e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 74.14  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   20 AQYDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEA 97
Cdd:PRK05597   7 ARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAES 86

                         90
                 ....*....|....*....
gi 58865692   98 SLERAQNLNPMVDVKVDTE 116
Cdd:PRK05597  87 AREAMLALNPDVKVTVSVR 105
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 30-158 9.94e-14

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 69.56  E-value: 9.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  30 GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPM- 108
Cdd:cd00755   2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPEc 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 58865692 109 -VDVKVDTEDIEKKPESFFTEFDAVcLTCCSkDVIIKVDQI--CHRNSIKFFT 158
Cdd:cd00755  82 eVDAVEEFLTPDNSEDLLGGDPDFV-VDAID-SIRAKVALIayCRKRKIPVIS 132
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 19-111 1.60e-13

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 70.09  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   19 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRtGSVGQNRAEAS 98
Cdd:PTZ00245   6 AVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQ-GEAGGTRGARA 84

                         90
                 ....*....|...
gi 58865692   99 LERAQNLNPMVDV 111
Cdd:PTZ00245  85 LGALQRLNPHVSV 97
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 41-132 5.89e-13

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: 68.54  E-value: 5.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPMVDVKVDTEDIEK 120
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90
                ....*....|..
gi 58865692 121 KPESFFTEFDAV 132
Cdd:cd01488  81 KDEEFYRQFNII 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
22-119 1.03e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 68.50  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   22 YDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASL 99
Cdd:PRK08762 116 YSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAA 195

                         90       100
                 ....*....|....*....|....*
gi 58865692  100 ERAQNLNPMVDV-----KVDTEDIE 119
Cdd:PRK08762 196 QRLAALNPDVQVeavqeRVTSDNVE 220
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 24-118 5.89e-12

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 66.06  E-value: 5.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   24 RQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:PRK05600  24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                         90
                 ....*....|....*..
gi 58865692  102 AQNLNPMVDVKVDTEDI 118
Cdd:PRK05600 104 LKEIQPDIRVNALRERL 120
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 41-168 1.89e-11

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: 62.98  E-value: 1.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNP---MVDVKVDTED 117
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPnckVVPYQNKVGP 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 58865692 118 IEKKPESFFTEFDAVclTCCSKDVIIK--VDQICHRNSIKFFTGDVFGYHGYT 168
Cdd:cd01484  81 EQDFNDTFFEQFHII--VNALDNIIARryVNGMLIFLIVPLIESGTEGFKGNA 131
PRK08328 PRK08328
hypothetical protein; Provisional
 21-166 8.60e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 58.27  E-value: 8.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   21 QYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQN----RAE 96
Cdd:PRK08328   9 RYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpkplSAK 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865692   97 ASLERAQNlnpmvDVKVDT---EDIEKKPESFFTEFDAVCLTCCSKDVIIKVDQICHRNSIKFFTGDVFGYHG 166
Cdd:PRK08328  89 WKLERFNS-----DIKIETfvgRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYG 156
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 41-133 9.76e-10

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: 57.01  E-value: 9.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLiRTGSVGQNRAEASLERAQNLNPMVDVKVDTEDIEK 120
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90
                ....*....|....
gi 58865692 121 KP-ESFFTEFDAVC 133
Cdd:cd01487  80 NNlEGLFGDCDIVV 93
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 41-132 1.26e-09

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 58.54  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPMV-------DVKV 113
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVkivayhaNIKD 80

                        90
                ....*....|....*....
gi 58865692 114 DTEDIEkkpesFFTEFDAV 132
Cdd:cd01489  81 PDFNVE-----FFKQFDLV 94
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
30-133 1.92e-09

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 56.79  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   30 GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQF-LIRtgSVGQNRAEASLERAQNLNPM 108
Cdd:PRK08644  19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQyFIS--QIGMPKVEALKENLLEINPF 96

                         90       100
                 ....*....|....*....|....*.
gi 58865692  109 VDVKVDTEDIEKKP-ESFFTEFDAVC 133
Cdd:PRK08644  97 VEIEAHNEKIDEDNiEELFKDCDIVV 122
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 20-119 3.63e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 57.80  E-value: 3.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   20 AQYDRQ--IRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEA 97
Cdd:PRK07878  21 ARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQS 100

                         90       100
                 ....*....|....*....|..
gi 58865692   98 SLERAQNLNPMVDVKVDTEDIE 119
Cdd:PRK07878 101 ARDSIVEINPLVNVRLHEFRLD 122
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 21-132 1.44e-08

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: 56.44  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692     21 QYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGV----KG-LTMLDHEQVSPEDLGAQFLIRTGSVGQNRA 95
Cdd:TIGR01408  401 RYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkKGmITVTDPDLIEKSNLNRQFLFRPHHIGKPKS 480

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 58865692     96 EASLERAQNLNPMVDVKVDTEDIEKKPES-----FFTEFDAV 132
Cdd:TIGR01408  481 YTAADATLKINPQIKIDAHQNRVGPETETifndeFYEKLDVV 522
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
20-113 3.03e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 54.74  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   20 AQYDRQIRL--WGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEA 97
Cdd:PRK07411  17 ERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIES 96

                         90
                 ....*....|....*.
gi 58865692   98 SLERAQNLNPMVDVKV 113
Cdd:PRK07411  97 AKNRILEINPYCQVDL 112
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 22-182 6.90e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 53.46  E-value: 6.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   22 YDRQIRLW--GLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQN--RAEA 97
Cdd:PRK07688   5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   98 SLERAQNLNPMVDVKVDTEDIekKPESFFTEFDAVcltccskDVIIK----------VDQICHRNSIKFFTGDVFGYHGY 167
Cdd:PRK07688  85 AKKRLEEINSDVRVEAIVQDV--TAEELEELVTGV-------DLIIDatdnfetrfiVNDAAQKYGIPWIYGACVGSYGL 155

                        170
                 ....*....|....*
gi 58865692  168 TFAnlgeheFVEEKT 182
Cdd:PRK07688 156 SYT------IIPGKT 164
PRK14851 PRK14851
hypothetical protein; Provisional
 19-132 1.28e-07

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 53.33  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   19 AAQYDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEAS 98
Cdd:PRK14851  23 EAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVM 102

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 58865692   99 LERAQNLNPMVDVKVDTEDI-EKKPESFFTEFDAV 132
Cdd:PRK14851 103 KEQALSINPFLEITPFPAGInADNMDAFLDGVDVV 137
PRK14852 PRK14852
hypothetical protein; Provisional
 22-130 1.29e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 53.55  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   22 YDRQIRLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLER 101
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100       110
                 ....*....|....*....|....*....|
gi 58865692  102 AQNLNPMVDVKVDTEDIEKKP-ESFFTEFD 130
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETiDAFLKDVD 424
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 41-132 1.77e-06

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: 49.21  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVK-----GLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPMVDV---- 111
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKItalq 80

                        90       100
                ....*....|....*....|....
gi 58865692 112 -KV--DTEDIEKkpESFFTEFDAV 132
Cdd:cd01490  81 nRVgpETEHIFN--DEFWEKLDGV 102
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 21-111 2.59e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 48.57  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   21 QYDRQIRLWGL--EAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIrTGSVGQNR---A 95
Cdd:PRK12475   4 RYSRQILFSGIgeEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLY-TEEDAKQKkpkA 82

                         90
                 ....*....|....*.
gi 58865692   96 EASLERAQNLNPMVDV 111
Cdd:PRK12475  83 IAAKEHLRKINSEVEI 98
PRK08223 PRK08223
hypothetical protein; Validated
 32-121 8.46e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 46.60  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   32 EAQKRLRASRVLIVGMKGLGAeiAKNLILA--GVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLNPMV 109
Cdd:PRK08223  20 TEQQRLRNSRVAIAGLGGVGG--IHLLTLArlGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPEL 97

                         90
                 ....*....|..
gi 58865692  110 DVKVDTEDIEKK 121
Cdd:PRK08223  98 EIRAFPEGIGKE 109
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 41-112 7.37e-05

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


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 43.90  E-value: 7.37e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865692  41 RVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSV--GQNRAEASLERAQNLNPMVDVK 112
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDAT 74
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 27-113 1.15e-04

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 43.25  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865692   27 RLWGLEAQKRLRASRVLIVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDLGAQFLIRTGSVGQNRAEASLERAQNLN 106
Cdd:PRK15116  18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQIN 97


                 ....*..
gi 58865692  107 PMVDVKV 113
Cdd:PRK15116  98 PECRVTV 104
 
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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