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Conserved domains on  [gi|42559897|sp|Q9UBE0|]
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RecName: Full=SUMO-activating enzyme subunit 1; AltName: Full=Ubiquitin-like 1-activating enzyme E1A; Contains: RecName: Full=SUMO-activating enzyme subunit 1, N-terminally processed

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 ...
 16-341 2.36e-103

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: 301.90  E-value: 2.36e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  16 AAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEAS 95
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  96 LERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLgehefv 175
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 176 eektkvakvsqgvedgpdtkrakldssettmvkkkvvfcpvkealevdwssekakaalkrttsdyfllqvllkfrtdkgr 255
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 256 dpssdtyeedselllqirndvldslgispdllpedfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 335
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 42559897 336 GNGIVE 341
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 ...
 16-341 2.36e-103

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: 301.90  E-value: 2.36e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  16 AAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEAS 95
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  96 LERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLgehefv 175
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 176 eektkvakvsqgvedgpdtkrakldssettmvkkkvvfcpvkealevdwssekakaalkrttsdyfllqvllkfrtdkgr 255
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 256 dpssdtyeedselllqirndvldslgispdllpedfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 335
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 42559897 336 GNGIVE 341
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-337 7.92e-54

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: 176.68  E-value: 7.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    19 YDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASL 96
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    97 ERAQNLNPMVDVKVDTEDIEKK-PESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFAnlgeheFV 175
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   176 EEKTKVAKVSQGVEDGPDTkrakldssettmvkkkVVFCPVKEALevdwssekakaalkrttsdyfllqvllkfrtdkgr 255
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPPKL----------------VPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   256 dpssdtyeedselllqirndvldslgispdllpedfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 333
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 42559897   334 MKGN 337
Cdd:pfam00899 220 LTMT 223
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 13-345 4.10e-40

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: 150.42  E-value: 4.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897     13 EEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRA 92
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897     93 EASLERAQNLNPMVDVKVDTEDIEkkpESFFTQFDAVCLTCCSRDVIVKVDQICHKN--SIKFFTGDVFGYHGYTFANLG 170
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    171 EhEFV-------EEKTK-VAKVSQ--------------GVEDGP--------------DTKRAK----------LDSSET 204
Cdd:TIGR01408  158 D-EFEvldtdgeEPKTGfIASITQanpgivtclenhrhKLETGDfvtfrevngmtglnDGSPRKitvispysfsIGDTTE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    205 ----------TMVK--KKVVFCPVKEALE------VDWSSEKAKAALkrttsdYFLLQVLLKFRTDKGRDPSSDTyEEDS 266
Cdd:TIGR01408  237 lgpylhggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPERPPEI------HTAFQALDQFQEKYSRKPNVGC-QQDA 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    267 ELLLQIRNDVLDSLGISPDLLPEDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgngIVE 341
Cdd:TIGR01408  310 EELLKLATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLP 385


                   ....
gi 42559897    342 CLGP 345
Cdd:TIGR01408  386 SLGK 389
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 12-164 4.48e-25

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: 101.36  E-value: 4.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  12 SEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGR 89
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  90 NRAEASLERAQNLNPMVDV-----KVDTEDIekkpESFFTQFDAVcLTCC----SRDVIvkvDQICHKNSIKFFTGDVFG 160
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdnfaTRYLL---NDACVKLGIPLVSGAVIG 152


                ....
gi 42559897 161 YHGY 164
Cdd:COG0476 153 FEGQ 156
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 13-108 4.31e-15

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 74.71  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   13 EEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRtGSVGRNRA 92
Cdd:PTZ00245   3 DAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQ-GEAGGTRG 81

                         90
                 ....*....|....*.
gi 42559897   93 EASLERAQNLNPMVDV 108
Cdd:PTZ00245  82 ARALGALQRLNPHVSV 97
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 16-341 2.36e-103

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: 301.90  E-value: 2.36e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  16 AAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEAS 95
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  96 LERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLgehefv 175
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 176 eektkvakvsqgvedgpdtkrakldssettmvkkkvvfcpvkealevdwssekakaalkrttsdyfllqvllkfrtdkgr 255
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 256 dpssdtyeedselllqirndvldslgispdllpedfvrycfseMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMK 335
Cdd:cd01492 155 -------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNFFVFDGET 191


                ....*.
gi 42559897 336 GNGIVE 341
Cdd:cd01492 192 SEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-337 7.92e-54

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: 176.68  E-value: 7.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    19 YDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASL 96
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    97 ERAQNLNPMVDVKVDTEDIEKK-PESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFAnlgeheFV 175
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPEnAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTV------VI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   176 EEKTKVAKVSQGVEDGPDTkrakldssettmvkkkVVFCPVKEALevdwssekakaalkrttsdyfllqvllkfrtdkgr 255
Cdd:pfam00899 155 PGKTPCYRCLFPEDPPPKL----------------VPSCTVAGVL----------------------------------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   256 dpssdtyeedselllqirndvldslgispdllpedfvrycfsemAPVCAVVGGILAQEIVKALSQRDPPH--NNFFFFDG 333
Cdd:pfam00899 184 --------------------------------------------GPTTAVVAGLQALEALKLLLGKGEPNlaGRLLQFDA 219


                  ....
gi 42559897   334 MKGN 337
Cdd:pfam00899 220 LTMT 223
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 19-345 4.94e-48

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: 163.21  E-value: 4.94e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  19 YDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLER 98
Cdd:cd01491   2 YSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  99 AQNLNPMVDVKVDTEDIEKkpeSFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEhEFV--- 175
Cdd:cd01491  82 LAELNPYVPVTVSTGPLTT---DELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFGD-EFTvyd 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 176 --EEKTK---VAKVSQGvEDGpdtkrakldssettmvkkkVVFCpvkealevdwsseKAKAALKRTTSDYfllqvlLKFR 250
Cdd:cd01491 158 pnGEEPKsgmISSISKD-NPG-------------------VVTC-------------LDETRHGFEDGDY------VTFS 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 251 TDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPdLLPEDFVRYcfSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFF 330
Cdd:cd01491 199 EVEGMTELNGCEPRKIKVKGPYTFSIGDTSSFSE-YIRGGIVTQ--VKLSPMAAFFGGLAAQEVLKACSGKFTPLKQWLY 275

                       330
                ....*....|....*
gi 42559897 331 FDGmkgngiVECLGP 345
Cdd:cd01491 276 FDA------LECLPE 284
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 19-166 1.30e-47

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: 159.51  E-value: 1.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  19 YDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSV--GRNRAEASL 96
Cdd:cd01485   2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAASY 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559897  97 ERAQNLNPMVDVKVDTED---IEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTF 166
Cdd:cd01485  82 EFLQELNPNVKLSIVEEDslsNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAF 154
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 13-345 4.10e-40

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: 150.42  E-value: 4.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897     13 EEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRA 92
Cdd:TIGR01408    1 EIDEALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897     93 EASLERAQNLNPMVDVKVDTEDIEkkpESFFTQFDAVCLTCCSRDVIVKVDQICHKN--SIKFFTGDVFGYHGYTFANLG 170
Cdd:TIGR01408   81 EAVVKKLAELNPYVHVSSSSVPFN---EEFLDKFQCVVLTEMSLPLQKEINDFCHSQcpPIAFISADVRGLFGSLFCDFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    171 EhEFV-------EEKTK-VAKVSQ--------------GVEDGP--------------DTKRAK----------LDSSET 204
Cdd:TIGR01408  158 D-EFEvldtdgeEPKTGfIASITQanpgivtclenhrhKLETGDfvtfrevngmtglnDGSPRKitvispysfsIGDTTE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    205 ----------TMVK--KKVVFCPVKEALE------VDWSSEKAKAALkrttsdYFLLQVLLKFRTDKGRDPSSDTyEEDS 266
Cdd:TIGR01408  237 lgpylhggiaTQVKtpKTVFFKSLREQLKdpkcliVDFSKPERPPEI------HTAFQALDQFQEKYSRKPNVGC-QQDA 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    267 ELLLQIRNDVLDSLGISPDLLPEDFVRYcFSEMA-----PVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKgngIVE 341
Cdd:TIGR01408  310 EELLKLATSISETLEEKVPDVDAKLVHW-LSWTAqgflsPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSAE---SLP 385


                   ....
gi 42559897    342 CLGP 345
Cdd:TIGR01408  386 SLGK 389
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 19-334 2.78e-34

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: 130.50  E-value: 2.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  19 YDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLER 98
Cdd:cd01493   3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  99 AQNLNPMVD----VKVDTEDIEKKPeSFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEH-- 172
Cdd:cd01493  83 LQELNPDVNgsavEESPEALLDNDP-SFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRIQLKEHti 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 173 ----------------------EFVEEKT-------------------KVAKVSQGVEDG--PDTKRakldssETTMVKK 209
Cdd:cd01493 162 veshpdnaledlrldnpfpelrEHADSIDlddmdpaehshtpyiviliKYLEKWRSAHNGqlPSTYK------EKKEFRD 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 210 KVVFCPVKEALE--VDWSSEKAKAALKRT---------------------TSDYFLLQVLLK-FRTDKGRDP-------- 257
Cdd:cd01493 236 LVRSLMRSNEDEenFEEAIKAVNKALNRTkipssveeifnddrcenltsqSSSFWIMARALKeFVAEENGLLplpgtlpd 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897 258 ---SSDTY-----------EEDSELLLQIRNDVLDSLGISPDLLPED------------FVRYCFSEMAPVCAVVGGILA 311
Cdd:cd01493 316 mtaDTEKYiklqniyrekaEKDAAEVEKYVREILKSLGRSPDSISDKeiklfcknaaflRVIRGRSLEHNISAFMGGIAA 395

                       410       420
                ....*....|....*....|...
gi 42559897 312 QEIVKALSQRDPPHNNFFFFDGM 334
Cdd:cd01493 396 QEVIKLITKQYVPIDNTFIFDGI 418
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 12-164 4.48e-25

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: 101.36  E-value: 4.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  12 SEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGR 89
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  90 NRAEASLERAQNLNPMVDV-----KVDTEDIekkpESFFTQFDAVcLTCC----SRDVIvkvDQICHKNSIKFFTGDVFG 160
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVeaipeRLTEENA----LELLAGADLV-LDCTdnfaTRYLL---NDACVKLGIPLVSGAVIG 152


                ....
gi 42559897 161 YHGY 164
Cdd:COG0476 153 FEGQ 156
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 38-164 1.40e-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: 89.25  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEK 117
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 42559897 118 -KPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGY 164
Cdd:cd01483  81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGD 128
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 19-164 6.19e-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: 89.84  E-value: 6.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  19 YDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASL 96
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42559897  97 ERAQNLNPMVDVKVDTEDI-EKKPESFFTQFDAVcLTCC----SRDVIvkvDQICHKNSIKFFTGDVFGYHGY 164
Cdd:cd00757  82 ERLRAINPDVEIEAYNERLdAENAEELIAGYDLV-LDCTdnfaTRYLI---NDACVKLGKPLVSGAVLGFEGQ 150
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 13-108 4.31e-15

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 74.71  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   13 EEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRtGSVGRNRA 92
Cdd:PTZ00245   3 DAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQ-GEAGGTRG 81

                         90
                 ....*....|....*.
gi 42559897   93 EASLERAQNLNPMVDV 108
Cdd:PTZ00245  82 ARALGALQRLNPHVSV 97
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-112 9.01e-15

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 72.96  E-value: 9.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   12 SEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGR 89
Cdd:PRK05690   6 SDEEMLRYNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQ 85

                         90       100
                 ....*....|....*....|...
gi 42559897   90 NRAEASLERAQNLNPmvDVKVDT 112
Cdd:PRK05690  86 PKVESARAALARINP--HIAIET 106
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 11-113 5.92e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 68.75  E-value: 5.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   11 ISEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVG 88
Cdd:PRK05597   1 VKNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVG 80

                         90       100
                 ....*....|....*....|....*
gi 42559897   89 RNRAEASLERAQNLNPMVDVKVDTE 113
Cdd:PRK05597  81 QPKAESAREAMLALNPDVKVTVSVR 105
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-116 3.31e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 66.96  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   12 SEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGR 89
Cdd:PRK08762 109 TDEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQ 188

                         90       100       110
                 ....*....|....*....|....*....|..
gi 42559897   90 NRAEASLERAQNLNPMVDV-----KVDTEDIE 116
Cdd:PRK08762 189 PKVDSAAQRLAALNPDVQVeavqeRVTSDNVE 220
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 27-155 3.44e-12

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: 65.32  E-value: 3.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  27 GLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPM- 105
Cdd:cd00755   2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPEc 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42559897 106 -VDVKVDTEDIEKKPESFFTQFDAVcLTCCSrDVIVKVDQI--CHKNSIKFFT 155
Cdd:cd00755  82 eVDAVEEFLTPDNSEDLLGGDPDFV-VDAID-SIRAKVALIayCRKRKIPVIS 132
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 38-129 7.52e-12

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: 65.07  E-value: 7.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEK 117
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90
                ....*....|..
gi 42559897 118 KPESFFTQFDAV 129
Cdd:cd01488  81 KDEEFYRQFNII 92
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 21-115 1.56e-11

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 64.90  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   21 RQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLER 98
Cdd:PRK05600  24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                         90
                 ....*....|....*..
gi 42559897   99 AQNLNPMVDVKVDTEDI 115
Cdd:PRK05600 104 LKEIQPDIRVNALRERL 120
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 38-165 3.90e-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: 62.21  E-value: 3.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNP---MVDVKVDTED 114
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPnckVVPYQNKVGP 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42559897 115 IEKKPESFFTQFDAVclTCCSRDVIVK--VDQICHKNSIKFFTGDVFGYHGYT 165
Cdd:cd01484  81 EQDFNDTFFEQFHII--VNALDNIIARryVNGMLIFLIVPLIESGTEGFKGNA 131
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 6-127 1.06e-10

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 62.42  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897    6 EAGGGISEEEAAQYDRQ--IRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIR 83
Cdd:PRK07878  10 EPAAELTRDEVARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHG 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 42559897   84 TGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKK-PESFFTQFD 127
Cdd:PRK07878  90 QSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSnAVELFSQYD 134
PRK08328 PRK08328
hypothetical protein; Provisional
 11-163 1.08e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 60.97  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   11 ISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEqvTPE--DPGAQFLIRTGSVG 88
Cdd:PRK08328   2 LSERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQ--TPElsNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   89 RN----RAEASLERAQNlnpmvDVKVDTEDIEKKPESFFTQFDAVcltccsrDVIVK----------VDQICHKNSIKFF 154
Cdd:PRK08328  80 KNpkplSAKWKLERFNS-----DIKIETFVGRLSEENIDEVLKGV-------DVIVDcldnfetrylLDDYAHKKGIPLV 147


                 ....*....
gi 42559897  155 TGDVFGYHG 163
Cdd:PRK08328 148 HGAVEGTYG 156
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 38-129 2.75e-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: 57.39  E-value: 2.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMV-------DVKV 110
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVkivayhaNIKD 80

                        90
                ....*....|....*....
gi 42559897 111 DTEDIEkkpesFFTQFDAV 129
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. ...
 38-130 3.83e-09

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: 55.47  E-value: 3.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLiRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEK 117
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90
                ....*....|....
gi 42559897 118 KP-ESFFTQFDAVC 130
Cdd:cd01487  80 NNlEGLFGDCDIVV 93
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
11-110 1.85e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 55.51  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   11 ISEEEAAQYDRQIRL--WGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVG 88
Cdd:PRK07411  11 LSKDEYERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100
                 ....*....|....*....|..
gi 42559897   89 RNRAEASLERAQNLNPMVDVKV 110
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDL 112
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 2-129 7.36e-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: 54.12  E-value: 7.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897      2 VEKEEAGGGISEEEAA----QYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGV----KG-LTMLDHEQVT 72
Cdd:TIGR01408  381 AESLPSLGKPECEEFLprgdRYDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkKGmITVTDPDLIE 460

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42559897     73 PEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPES-----FFTQFDAV 129
Cdd:TIGR01408  461 KSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETifndeFYEKLDVV 522
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
27-130 2.99e-07

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 50.24  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   27 GLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVtpeDPG----AQFLIRtgSVGRNRAEASLERAQNL 102
Cdd:PRK08644  19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVV---EPSnlnrQQYFIS--QIGMPKVEALKENLLEI 93

                         90       100
                 ....*....|....*....|....*....
gi 42559897  103 NPMVDVKVDTEDIEKKP-ESFFTQFDAVC 130
Cdd:PRK08644  94 NPFVEIEAHNEKIDEDNiEELFKDCDIVV 122
PRK14851 PRK14851
hypothetical protein; Provisional
 10-129 3.69e-07

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 51.78  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   10 GISEEEA---AQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGS 86
Cdd:PRK14851  14 GISSAAEyreAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPS 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 42559897   87 VGRNRAEASLERAQNLNPMVDVKVDTEDI-EKKPESFFTQFDAV 129
Cdd:PRK14851  94 FGRPKLAVMKEQALSINPFLEITPFPAGInADNMDAFLDGVDVV 137
PRK14852 PRK14852
hypothetical protein; Provisional
 19-127 1.17e-06

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 50.46  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   19 YDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLER 98
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100       110
                 ....*....|....*....|....*....|
gi 42559897   99 AQNLNPMVDVKVDTEDIEKKP-ESFFTQFD 127
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETiDAFLKDVD 424
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 38-109 1.43e-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: 46.21  E-value: 1.43e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSV--GRNRAEASLERAQNLNPMVDVK 109
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDAT 74
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 18-71 2.66e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 45.49  E-value: 2.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 42559897   18 QYDRQIRLWGL--EAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQV 71
Cdd:PRK12475   4 RYSRQILFSGIgeEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYV 59
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 19-179 2.68e-05

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 45.37  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   19 YDRQIRLW--GLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRN--RAEA 94
Cdd:PRK07688   5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   95 SLERAQNLNPMVDVKVDTEDIekKPESFFTQFDAVcltccsrDVIVK----------VDQICHKNSIKFFTGDVFGYHGY 164
Cdd:PRK07688  85 AKKRLEEINSDVRVEAIVQDV--TAEELEELVTGV-------DLIIDatdnfetrfiVNDAAQKYGIPWIYGACVGSYGL 155

                        170
                 ....*....|....*
gi 42559897  165 TFAnlgeheFVEEKT 179
Cdd:PRK07688 156 SYT------IIPGKT 164
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 38-129 3.02e-05

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: 45.36  E-value: 3.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897  38 RVLLVGLKGLGAEIAKNLILAGVK-----GLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDV---- 108
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVGtgesgEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKItalq 80

                        90       100
                ....*....|....*....|....
gi 42559897 109 -KV--DTEDIEKkpESFFTQFDAV 129
Cdd:cd01490  81 nRVgpETEHIFN--DEFWEKLDGV 102
PRK08223 PRK08223
hypothetical protein; Validated
 29-118 1.92e-04

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 42.75  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   29 EAQKRLRASRVLLVGLKGLGAeiAKNLILA--GVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMV 106
Cdd:PRK08223  20 TEQQRLRNSRVAIAGLGGVGG--IHLLTLArlGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPEL 97

                         90
                 ....*....|..
gi 42559897  107 DVKVDTEDIEKK 118
Cdd:PRK08223  98 EIRAFPEGIGKE 109
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 24-110 7.96e-04

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 40.56  E-value: 7.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42559897   24 RLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLN 103
Cdd:PRK15116  18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQIN 97


                 ....*..
gi 42559897  104 PMVDVKV 110
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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