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Conserved domains on  [gi|6325438|ref|NP_015506|]
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E1 ubiquitin-activating protein AOS1 [Saccharomyces cerevisiae S288C]

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 ...
 13-345 3.86e-96

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: 283.41  E-value: 3.86e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   13 IALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDAT 92
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   93 KERIQDLNPRIELNFDKQDLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDLiefise 172
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  173 deklqsvrpttvgpissnrsiievttrkdeedekktyeriktkncyrplnevlstatlkekmtqrqlkrvtsilpltlsl 252
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  253 lqyglnqkgkaisfeqmkrdaavwcenlgvpatvvkddyiqqfikqkgieFAPVAAIIGGAVAQDVINILGKRLSPLNNF 332
Cdd:cd01492 155 --------------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNF 184

                       330
                ....*....|...
gi 6325438  333 IVFDGITLDMPLF 345
Cdd:cd01492 185 FVFDGETSEAPIY 197
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-345 3.86e-96

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: 283.41  E-value: 3.86e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   13 IALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDAT 92
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   93 KERIQDLNPRIELNFDKQDLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDLiefise 172
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  173 deklqsvrpttvgpissnrsiievttrkdeedekktyeriktkncyrplnevlstatlkekmtqrqlkrvtsilpltlsl 252
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  253 lqyglnqkgkaisfeqmkrdaavwcenlgvpatvvkddyiqqfikqkgieFAPVAAIIGGAVAQDVINILGKRLSPLNNF 332
Cdd:cd01492 155 --------------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNF 184

                       330
                ....*....|...
gi 6325438  333 IVFDGITLDMPLF 345
Cdd:cd01492 185 FVFDGETSEAPIY 197
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 16-163 4.70e-28

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: 109.27  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     16 YDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATK 93
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325438     94 ERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV------ATEMQIDEAIKintltrKLNIPLYVAGSNGLFAYVF 163
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENaEELIKSFDIVVdatdnfAARYLVNDACV------KLGKPLIEAGVLGFKGQVT 151
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 11-338 3.26e-26

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: 109.98  E-value: 3.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438      11 DEiALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKID 90
Cdd:TIGR01408    3 DE-ALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438      91 ATKERIQDLNPRIELNFDKQDLqekDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPL-YV-AGSNGLFAYVFIDL-I 167
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPF---NEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIaFIsADVRGLFGSLFCDFgD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     168 EFISEDEKLQSVRPTTVGPISSNRSIIeVTTRKDEEDEKKTYERIKtkncyrpLNEVLSTATLKEKMTQrqlkRVTSILP 247
Cdd:TIGR01408  159 EFEVLDTDGEEPKTGFIASITQANPGI-VTCLENHRHKLETGDFVT-------FREVNGMTGLNDGSPR----KITVISP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     248 LTLSL---LQYGLNQKG---------KAISFEQMKR-------------------------------------------- 271
Cdd:TIGR01408  227 YSFSIgdtTELGPYLHGgiatqvktpKTVFFKSLREqlkdpkclivdfskperppeihtafqaldqfqekysrkpnvgcq 306

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325438     272 -DAAVWCENLGVPATV-------VKDDYIQQFIKQKGIEFAPVAAIIGGAVAQDVINILGKRLSPLNNFIVFDGI 338
Cdd:TIGR01408  307 qDAEELLKLATSISETleekvpdVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSA 381
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 9-163 8.33e-24

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 97.89  E-value: 8.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    9 SEDEIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQ 86
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   87 WKIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV------ATEMQIDEAikintlTRKLNIPLYVAGSNGLF 159
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLdctdnfATRYLLNDA------CVKLGIPLVSGAVIGFE 154


                ....
gi 6325438  160 AYVF 163
Cdd:COG0476 155 GQVT 158
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 6-127 8.74e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 75.65  E-value: 8.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     6 EKLSEDEIALYDRQIRLWGM--TAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSED 83
Cdd:PRK05690   3 AELSDEEMLRYNRQIILRGFdfDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDAT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 6325438    84 VGQWKIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV 127
Cdd:PRK05690  83 IGQPKVESARAALARINPHIAIETINARLDDDElAALIAGHDLVL 127
 
Name Accession Description Interval E-value
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-345 3.86e-96

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: 283.41  E-value: 3.86e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   13 IALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDAT 92
Cdd:cd01492   1 IALYDRQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   93 KERIQDLNPRIELNFDKQDLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDLiefise 172
Cdd:cd01492  81 LERLRALNPRVKVSVDTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFGFVFADL------ 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  173 deklqsvrpttvgpissnrsiievttrkdeedekktyeriktkncyrplnevlstatlkekmtqrqlkrvtsilpltlsl 252
Cdd:cd01492     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  253 lqyglnqkgkaisfeqmkrdaavwcenlgvpatvvkddyiqqfikqkgieFAPVAAIIGGAVAQDVINILGKRLSPLNNF 332
Cdd:cd01492 155 --------------------------------------------------LAPVAAVVGGILAQDVINALSKRESPLNNF 184

                       330
                ....*....|...
gi 6325438  333 IVFDGITLDMPLF 345
Cdd:cd01492 185 FVFDGETSEAPIY 197
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 16-339 9.54e-49

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: 169.02  E-value: 9.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   16 YDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKER 95
Cdd:cd01493   3 YDRQLRLWGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEATCEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   96 IQDLNPRIELNFDKQ---DLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYV---------- 162
Cdd:cd01493  83 LQELNPDVNGSAVEEspeALLDNDPSFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIriqlkehtiv 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  163 ----------------FIDLIEFISEDEK--------------------LQSVRPTTVGPISSN-------RSIIEVTTR 199
Cdd:cd01493 163 eshpdnaledlrldnpFPELREHADSIDLddmdpaehshtpyivilikyLEKWRSAHNGQLPSTykekkefRDLVRSLMR 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  200 KDeEDEKKTYERIktKNCYRPLNEVLSTATLKE--KMTQ-RQLKRVTSI------------------LPLTLSL------ 252
Cdd:cd01493 243 SN-EDEENFEEAI--KAVNKALNRTKIPSSVEEifNDDRcENLTSQSSSfwimaralkefvaeenglLPLPGTLpdmtad 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  253 ------LQyglnqkgkAISFEQMKRDAAVW-------CENLGVPATVVKDDYIQQFIKQ---------KGIEFaPVAAII 310
Cdd:cd01493 320 tekyikLQ--------NIYREKAEKDAAEVekyvreiLKSLGRSPDSISDKEIKLFCKNaaflrvirgRSLEH-NISAFM 390

                       410       420
                ....*....|....*....|....*....
gi 6325438  311 GGAVAQDVINILGKRLSPLNNFIVFDGIT 339
Cdd:cd01493 391 GGIAAQEVIKLITKQYVPIDNTFIFDGIR 419
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 15-166 2.48e-48

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: 161.44  E-value: 2.48e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   15 LYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDV--GQWKIDAT 92
Cdd:cd01485   1 LYDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSnsGMNRAAAS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325438   93 KERIQDLNPRIELNF---DKQDLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDL 166
Cdd:cd01485  81 YEFLQELNPNVKLSIveeDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFDF 157
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 15-336 9.51e-38

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: 136.63  E-value: 9.51e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   15 LYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKE 94
Cdd:cd01491   1 LYSRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   95 RIQDLNPRIELNFDKQDLqekDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDL-IEFISED 173
Cdd:cd01491  81 RLAELNPYVPVTVSTGPL---TTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFCDFgDEFTVYD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  174 eklqsvrPTTVGPISSNRSIIE-----VTTRKDE-----EDekktyeriktkNCYRPLNEVlstatlkEKMTQ---RQLK 240
Cdd:cd01491 158 -------PNGEEPKSGMISSISkdnpgVVTCLDEtrhgfED-----------GDYVTFSEV-------EGMTElngCEPR 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438  241 RVTSILPLTLSLlqyglnqkGKAISFEQMKRDAAVwcenlgvpaTVVKddyiqqfikqkgieFAPVAAIIGGAVAQDVIN 320
Cdd:cd01491 213 KIKVKGPYTFSI--------GDTSSFSEYIRGGIV---------TQVK--------------LSPMAAFFGGLAAQEVLK 261

                       330
                ....*....|....*.
gi 6325438  321 ILGKRLSPLNNFIVFD 336
Cdd:cd01491 262 ACSGKFTPLKQWLYFD 277
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 16-163 4.70e-28

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: 109.27  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     16 YDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATK 93
Cdd:pfam00899   1 YSRQLALplIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325438     94 ERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV------ATEMQIDEAIKintltrKLNIPLYVAGSNGLFAYVF 163
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENaEELIKSFDIVVdatdnfAARYLVNDACV------KLGKPLIEAGVLGFKGQVT 151
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 11-338 3.26e-26

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: 109.98  E-value: 3.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438      11 DEiALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKID 90
Cdd:TIGR01408    3 DE-ALYSRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438      91 ATKERIQDLNPRIELNFDKQDLqekDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPL-YV-AGSNGLFAYVFIDL-I 167
Cdd:TIGR01408   82 AVVKKLAELNPYVHVSSSSVPF---NEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPIaFIsADVRGLFGSLFCDFgD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     168 EFISEDEKLQSVRPTTVGPISSNRSIIeVTTRKDEEDEKKTYERIKtkncyrpLNEVLSTATLKEKMTQrqlkRVTSILP 247
Cdd:TIGR01408  159 EFEVLDTDGEEPKTGFIASITQANPGI-VTCLENHRHKLETGDFVT-------FREVNGMTGLNDGSPR----KITVISP 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     248 LTLSL---LQYGLNQKG---------KAISFEQMKR-------------------------------------------- 271
Cdd:TIGR01408  227 YSFSIgdtTELGPYLHGgiatqvktpKTVFFKSLREqlkdpkclivdfskperppeihtafqaldqfqekysrkpnvgcq 306

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325438     272 -DAAVWCENLGVPATV-------VKDDYIQQFIKQKGIEFAPVAAIIGGAVAQDVINILGKRLSPLNNFIVFDGI 338
Cdd:TIGR01408  307 qDAEELLKLATSISETleekvpdVDAKLVHWLSWTAQGFLSPMAAAVGGVVSQEVLKAVTGKFSPLCQWFYFDSA 381
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 35-167 1.55e-24

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: 97.34  E-value: 1.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELNFDKQDLQE 114
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6325438  115 -KDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDLI 167
Cdd:cd01483  81 dNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 9-163 8.33e-24

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 97.89  E-value: 8.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    9 SEDEIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQ 86
Cdd:COG0476   1 TDEELERYSRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   87 WKIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV------ATEMQIDEAikintlTRKLNIPLYVAGSNGLF 159
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENaLELLAGADLVLdctdnfATRYLLNDA------CVKLGIPLVSGAVIGFE 154


                ....
gi 6325438  160 AYVF 163
Cdd:COG0476 155 GQVT 158
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 16-162 3.88e-19

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: 84.84  E-value: 3.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   16 YDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATK 93
Cdd:cd00757   2 YSRQILLpeIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   94 ERIQDLNPRIEL-----NFDKQDLqekdEEFFQQFDLVV------ATEMQIDEAIkintltRKLNIPLYVAGSNGLFAYV 162
Cdd:cd00757  82 ERLRAINPDVEIeayneRLDAENA----EELIAGYDLVLdctdnfATRYLINDAC------VKLGKPLVSGAVLGFEGQV 151
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 6-127 8.74e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 75.65  E-value: 8.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     6 EKLSEDEIALYDRQIRLWGM--TAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSED 83
Cdd:PRK05690   3 AELSDEEMLRYNRQIILRGFdfDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDAT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 6325438    84 VGQWKIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV 127
Cdd:PRK05690  83 IGQPKVESARAALARINPHIAIETINARLDDDElAALIAGHDLVL 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 8-127 9.13e-15

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 74.53  E-value: 9.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     8 LSEDEIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVG 85
Cdd:PRK05600  14 LPTSELRRTARQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6325438    86 QWKIDATKERIQDLNPRIELNFDKQDLQ-EKDEEFFQQFDLVV 127
Cdd:PRK05600  94 RPKVEVAAERLKEIQPDIRVNALRERLTaENAVELLNGVDLVL 136
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 35-157 9.87e-14

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: 69.91  E-value: 9.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNP--RIELNFDK-QD 111
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPncKVVPYQNKvGP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6325438  112 LQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNG 157
Cdd:cd01484  81 EQDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEG 126
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 6-155 1.45e-13

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 70.89  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     6 EKLSEDEIALYDRQ--IRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSED 83
Cdd:PRK07878  13 AELTRDEVARYSRHliIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSD 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325438    84 VGQWKIDATKERIQDLNPRIELNFDKQDLQ-EKDEEFFQQFDLVV------ATEMQIDEAIKIntltrkLNIPlYVAGS 155
Cdd:PRK07878  93 VGRSKAQSARDSIVEINPLVNVRLHEFRLDpSNAVELFSQYDLILdgtdnfATRYLVNDAAVL------AGKP-YVWGS 164
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 27-157 7.84e-13

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


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 67.24  E-value: 7.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   27 AQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELN 106
Cdd:cd00755   5 GLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6325438  107 --FDKQDLQEKDEEFFQQFDLVV-AtemqIDE-AIKINTLT--RKLNIPLYVAGSNG 157
Cdd:cd00755  85 avEEFLTPDNSEDLLGGDPDFVVdA----IDSiRAKVALIAycRKRKIPVISSMGAG 137
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 35-162 8.47e-13

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: 68.17  E-value: 8.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELNFDKQDLQE 114
Cdd:cd01489   1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6325438  115 KD--EEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYV 162
Cdd:cd01489  81 PDfnVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQV 130
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 35-128 3.06e-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: 66.23  E-value: 3.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELNFDKQDLQE 114
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90
                ....*....|....
gi 6325438  115 KDEEFFQQFDLVVA 128
Cdd:cd01488  81 KDEEFYRQFNIIIC 94
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-127 5.48e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 66.19  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     8 LSEDEIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVG 85
Cdd:PRK08762 108 LTDEQDERYSRHLRLpeVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6325438    86 QWKIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVV 127
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNvEALLQDVDVVV 230
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 16-155 5.65e-12

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 65.91  E-value: 5.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    16 YDRQIRLW--GMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQW--KIDA 91
Cdd:PRK12475   5 YSRQILFSgiGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKkpKAIA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325438    92 TKERIQDLNPRIELNFDKQDLQ-EKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPlYVAGS 155
Cdd:PRK12475  85 AKEHLRKINSEVEIVPVVTDVTvEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIP-WIYGG 148
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 1-154 9.61e-12

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 63.95  E-value: 9.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    1 MDMKveklsedeiALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIG 80
Cdd:COG1179   1 MDME---------RRFSRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   81 SEDVGQWKIDATKERIQDLNPRIELNFdKQDLQEKD--EEFF-QQFDLVvatemqIDeAI-----KINTLT--RKLNIPL 150
Cdd:COG1179  72 DSTVGRPKVEVMAERIRDINPDCEVTA-IDEFVTPEnaDELLsEDYDYV------ID-AIdsvsaKAALIAwcRRRGIPI 143


                ....
gi 6325438  151 YVAG 154
Cdd:COG1179 144 ISSM 147
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
7-127 1.51e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 64.76  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     7 KLSEDEIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDV 84
Cdd:PRK07411  10 QLSKDEYERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6325438    85 GQWKIDATKERIQDLNPRIELN-FDKQDLQEKDEEFFQQFDLVV 127
Cdd:PRK07411  90 GKPKIESAKNRILEINPYCQVDlYETRLSSENALDILAPYDVVV 133
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 35-158 4.14e-11

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: 60.86  E-value: 4.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSeDVGQWKIDATKERIQDLNPRIELNFDKQDLQE 114
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6325438  115 KD-EEFFQQFDLVV-ATEMQIDEAIKINTLTRKLNIPlyVAGSNGL 158
Cdd:cd01487  80 NNlEGLFGDCDIVVeAFDNAETKAMLAESLLGNKNKP--VVCASGM 123
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
32-155 6.95e-11

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 61.03  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    32 RSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQ-FFIgsEDVGQWKIDATKERIQDLNPRIELNFDKQ 110
Cdd:PRK08644  27 KKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQqYFI--SQIGMPKVEALKENLLEINPFVEIEAHNE 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6325438   111 DLQEKD-EEFFQQFDLVV-ATEMQIDEAIKINTLTRKLNIPLyVAGS 155
Cdd:PRK08644 105 KIDEDNiEELFKDCDIVVeAFDNAETKAMLVETVLEHPGKKL-VAAS 150
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 16-127 8.48e-11

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: 63.37  E-value: 8.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438      16 YDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGI-----GHLTILDGHMVTEEDLGSQFFIGSEDVGQWKID 90
Cdd:TIGR01408  402 YDAQIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSY 481

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6325438      91 ATKERIQDLNPRIELnfdkQDLQEK---------DEEFFQQFDLVV 127
Cdd:TIGR01408  482 TAADATLKINPQIKI----DAHQNRvgpetetifNDEFYEKLDVVI 523
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 12-101 1.61e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 61.43  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    12 EIALYDRQIRL--WGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKI 89
Cdd:PRK05597   5 DIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90
                 ....*....|..
gi 6325438    90 DATKERIQDLNP 101
Cdd:PRK05597  85 ESAREAMLALNP 96
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 16-164 2.03e-09

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 58.08  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    16 YDRQIRLW--GMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQW--KIDA 91
Cdd:PRK07688   5 YSRQELFSpiGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAVA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325438    92 TKERIQDLNPRIELNFDKQDLQ-EKDEEFFQQFDLVV-ATEmQIDEAIKINTLTRKLNIP-LYVA--GSNGLfAYVFI 164
Cdd:PRK07688  85 AKKRLEEINSDVRVEAIVQDVTaEELEELVTGVDLIIdATD-NFETRFIVNDAAQKYGIPwIYGAcvGSYGL-SYTII 160
PRK08328 PRK08328
hypothetical protein; Provisional
 8-162 1.69e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 54.42  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     8 LSEDEIALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQW 87
Cdd:PRK08328   2 LSERELERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325438    88 -KIDATKERIQDLNPRIELNFDKQDLQEKD-EEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYV 162
Cdd:PRK08328  82 pKPLSAKWKLERFNSDIKIETFVGRLSEENiDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
PTZ00245 PTZ00245
ubiquitin activating enzyme; Provisional
 8-105 3.22e-08

ubiquitin activating enzyme; Provisional


Pssm-ID: 140272  Cd Length: 287  Bit Score: 54.29  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438     8 LSEDEIALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQW 87
Cdd:PTZ00245   1 MRDAEAVRYDRQIRLWGKSTQQQLMHTSVALHGVAGAAAEAAKNLVLAGVRAVAVADEGLVTDADVCTNYLMQGEAGGTR 80

                         90
                 ....*....|....*...
gi 6325438    88 KIDATKErIQDLNPRIEL 105
Cdd:PTZ00245  81 GARALGA-LQRLNPHVSV 97
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 35-128 9.97e-07

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: 49.98  E-value: 9.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438   35 KVLLINLGAIGSEITKSIVLSGI-----GHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELNfdk 109
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVgtgesGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKIT--- 77

                        90       100
                ....*....|....*....|....*...
gi 6325438  110 qDLQEK---------DEEFFQQFDLVVA 128
Cdd:cd01490  78 -ALQNRvgpetehifNDEFWEKLDGVAN 104
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 21-101 5.25e-06

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 47.11  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    21 RLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLN 100
Cdd:PRK15116  18 RLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQIN 97


                 .
gi 6325438   101 P 101
Cdd:PRK15116  98 P 98
PRK14852 PRK14852
hypothetical protein; Provisional
 16-157 2.79e-04

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 42.76  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    16 YDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKER 95
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325438    96 IQDLNPRIEL-NFDKQDLQEKDEEFFQQFDLVV--ATEMQIDEAIKINTLTRKLNIPLYVAGSNG 157
Cdd:PRK14852 395 ALSVNPFLDIrSFPEGVAAETIDAFLKDVDLLVdgIDFFALDIRRRLFNRALELGIPVITAGPLG 459
PRK14851 PRK14851
hypothetical protein; Provisional
 13-120 5.17e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 38.69  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325438    13 IALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDAT 92
Cdd:PRK14851  23 EAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVM 102

                         90       100
                 ....*....|....*....|....*...
gi 6325438    93 KERIQDLNPRIELNFDKQDLQEKDEEFF 120
Cdd:PRK14851 103 KEQALSINPFLEITPFPAGINADNMDAF 130
 
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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