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Conserved domains on  [gi|1390081923|ref|XP_025002851|]
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ubiquitin-like modifier-activating enzyme 5 isoform X1 [Gallus gallus]

Protein Classification

ubiquitin-activating E1 family protein( domain architecture ID 320623)

ubiquitin-activating E1 family protein is an activating enzyme similar to Osphranter rufus ubiquitin-activating enzyme E1 Y that activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E1_enzyme_family super family cl22428
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-185 8.36e-53

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.


The actual alignment was detected with superfamily member cd00757:

Pssm-ID: 451392 [Multi-domain]  Cd Length: 228  Bit Score: 171.89  E-value: 8.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  80 NTACNELGQIWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1390081923 160 YLLNFGTV--SYYLGYNAMQDFFPTMAM 185
Cdd:cd00757   201 ILLGIGEPlaGRLLLFDALSMSFRTLKL 228
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 1-185 8.36e-53

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: 171.89  E-value: 8.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  80 NTACNELGQIWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1390081923 160 YLLNFGTV--SYYLGYNAMQDFFPTMAM 185
Cdd:cd00757   201 ILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-192 1.25e-38

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: 135.85  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNFEHFmdrisngaleegKPVDLVLSCVDNFEARMAI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  80 NTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1390081923 160 YLLNFGTVSY---YLGYNAMQDFFPTMAMK-PNPQCS 192
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNCP 237
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 7.79e-28

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: 107.52  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  11 AGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNfehfmdrisngALEEGKPVDLVLSCVDNFEARMAINTACNELGQIW 90
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTE-EN-----------ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  91 MESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKYLLNFGT--VS 168
Cdd:COG0476   146 VSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEplAG 216

                         170       180
                  ....*....|....*....|...
gi 1390081923 169 YYLGYNAMQDFFPTMAMKPNPQC 191
Cdd:COG0476   217 RLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-192 2.96e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 69.27  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEhfmdrisngALEEGkpVDLVLSCVDNFEARMAINTACNELGqIWM 91
Cdd:PRK08762  187 GQPKVDSAAQRLAALNPDVQVEAVQERVTS-DNVE---------ALLQD--VDVVVDGADNFPTRYLLNDACVKLG-KPL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  92 ESGvsenAV---SGHIQLIIPGESA----CFAC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKY 160
Cdd:PRK08762  254 VYG----AVfrfEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKL 320

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1390081923 161 LLNFGT--VSYYLGYNAMQDFFPTMAMKPNPQCS 192
Cdd:PRK08762  321 LLGIGDplTGRLLTFDALAMRFRELRLPPDPHCP 354
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 1-109 2.63e-03

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: 39.49  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923    1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNI--TTldnfehfmDRISNGALEEGkpVDLVLSCVDNFEARM 77
Cdd:TIGR01408  464 LNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpET--------ETIFNDEFYEK--LDVVINALDNVEARR 533

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1390081923   78 AINTACNELGQIWMESGVSenAVSGHIQLIIP 109
Cdd:TIGR01408  534 YVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 1-185 8.36e-53

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: 171.89  E-value: 8.36e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  80 NTACNELGQIWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1390081923 160 YLLNFGTV--SYYLGYNAMQDFFPTMAM 185
Cdd:cd00757   201 ILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-192 1.25e-38

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: 135.85  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNFEHFmdrisngaleegKPVDLVLSCVDNFEARMAI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  80 NTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1390081923 160 YLLNFGTVSY---YLGYNAMQDFFPTMAMK-PNPQCS 192
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNCP 237
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 7.79e-28

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: 107.52  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  11 AGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNfehfmdrisngALEEGKPVDLVLSCVDNFEARMAINTACNELGQIW 90
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTE-EN-----------ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  91 MESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKYLLNFGT--VS 168
Cdd:COG0476   146 VSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEplAG 216

                         170       180
                  ....*....|....*....|...
gi 1390081923 169 YYLGYNAMQDFFPTMAMKPNPQC 191
Cdd:COG0476   217 RLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-192 2.96e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 69.27  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEhfmdrisngALEEGkpVDLVLSCVDNFEARMAINTACNELGqIWM 91
Cdd:PRK08762  187 GQPKVDSAAQRLAALNPDVQVEAVQERVTS-DNVE---------ALLQD--VDVVVDGADNFPTRYLLNDACVKLG-KPL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  92 ESGvsenAV---SGHIQLIIPGESA----CFAC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKY 160
Cdd:PRK08762  254 VYG----AVfrfEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKL 320

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1390081923 161 LLNFGT--VSYYLGYNAMQDFFPTMAMKPNPQCS 192
Cdd:PRK08762  321 LLGIGDplTGRLLTFDALAMRFRELRLPPDPHCP 354
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 1-119 1.53e-11

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: 63.55  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLD-NFEHFmdrisngaleegKPVDLVLSCVDNFEARMA 78
Cdd:cd01489    39 LNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDPDfNVEFF------------KQFDLVFNALDNLAARRH 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1390081923  79 INTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACAP 119
Cdd:cd01489   107 VNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 10-117 2.92e-10

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 60.01  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  10 QAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMDRisngaleegkpVDLVLSCVDNFEARMAINTACNELGQI 89
Cdd:PRK07688   76 KNNLPKAVAAKKRLEEINSDVRVEAIVQDVTA-EELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIP 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 1390081923  90 WMESGvsenAVS--GHIQLIIPGESACFAC 117
Cdd:PRK07688  144 WIYGA----CVGsyGLSYTIIPGKTPCLRC 169
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-191 3.14e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 59.09  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNyniTTLDnfEHFMDRISNGaleegkpVDLVLSCVDNFEARMAINTACNELGQ--- 88
Cdd:PRK05690   84 GQPKVESARAALARINPHIAIETIN---ARLD--DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKplv 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  89 ----IWMEsgvsenavsGHIQLIIPGESA-CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKYLLN 163
Cdd:PRK05690  152 sgaaIRME---------GQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTG 215

                         170       180       190
                  ....*....|....*....|....*....|
gi 1390081923 164 FGT--VSYYLGYNAMQDFFPTMAMKPNPQC 191
Cdd:PRK05690  216 YGEplSGRLLLYDAMTMQFREMKLKRDPGC 245
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-114 3.53e-10

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: 57.28  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVqfevhnyNITTldnfeHFMDRISNGALEEGKPVDLVLSCVDNFEARMAI 79
Cdd:cd01483    39 LNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTA-----VPEGISEDNLDDFLDGVDLVIDAIDNIAVRRAL 106

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1390081923  80 NTACNELGQIWMESGVSenAVSGHIQLIIPGESAC 114
Cdd:cd01483   107 NRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 1-120 8.19e-08

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: 51.81  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNF-EHFMDRIsngaleegkpvDLVLSCVDNFEARMA 78
Cdd:cd01484    39 LNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFnDTFFEQF-----------HIIVNALDNIIARRY 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1390081923  79 INTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACA--PP 120
Cdd:cd01484   108 VNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
2-95 2.57e-07

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 50.24  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   2 NRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEA-RMAIN 80
Cdd:PRK08644   69 NRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF-----------KDCDIVVEAFDNAETkAMLVE 136

                          90
                  ....*....|....*.
gi 1390081923  81 TACNELGQ-IWMESGV 95
Cdd:PRK08644  137 TVLEHPGKkLVAASGM 152
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 13-117 1.66e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 48.57  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  13 LSKVQAAEHTLRNINPDVQFEVHNYNITtLDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWME 92
Cdd:PRK12475   79 KPKAIAAKEHLRKINSEVEIVPVVTDVT-VEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIY 146

                          90       100
                  ....*....|....*....|....*.
gi 1390081923  93 SG-VSENAVSghiQLIIPGESACFAC 117
Cdd:PRK12475  147 GGcVGSYGVT---YTIIPGKTPCLRC 169
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-191 4.99e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 44.31  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNyniTTLDnfehfmdriSNGALEEGKPVDLVLSCVDNFEARMAINTACNELGQ--I 89
Cdd:PRK07878   94 GRSKAQSARDSIVEINPLVNVRLHE---FRLD---------PSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKpyV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  90 W-----MESGVS---ENAVSGHiqliipgeSACFAC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQN 156
Cdd:PRK07878  162 WgsiyrFEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTE 223

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1390081923 157 VLKYLLNFGT--VSYYLGYNAMQDFFPTMAMKPNPQC 191
Cdd:PRK07878  224 AIKLITGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 1-122 1.75e-04

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: 42.34  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDnfEHFMDRISngaleegkpvdLVLSCVDNFEARMAI 79
Cdd:cd01488    39 LNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKD--EEFYRQFN-----------IIICGLDSIEARRWI 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1390081923  80 N-TACNELGQ------IWMESGVSEnAVSGHIQLIIPGESACFAC----APPLV 122
Cdd:cd01488   106 NgTLVSLLLYedpesiIPLIDGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
12-191 1.91e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 42.41  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNYNITtldnfehfmdriSNGALEEGKPVDLVLSCVDNFEARMAINTAC------NE 85
Cdd:PRK07411   90 GKPKIESAKNRILEINPYCQVDLYETRLS------------SENALDILAPYDVVVDGTDNFPTRYLVNDACvllnkpNV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  86 LGQIWMESGVSE--NAVSGhiqliiPGESACFACAPP--LVVAANidektlkrEGVCAASLPttmGVVAGILVQNVLKYL 161
Cdd:PRK07411  158 YGSIFRFEGQATvfNYEGG------PNYRDLYPEPPPpgMVPSCA--------EGGVLGILP---GIIGVIQATETIKII 220

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1390081923 162 LNFGTV--SYYLGYNAMQDFFPTMAMKPNPQC 191
Cdd:PRK07411  221 LGAGNTlsGRLLLYNALDMKFRELKLRPNPER 252
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 1-82 4.16e-04

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: 40.44  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNFEHFMDrisngaleegkpVDLVLSCVDNFEA-RMAI 79
Cdd:cd01487    39 LNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGD------------CDIVVEAFDNAETkAMLA 106


                  ...
gi 1390081923  80 NTA 82
Cdd:cd01487   107 ESL 109
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 1-109 1.43e-03

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: 39.97  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNI--TTLDNF-EHFMDRisngaleegkpVDLVLSCVDNFEAR 76
Cdd:cd01490    44 LNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpETEHIFnDEFWEK-----------LDGVANALDNVDAR 112

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1390081923  77 MAINTACNELGQIWMESGVSenAVSGHIQLIIP 109
Cdd:cd01490   113 MYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 1-109 2.63e-03

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: 39.49  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923    1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNI--TTldnfehfmDRISNGALEEGkpVDLVLSCVDNFEARM 77
Cdd:TIGR01408  464 LNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpET--------ETIFNDEFYEK--LDVVINALDNVEARR 533

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1390081923   78 AINTACNELGQIWMESGVSenAVSGHIQLIIP 109
Cdd:TIGR01408  534 YVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 3-76 3.65e-03

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 38.32  E-value: 3.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390081923   3 RLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITtldnfehfmdriSNGALEEGKPVDLVLSCVDNFEAR 76
Cdd:PRK05600   84 QILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVELLNGVDLVLDGSDSFATK 145
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 12-90 3.66e-03

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 38.31  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNYNITTldnfehfmdrisNGALEEGKPVDLVLSCVDNFEARMAINTACNELG--QI 89
Cdd:PRK05597   80 GQPKAESAREAMLALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLGipHV 147


                  .
gi 1390081923  90 W 90
Cdd:PRK05597  148 W 148
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 12-79 5.49e-03

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: 37.58  E-value: 5.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390081923  12 GLSKVQAAEHTLRNINPDVQFEVHNYNItTLDNFEHFMdrisngaleeGKPVDLVLSCVDNFEARMAI 79
Cdd:cd00755    63 GKPKVEVMAERIRDINPECEVDAVEEFL-TPDNSEDLL----------GGDPDFVVDAIDSIRAKVAL 119
 
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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