NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1007393879|ref|NP_001308168|]
View 

ubiquitin-like modifier-activating enzyme 5 isoform 4 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.16e-51

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: 169.20  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  80 NTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1007393879 160 FLLNFGTV--SFYLGYNAMQDFFPTMSM 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 1.16e-51

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: 169.20  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  80 NTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1007393879 160 FLLNFGTV--SFYLGYNAMQDFFPTMSM 185
Cdd:cd00757   201 ILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-191 2.96e-37

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: 132.38  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  80 NTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1007393879 160 FLLNFGTVSF---YLGYNAMQDFFPTMSMK-PNPQC 191
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 2.67e-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: 98.28  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  11 AGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTW 90
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  91 MESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF- 169
Cdd:COG0476   146 VSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAg 216

                         170       180
                  ....*....|....*....|...
gi 1007393879 170 -YLGYNAMQDFFPTMSMKPNPQC 191
Cdd:COG0476   217 rLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-191 9.05e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.65  E-value: 9.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  12 GLSKVQAAEHTLRNINPDVlfevhnynitTVENFQhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTW 90
Cdd:PRK08762  187 GQPKVDSAAQRLAALNPDV----------QVEAVQ---ERVTSDNVEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  91 MESGVSEnaVSGHIQLIIPGESA----CFAC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLL 162
Cdd:PRK08762  254 VYGAVFR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLL 322

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1007393879 163 NFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 191
Cdd:PRK08762  323 GIGDplTGRLLTFDALAMRFRELRLPPDPHC 353
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 1-109 1.17e-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: 40.26  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879    1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPVDLVLSCVDNFEARMT 78
Cdd:TIGR01408  464 LNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKLDVVINALDNVEARRY 534

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1007393879   79 INTACNELGQTWMESGVSenAVSGHIQLIIP 109
Cdd:TIGR01408  535 VDSRCLAFLKPLLESGTL--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 1.16e-51

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: 169.20  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTI 79
Cdd:cd00757    61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELI-----------AGYDLVLDCTDNFATRYLI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  80 NTACNELGQTWMESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757   129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                         170       180
                  ....*....|....*....|....*...
gi 1007393879 160 FLLNFGTV--SFYLGYNAMQDFFPTMSM 185
Cdd:cd00757   201 ILLGIGEPlaGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-191 2.96e-37

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: 132.38  E-value: 2.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  80 NTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1007393879 160 FLLNFGTVSF---YLGYNAMQDFFPTMSMK-PNPQC 191
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 2.67e-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: 98.28  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  11 AGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTW 90
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  91 MESGVSEnaVSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF- 169
Cdd:COG0476   146 VSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAg 216

                         170       180
                  ....*....|....*....|...
gi 1007393879 170 -YLGYNAMQDFFPTMSMKPNPQC 191
Cdd:COG0476   217 rLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-191 9.05e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.65  E-value: 9.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  12 GLSKVQAAEHTLRNINPDVlfevhnynitTVENFQhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTW 90
Cdd:PRK08762  187 GQPKVDSAAQRLAALNPDV----------QVEAVQ---ERVTSDNVEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  91 MESGVSEnaVSGHIQLIIPGESA----CFAC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLL 162
Cdd:PRK08762  254 VYGAVFR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLL 322

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1007393879 163 NFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 191
Cdd:PRK08762  323 GIGDplTGRLLTFDALAMRFRELRLPPDPHC 353
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 1-119 2.59e-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: 63.17  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT----VENFQHFmdrisnggleegkpvDLVLSCVDNFEA 75
Cdd:cd01489    39 LNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEFFKQF---------------DLVFNALDNLAA 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1007393879  76 RMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 119
Cdd:cd01489   104 RRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 10-117 3.24e-10

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 60.01  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  10 QAGLSKVQAAEHTLRNINPDVLFEVHNYNITtVENFQHFMDRisnggleegkpVDLVLSCVDNFEARMTINTACNELGQT 89
Cdd:PRK07688   76 KNNLPKAVAAKKRLEEINSDVRVEAIVQDVT-AEELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIP 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 1007393879  90 WMESGvsenAVS--GHIQLIIPGESACFAC 117
Cdd:PRK07688  144 WIYGA----CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-114 3.16e-09

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: 54.58  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNR-LFFQPHQAGLSKVQAAEHTLRNINPDVlfevhnyNITTVEnfqhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMT 78
Cdd:cd01483    39 LNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAVP------EGISEDNLDDfLDGVDLVIDAIDNIAVRRA 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1007393879  79 INTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 114
Cdd:cd01483   106 LNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 1-120 1.40e-07

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: 51.43  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPdvlfevhNYNITTvenFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTI 79
Cdd:cd01484    39 LNRQFlFRPKDIGRPKSEVAAEAVNDRNP-------NCKVVP---YQNKVGPEQDFNDTFFEQFHIIVNALDNIIARRYV 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1007393879  80 NTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 120
Cdd:cd01484   109 NGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-191 3.78e-07

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 50.23  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  12 GLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfQHFMDRISNGgleegkpVDLVLSCVDNFEARMTINTACNELGQTWm 91
Cdd:PRK05690   84 GQPKVESARAALARINPHIAIETINARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  92 esgVSENAV--SGHIQLIIPGESA-CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLNFGT-- 166
Cdd:PRK05690  151 ---VSGAAIrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEpl 220

                         170       180
                  ....*....|....*....|....*
gi 1007393879 167 VSFYLGYNAMQDFFPTMSMKPNPQC 191
Cdd:PRK05690  221 SGRLLLYDAMTMQFREMKLKRDPGC 245
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 13-117 5.59e-07

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 50.11  E-value: 5.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  13 LSKVQAAEHTLRNINPDVlfEVHNYNI-TTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWM 91
Cdd:PRK12475   79 KPKAIAAKEHLRKINSEV--EIVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWI 145

                          90       100
                  ....*....|....*....|....*..
gi 1007393879  92 ESG-VSENAVSghiQLIIPGESACFAC 117
Cdd:PRK12475  146 YGGcVGSYGVT---YTIIPGKTPCLRC 169
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
2-87 6.00e-07

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 49.08  E-value: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   2 NRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEA-RMTIN 80
Cdd:PRK08644   69 NRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF-----------KDCDIVVEAFDNAETkAMLVE 136


                  ....*..
gi 1007393879  81 TACNELG 87
Cdd:PRK08644  137 TVLEHPG 143
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-191 6.51e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.85  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  12 GLSKVQAAEHTLRNINPDVLFEVHNYNITT---VENFQHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQ 88
Cdd:PRK07878   94 GRSKAQSARDSIVEINPLVNVRLHEFRLDPsnaVELFSQY---------------DLILDGTDNFATRYLVNDAAVLAGK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  89 --TW-----MESGVS---ENAVSGHiqliipgeSACFAC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGIL 153
Cdd:PRK07878  159 pyVWgsiyrFEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIM 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1007393879 154 VQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 191
Cdd:PRK07878  221 GTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 1-109 1.17e-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: 40.26  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879    1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPVDLVLSCVDNFEARMT 78
Cdd:TIGR01408  464 LNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKLDVVINALDNVEARRY 534

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1007393879   79 INTACNELGQTWMESGVSenAVSGHIQLIIP 109
Cdd:TIGR01408  535 VDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 1-82 2.00e-03

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: 38.13  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDrisnggleegkpVDLVLSCVDNFEA-RMTI 79
Cdd:cd01487    39 LNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGD------------CDIVVEAFDNAETkAMLA 106


                  ...
gi 1007393879  80 NTA 82
Cdd:cd01487   107 ESL 109
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 1-122 4.47e-03

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: 38.11  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879   1 MNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT--VENFQHFmdrisnggleegkpvDLVLSCVDNFEARM 77
Cdd:cd01488    39 LNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDkdEEFYRQF---------------NIIICGLDSIEARR 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1007393879  78 TIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 122
Cdd:cd01488   104 WINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK08328 PRK08328
hypothetical protein; Provisional
 48-165 6.05e-03

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 37.47  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007393879  48 FMDRISNGGLEEG-KPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAPPlvvaaN 126
Cdd:PRK08328  103 FVGRLSEENIDEVlKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTKRLREIFP-----K 175

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1007393879 127 IDEKTLKREGVCAaslptTMGVVAGILVQNVLKFLLNFG 165
Cdd:PRK08328  176 VKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH