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Conserved domains on  [gi|568963086|ref|XP_006511854|]
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ubiquitin-like modifier-activating enzyme 5 isoform X1 [Mus musculus]

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 ...
 1-183 1.20e-47

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: 158.79  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNR-LFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITtVEHFEHFMNRisnggleegqpVDLVLSCVDNFEARMAI 79
Cdd:cd00757   61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELIAG-----------YDLVLDCTDNFATRYLI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  80 NTACNELGQTWMESGVSEnaVSGHIQLMIPGESACFACAPPLVVASNIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757  129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                        170       180
                 ....*....|....*....|....*.
gi 568963086 160 FLLKFGTV--SFYLGYNAMQDFFPTM 183
Cdd:cd00757  201 ILLGIGEPlaGRLLLFDALSMSFRTL 226
 
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 ...
 1-183 1.20e-47

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: 158.79  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNR-LFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITtVEHFEHFMNRisnggleegqpVDLVLSCVDNFEARMAI 79
Cdd:cd00757   61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELIAG-----------YDLVLDCTDNFATRYLI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  80 NTACNELGQTWMESGVSEnaVSGHIQLMIPGESACFACAPPLVVASNIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757  129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                        170       180
                 ....*....|....*....|....*.
gi 568963086 160 FLLKFGTV--SFYLGYNAMQDFFPTM 183
Cdd:cd00757  201 ILLGIGEPlaGRLLLFDALSMSFRTL 226
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-191 5.11e-33

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: 121.21  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086    1 MNRLF-FQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITTVEHFEHFmnrisnggleegQPVDLVLSCVDNFEARMAI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   80 NTACNELGQTWMESGVSenAVSGHIQLMIPGESACFACapplvVASNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568963086  160 FLLKFGTVSF---YLGYNAMQDFFPTMFMK-PNPQC 191
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 4.64e-22

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: 92.11  E-value: 4.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  11 AGLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfehfmnriSNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTW 90
Cdd:COG0476   78 VGRPKVEAAAERLRALNPDVEVEAIPERLT------------EENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  91 MESGVSEnaVSGHIQLMIPGESACFAC----APPlvvasniDEKTLKREGVcaasLPTTMGVVAGILVQNVLKFLLKFGT 166
Cdd:COG0476  146 VSGAVIG--FEGQVTVFIPGDTPCYRClfpePPE-------PGPSCAEAGV----LGPLVGVIGSLQATEAIKLLTGIGE 212

                        170       180
                 ....*....|....*....|....*..
gi 568963086 167 VSF--YLGYNAMQDFFPTMFMKPNPQC 191
Cdd:COG0476  213 PLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-191 3.92e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 62.72  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  12 GLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfehfmnriSNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTWM 91
Cdd:PRK08762 187 GQPKVDSAAQRLAALNPDVQVEAVQERVT------------SDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLV 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  92 ESGVSEnaVSGHIQLMIPGESA----CFAC----APPLVVASNIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLK 163
Cdd:PRK08762 255 YGAVFR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLG 323

                        170       180       190
                 ....*....|....*....|....*....|
gi 568963086 164 FGT--VSFYLGYNAMQDFFPTMFMKPNPQC 191
Cdd:PRK08762 324 IGDplTGRLLTFDALAMRFRELRLPPDPHC 353
 
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 ...
 1-183 1.20e-47

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: 158.79  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNR-LFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITtVEHFEHFMNRisnggleegqpVDLVLSCVDNFEARMAI 79
Cdd:cd00757   61 LQRqILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLD-AENAEELIAG-----------YDLVLDCTDNFATRYLI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  80 NTACNELGQTWMESGVSEnaVSGHIQLMIPGESACFACAPPLVVASNIdektlkREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:cd00757  129 NDACVKLGKPLVSGAVLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALK 200

                        170       180
                 ....*....|....*....|....*.
gi 568963086 160 FLLKFGTV--SFYLGYNAMQDFFPTM 183
Cdd:cd00757  201 ILLGIGEPlaGRLLLFDALSMSFRTL 226
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-191 5.11e-33

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: 121.21  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086    1 MNRLF-FQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITTVEHFEHFmnrisnggleegQPVDLVLSCVDNFEARMAI 79
Cdd:pfam00899  60 LNRQFlFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   80 NTACNELGQTWMESGVSenAVSGHIQLMIPGESACFACapplvVASNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLK 159
Cdd:pfam00899 128 NDACVKLGKPLIEAGVL--GFKGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALK 200

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568963086  160 FLLKFGTVSF---YLGYNAMQDFFPTMFMK-PNPQC 191
Cdd:pfam00899 201 LLLGKGEPNLagrLLQFDALTMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 11-191 4.64e-22

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: 92.11  E-value: 4.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  11 AGLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfehfmnriSNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTW 90
Cdd:COG0476   78 VGRPKVEAAAERLRALNPDVEVEAIPERLT------------EENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  91 MESGVSEnaVSGHIQLMIPGESACFAC----APPlvvasniDEKTLKREGVcaasLPTTMGVVAGILVQNVLKFLLKFGT 166
Cdd:COG0476  146 VSGAVIG--FEGQVTVFIPGDTPCYRClfpePPE-------PGPSCAEAGV----LGPLVGVIGSLQATEAIKLLTGIGE 212

                        170       180
                 ....*....|....*....|....*..
gi 568963086 167 VSF--YLGYNAMQDFFPTMFMKPNPQC 191
Cdd:COG0476  213 PLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-191 3.92e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 62.72  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  12 GLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfehfmnriSNGGLEEGQPVDLVLSCVDNFEARMAINTACNELGQTWM 91
Cdd:PRK08762 187 GQPKVDSAAQRLAALNPDVQVEAVQERVT------------SDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLV 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  92 ESGVSEnaVSGHIQLMIPGESA----CFAC----APPLVVASNIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLK 163
Cdd:PRK08762 255 YGAVFR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLG 323

                        170       180       190
                 ....*....|....*....|....*....|
gi 568963086 164 FGT--VSFYLGYNAMQDFFPTMFMKPNPQC 191
Cdd:PRK08762 324 IGDplTGRLLTFDALAMRFRELRLPPDPHC 353
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 1-119 1.25e-10

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: 60.86  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNRLF-FQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITT----VEHFEHFmnrisnggleegqpvDLVLSCVDNFEA 75
Cdd:cd01489   39 LNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEFFKQF---------------DLVFNALDNLAA 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568963086  76 RMAINTACNELGQTWMESGVSenAVSGHIQLMIPGESACFACAP 119
Cdd:cd01489  104 RRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 10-117 1.49e-08

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 55.00  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  10 QAGLSKVHAAEHTLRNINPDVLFEVHNYNITtVEHFEHFMNRisnggleegqpVDLVLSCVDNFEARMAINTACNELGQT 89
Cdd:PRK07688  76 KNNLPKAVAAKKRLEEINSDVRVEAIVQDVT-AEELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIP 143

                         90       100       110
                 ....*....|....*....|....*....|
gi 568963086  90 WMESGvsenAVS--GHIQLMIPGESACFAC 117
Cdd:PRK07688 144 WIYGA----CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 1-116 7.88e-08

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: 50.34  E-value: 7.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNRLFFQPyQA--GLSKVHAAEHTLRNINPDVlfevhnyNITTVEHFEHFMNRisnggLEEGQPVDLVLSCVDNFEARMA 78
Cdd:cd01483   39 LNRQFLAR-QAdiGKPKAEVAARRLNELNPGV-------NVTAVPEGISEDNL-----DDFLDGVDLVIDAIDNIAVRRA 105

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568963086  79 INTACNELGQTWMESGVSEnavsGHIQLMIPGESACFA 116
Cdd:cd01483  106 LNRACKELGIPVIDAGGLG----LGGDIQVIDIGSLSA 139
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 1-120 1.76e-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: 51.04  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   1 MNRLF-FQPYQAGLSKVHAAEHTLRNINPdvlfevhnyNITTVEHFEHFMNrISNGGLEEGQPVDLVLSCVDNFEARMAI 79
Cdd:cd01484   39 LNRQFlFRPKDIGRPKSEVAAEAVNDRNP---------NCKVVPYQNKVGP-EQDFNDTFFEQFHIIVNALDNIIARRYV 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568963086  80 NTACNELGQTWMESGVSenAVSGHIQLMIPGESACFACA--PP 120
Cdd:cd01484  109 NGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 12-191 1.37e-06

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 48.30  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  12 GLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfEHFMNRISNGgleegqpVDLVLSCVDNFEARMAINTACNELGQTWm 91
Cdd:PRK05690  84 GQPKVESARAALARINPHIAIETINARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  92 esgVSENAV--SGHIQLMIPGESA-CFACAPPLVVASNIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLKFGT-- 166
Cdd:PRK05690 151 ---VSGAAIrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEpl 220

                        170       180
                 ....*....|....*....|....*
gi 568963086 167 VSFYLGYNAMQDFFPTMFMKPNPQC 191
Cdd:PRK05690 221 SGRLLLYDAMTMQFREMKLKRDPGC 245
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 13-117 2.45e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 48.19  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  13 LSKVHAAEHTLRNINPDVlfEVHNYNI-TTVEHFEHFMnrisnggleegQPVDLVLSCVDNFEARMAINTACNELGQTWM 91
Cdd:PRK12475  79 KPKAIAAKEHLRKINSEV--EIVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWI 145

                         90       100
                 ....*....|....*....|....*..
gi 568963086  92 ESG-VSENAVSGHIqlmIPGESACFAC 117
Cdd:PRK12475 146 YGGcVGSYGVTYTI---IPGKTPCLRC 169
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
2-87 8.09e-06

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 45.62  E-value: 8.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   2 NRLFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNynittvehfehfmNRISNGGLEE-GQPVDLVLSCVDNFEA-RMAI 79
Cdd:PRK08644  69 NRQQYFISQIGMPKVEALKENLLEINPFVEIEAHN-------------EKIDEDNIEElFKDCDIVVEAFDNAETkAMLV 135


                 ....*...
gi 568963086  80 NTACNELG 87
Cdd:PRK08644 136 ETVLEHPG 143
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-191 1.23e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.08  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  12 GLSKVHAAEHTLRNINPDVLFEVHNYNITT---VEHFEHFmnrisnggleegqpvDLVLSCVDNFEARMAINTACNELGQ 88
Cdd:PRK07878  94 GRSKAQSARDSIVEINPLVNVRLHEFRLDPsnaVELFSQY---------------DLILDGTDNFATRYLVNDAAVLAGK 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  89 --TW-----MESGVS---ENAVSGHiqlmipgeSACFAC-----APPLVVASNIDEKTLkreGVCAASlpttmgvVAGIL 153
Cdd:PRK07878 159 pyVWgsiyrFEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIM 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568963086 154 VQNVLKFLLKFGT--VSFYLGYNAMQDFFPTMFMKPNPQC 191
Cdd:PRK07878 221 GTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 3-189 1.83e-03

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 39.48  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086   3 RLFFQPYQAGLSKVHAAEHTLRNINPDVLFEVHNYNITtvehfehfmnriSNGGLEEGQPVDLVLSCVDNFEARMAINTA 82
Cdd:PRK05600  84 QILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVELLNGVDLVLDGSDSFATKFLVADA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963086  83 CNELGQTWMESGVsenavsghiqLMIPGESACFACAPPlvvASNIDEKTLKREGVCAASLP---------TTMGVVAGIL 153
Cdd:PRK05600 152 AEITGTPLVWGTV----------LRFHGELAVFNSGPD---HRGVGLRDLFPEQPSGDSIPdcatagvlgATTAVIGALM 218

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568963086 154 VQNVLKFLLKFGTVSF--YLGYNAMQDFFPTMFMKPNP 189
Cdd:PRK05600 219 ATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
 
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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