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Conserved domains on  [gi|496843505|ref|WP_009382828|]
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ThiF family adenylyltransferase [Staphylococcus massiliensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07688 super family cl32237
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-334 6.14e-147

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


The actual alignment was detected with superfamily member PRK07688:

Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 417.47  E-value: 6.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   1 MNQsRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGI 80
Cdd:PRK07688   1 MNE-RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  81 PKVVAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAF 160
Cdd:PRK07688  80 PKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 161 IPGETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGVPFQAK---LTFgDIWDMTHQVIGFSRMQET 237
Cdd:PRK07688 160 IPGKTPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDYEALRdglVSF-DVWKNEYSCMNVQKLKKD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 238 SCPTCGTEPSYPHL-KEAKHHYATLCGRDTVQYHNP---QLSVDTLVGYLEDKGIQYHTNGYLVRFKFESYRIVCFQDGR 313
Cdd:PRK07688 239 NCPSCGEKALYPYLnYENTTKTAVLCGRNTVQIRPPhkeEYDLEELAELLRDRGLDVNVNPYLLSFSLEEKRLVLFKDGR 318

                        330       340
                 ....*....|....*....|.
gi 496843505 314 MLIHGLTDPNNAQTLIHKLFG 334
Cdd:PRK07688 319 VLVHGTKDISEAKTIYHRYIG 339
 
Name Accession Description Interval E-value
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-334 6.14e-147

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 417.47  E-value: 6.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   1 MNQsRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGI 80
Cdd:PRK07688   1 MNE-RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  81 PKVVAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAF 160
Cdd:PRK07688  80 PKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 161 IPGETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGVPFQAK---LTFgDIWDMTHQVIGFSRMQET 237
Cdd:PRK07688 160 IPGKTPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDYEALRdglVSF-DVWKNEYSCMNVQKLKKD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 238 SCPTCGTEPSYPHL-KEAKHHYATLCGRDTVQYHNP---QLSVDTLVGYLEDKGIQYHTNGYLVRFKFESYRIVCFQDGR 313
Cdd:PRK07688 239 NCPSCGEKALYPYLnYENTTKTAVLCGRNTVQIRPPhkeEYDLEELAELLRDRGLDVNVNPYLLSFSLEEKRLVLFKDGR 318

                        330       340
                 ....*....|....*....|.
gi 496843505 314 MLIHGLTDPNNAQTLIHKLFG 334
Cdd:PRK07688 319 VLVHGTKDISEAKTIYHRYIG 339
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 5-244 6.61e-100

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: 294.34  E-value: 6.61e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:COG0476    7 RYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV--GRPKVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:COG0476   85 AAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 165 TPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGFSRMQEtsCPTC 242
Cdd:COG0476  165 TPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIgePLAGRLLLFDALTMEFRTIKLPRDPD--CPVC 242


                 ..
gi 496843505 243 GT 244
Cdd:COG0476  243 GE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 5-231 1.72e-95

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: 282.44  E-value: 1.72e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV--GQPKAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:cd00757   79 AAAERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 165 TPCFNCMLPNIPAIS-LTCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGF 231
Cdd:cd00757  159 GPCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIgePLAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 5-207 1.07e-72

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 223.77  E-value: 1.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505    5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDV--GRPKVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPG- 163
Cdd:TIGR02356  79 VAAQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGg 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 496843505  164 ETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKIL 207
Cdd:TIGR02356 159 EGPCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 6-241 7.80e-69

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: 214.81  E-value: 7.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505    6 YSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEqaSNGIPKVVA 85
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREA--DIGKPKAEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   86 AKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGET 165
Cdd:pfam00899  79 AAERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  166 PCFNCMLPNIPAISL--TCDTVGVIAPAVTMTTSFQLRDALKILAG---VPFQAKLTFGDIWDMTHQVIGFSRMQeTSCP 240
Cdd:pfam00899 159 PCYRCLFPEDPPPKLvpSCTVAGVLGPTTAVVAGLQALEALKLLLGkgePNLAGRLLQFDALTMTFRELRLALKN-PNCP 237


                  .
gi 496843505  241 T 241
Cdd:pfam00899 238 V 238
 
Name Accession Description Interval E-value
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-334 6.14e-147

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 417.47  E-value: 6.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   1 MNQsRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGI 80
Cdd:PRK07688   1 MNE-RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  81 PKVVAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAF 160
Cdd:PRK07688  80 PKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 161 IPGETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGVPFQAK---LTFgDIWDMTHQVIGFSRMQET 237
Cdd:PRK07688 160 IPGKTPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDYEALRdglVSF-DVWKNEYSCMNVQKLKKD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 238 SCPTCGTEPSYPHL-KEAKHHYATLCGRDTVQYHNP---QLSVDTLVGYLEDKGIQYHTNGYLVRFKFESYRIVCFQDGR 313
Cdd:PRK07688 239 NCPSCGEKALYPYLnYENTTKTAVLCGRNTVQIRPPhkeEYDLEELAELLRDRGLDVNVNPYLLSFSLEEKRLVLFKDGR 318

                        330       340
                 ....*....|....*....|.
gi 496843505 314 MLIHGLTDPNNAQTLIHKLFG 334
Cdd:PRK07688 319 VLVHGTKDISEAKTIYHRYIG 339
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 3-334 1.35e-125

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 363.28  E-value: 1.35e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   3 QSRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGIPK 82
Cdd:PRK12475   2 QERYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKKPK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  83 VVAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIP 162
Cdd:PRK12475  82 AIAAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 163 GETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGvPFQA----KLTFgDIWDMTHQVIGFSRMQETS 238
Cdd:PRK12475 162 GKTPCLRCLMEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVE-DFEAlretFLSF-DIWNNQNMSIKVNKQKKDT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 239 CPTCGTEPSYPHLK-EAKHHYATLCGRDTVQYH---NPQLSVDTLVGYLEdKGIQYHTNGYLVRFKFESYRIVCFQDGRM 314
Cdd:PRK12475 240 CPSCGLTRTYPSLTfENQTKTEVLCGRNTVQIRpgvRRRLNLEEIKKRLQ-KIGKVDANPYLLSFQLDEYRFVLFTDGRA 318

                        330       340
                 ....*....|....*....|
gi 496843505 315 LIHGLTDPNNAQTLIHKLFG 334
Cdd:PRK12475 319 FIHGTNDIKKAKRLYARYIG 338
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 5-244 6.61e-100

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: 294.34  E-value: 6.61e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:COG0476    7 RYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADV--GRPKVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:COG0476   85 AAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVFIPGD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 165 TPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGFSRMQEtsCPTC 242
Cdd:COG0476  165 TPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIgePLAGRLLLFDALTMEFRTIKLPRDPD--CPVC 242


                 ..
gi 496843505 243 GT 244
Cdd:COG0476  243 GE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 5-231 1.72e-95

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: 282.44  E-value: 1.72e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADV--GQPKAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:cd00757   79 AAAERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 165 TPCFNCMLPNIPAIS-LTCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGF 231
Cdd:cd00757  159 GPCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIgePLAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 5-207 1.07e-72

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 223.77  E-value: 1.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505    5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDV--GRPKVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPG- 163
Cdd:TIGR02356  79 VAAQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGg 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 496843505  164 ETPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKIL 207
Cdd:TIGR02356 159 EGPCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 6-241 7.80e-69

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: 214.81  E-value: 7.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505    6 YSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEqaSNGIPKVVA 85
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREA--DIGKPKAEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   86 AKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGET 165
Cdd:pfam00899  79 AAERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  166 PCFNCMLPNIPAISL--TCDTVGVIAPAVTMTTSFQLRDALKILAG---VPFQAKLTFGDIWDMTHQVIGFSRMQeTSCP 240
Cdd:pfam00899 159 PCYRCLFPEDPPPKLvpSCTVAGVLGPTTAVVAGLQALEALKLLLGkgePNLAGRLLQFDALTMTFRELRLALKN-PNCP 237


                  .
gi 496843505  241 T 241
Cdd:pfam00899 238 V 238
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
4-263 1.02e-48

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 167.50  E-value: 1.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   4 SRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEeqASNGIPKV 83
Cdd:PRK08762 114 ERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTE--DRVGQPKV 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  84 VAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVV----QSTYVEAA 159
Cdd:PRK08762 192 DSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFrfegQVSVFDAG 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 160 FIPGETPCFNCMLPNIPAISLT--CDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGFSRmq 235
Cdd:PRK08762 272 RQRGQAPCYRCLFPEPPPPELApsCAEAGVLGVLPGVIGLLQATEAIKLLLGIgdPLTGRLLTFDALAMRFRELRLPP-- 349

                        250       260
                 ....*....|....*....|....*...
gi 496843505 236 ETSCPTCGTEPSYPHLKEakhhYATLCG 263
Cdd:PRK08762 350 DPHCPVCAPGRPFPGYID----YAAFCA 373
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 5-209 1.48e-44

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 152.69  E-value: 1.48e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEeqASNGIPKVV 84
Cdd:PRK05690  12 RYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDD--ATIGQPKVE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:PRK05690  90 SARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTVFTYQD 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 496843505 165 -TPCFNCMLPNIPAISLTCDTVGVIAPAVTMTTSFQLRDALKILAG 209
Cdd:PRK05690 170 dEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTG 215
PRK08328 PRK08328
hypothetical protein; Provisional
 5-229 8.11e-35

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 126.83  E-value: 8.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFkaINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGiPKVV 84
Cdd:PRK08328   9 RYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKN-PKPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGvVQSTYVE-AAFIPG 163
Cdd:PRK08328  86 SAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGA-VEGTYGQvTTIVPG 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496843505 164 ETPCFNCMLPNIP----AISLTCDTVGVIApavtmttSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVI 229
Cdd:PRK08328 165 KTKRLREIFPKVKkkkgKFPILGATAGVIG-------SIQAMEVIKLITGYgePLLNKLLIVDLANNVFEVV 229
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 4-229 6.92e-34

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 127.68  E-value: 6.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   4 SRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEeqASNGIPKV 83
Cdd:PRK05597   7 ARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHST--AGVGQPKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  84 VAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPG 163
Cdd:PRK05597  85 ESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAG 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 164 ETPCFNCMLPNIPAISL--TCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVI 229
Cdd:PRK05597 165 HGPIYEDLFPTPPPPGSvpSCSQAGVLGPVVGVVGSAMAMEALKLITGVgtPLIGKLGYYDSLDGTWEYI 234
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 28-163 2.06e-33

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: 120.45  E-value: 2.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  28 VAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTeeQASNGIPKVVAAKEKLTEIRHDIEIEAFIEHAT 107
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLAR--QADIGKPKAEVAARRLNELNPGVNVTAVPEGIS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496843505 108 PSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWI-YGGVVQSTYVEAAFIPG 163
Cdd:cd01483   80 EDNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIdAGGLGLGGDIQVIDIGS 136
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 3-210 8.47e-28

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 111.51  E-value: 8.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   3 QSRYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPK 82
Cdd:PRK05600  19 LRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDV--GRPK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  83 VVAAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQstyveaafIP 162
Cdd:PRK05600  97 VEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLR--------FH 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496843505 163 GETPCFNC-----------MLPNIPAISLT--CDTVGVIAPAVTMTTSFQLRDALKILAGV 210
Cdd:PRK05600 169 GELAVFNSgpdhrgvglrdLFPEQPSGDSIpdCATAGVLGATTAVIGALMATEAIKFLTGI 229
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 5-241 2.47e-26

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 107.49  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLftEEQASNGIPKVV 84
Cdd:PRK07878  22 RYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVI--HGQSDVGRSKAQ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVV----QSTYVEAAF 160
Cdd:PRK07878 100 SARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYrfegQASVFWEDA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505 161 IPGETPCFNCMLPNIPAISL--TCDTVGVIAPAVTMTTSFQLRDALKILAGV--PFQAKLTFGDIWDMTHQVIGFSRmqE 236
Cdd:PRK07878 180 PDGLGLNYRDLYPEPPPPGMvpSCAEGGVLGVLCASIGSIMGTEAIKLITGIgePLLGRLMVYDALEMTYRTIKIRK--D 257


                 ....*
gi 496843505 237 TSCPT 241
Cdd:PRK07878 258 PSTPK 262
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
5-225 5.32e-25

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 104.05  E-value: 5.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVV 84
Cdd:PRK07411  18 RYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWV--GKPKIE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGE 164
Cdd:PRK07411  96 SAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVFNYEG 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496843505 165 TPCFNCMLPNIPAISL--TCDTVGV--IAPAVTMTtsFQLRDALKILAGVP--FQAKLTFGDIWDMT 225
Cdd:PRK07411 176 GPNYRDLYPEPPPPGMvpSCAEGGVlgILPGIIGV--IQATETIKIILGAGntLSGRLLLYNALDMK 240
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 15-146 2.84e-24

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: 98.83  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  15 INQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVAAKEKLTEIR 94
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTV--GKPKVEVMAERIRDIN 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496843505  95 HDIEIEAFIEHATPSFLEKHL-QKVDLIIDATDNFDTRLMINDFAYKHRIPWI 146
Cdd:cd00755   79 PECEVDAVEEFLTPDNSEDLLgGDPDFVVDAIDSIRAKVALIAYCRKRKIPVI 131
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
8-141 2.60e-23

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 95.69  E-value: 2.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   8 RQVLFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQasnGIPKVVAAK 87
Cdd:PRK08644  11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQI---GMPKVEALK 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496843505  88 EKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKH 141
Cdd:PRK08644  88 ENLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLEH 141
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 27-134 5.70e-21

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: 88.21  E-value: 5.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  27 SVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQasnGIPKVVAAKEKLTEIRHDIEIEAFIEHA 106
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQI---GEPKVEALKENLREINPFVKIEAINIKI 77

                         90       100
                 ....*....|....*....|....*...
gi 496843505 107 TPSFLEKHLQKVDLIIDATDNFDTRLMI 134
Cdd:cd01487   78 DENNLEGLFGDCDIVVEAFDNAETKAML 105
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 6-149 1.98e-14

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 70.91  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   6 YSRQVlfKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGIPKVVA 85
Cdd:cd01485    2 YDRQI--RLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSNSGMNRAAA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496843505  86 AKEKLTEIRHDIEIEaFIEHATPSFL---EKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGG 149
Cdd:cd01485   80 SYEFLQELNPNVKLS-IVEEDSLSNDsniEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCA 145
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 28-170 1.29e-13

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 70.49  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  28 VAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVAAKEKLTEIRHDIEIEAFieHAT 107
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHV--GKSKAQVAKEAVLSFNPNVKIVAY--HAN 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496843505 108 ---PSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWI------YGGVVQstyveaAFIPGETPCFNC 170
Cdd:cd01489   78 ikdPDFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIesgttgFLGQVQ------VIKKGKTECYEC 143
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 27-172 1.12e-12

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: 66.45  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  27 SVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFteEQASNGIPKVVAAKEKLTEIRHDIEIEAFIEHA 106
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLF--RPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496843505 107 TP--SFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPGETPCFNCML 172
Cdd:cd01484   79 GPeqDFNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECTL 146
PRK08223 PRK08223
hypothetical protein; Validated
 15-144 2.54e-11

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 63.16  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  15 INQEGQARIMSKSVAIIGMGALG-THVAEgLTRSGVKRIVMVDRDYIETSNLQRQtlFTEEQASNGIPKVVAAKEKLTEI 93
Cdd:PRK08223  17 ITPTEQQRLRNSRVAIAGLGGVGgIHLLT-LARLGIGKFTIADFDVFELRNFNRQ--AGAMMSTLGRPKAEVLAEMVRDI 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496843505  94 RHDIEIEAFIEHATPSFLEKHLQKVDLIIDATD--NFDTRLMINDFAYKHRIP 144
Cdd:PRK08223  94 NPELEIRAFPEGIGKENADAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIP 146
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 27-172 2.24e-10

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: 60.45  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  27 SVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVAAKEKLTEIRHDIEIEAF---I 103
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDI--GKPKAEVAAKFVNDRVPGVNVTPHfgkI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496843505 104 EHATPSFlekhLQKVDLIIDATDNFDTRLMINDFA--------YKHRIPWIYGGVVQSTYVEAAFIPGETPCFNCML 172
Cdd:cd01488   79 QDKDEEF----YRQFNIIICGLDSIEARRWINGTLvslllyedPESIIPLIDGGTEGFKGHARVILPGITACIECSL 151
PRK14852 PRK14852
hypothetical protein; Provisional
 15-163 3.74e-10

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 61.25  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  15 INQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQtlFTEEQASNGIPKVVAAKEKLTEIR 94
Cdd:PRK14852 322 VDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQ--YGASIASFGRGKLDVMTERALSVN 399

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496843505  95 HDIEIEAFIEHATPSFLEKHLQKVDLIIDATDNF--DTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIPG 163
Cdd:PRK14852 400 PFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFalDIRRRLFNRALELGIPVITAGPLGYSCALLVFMPG 470
PRK14851 PRK14851
hypothetical protein; Provisional
 6-163 8.34e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 59.87  E-value: 8.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   6 YSRQV-LFKAINQEgqaRIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQtlFTEEQASNGIPKVV 84
Cdd:PRK14851  26 FSRNIgLFTPGEQE---RLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQ--FGARVPSFGRPKLA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  85 AAKEKLTEIRHDIEIEAFIEHATPSFLEKHLQKVDLIIDATD--NFDTRLMINDFAYKHRIPWIYGGVVQSTYVEAAFIP 162
Cdd:PRK14851 101 VMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDffQFEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTP 180


                 .
gi 496843505 163 G 163
Cdd:PRK14851 181 Q 181
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 4-135 1.02e-09

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: 59.90  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505     4 SRYSRQVlfKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVK-----RIVMVDRDYIETSNLQRQTLFTEEQAsn 78
Cdd:TIGR01408  400 DRYDAQI--AVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHI-- 475

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496843505    79 GIPKVVAAKEKLTEIRHDIEIEAFIEHATPS----FLEKHLQKVDLIIDATDNFDTRLMIN 135
Cdd:TIGR01408  476 GKPKSYTAADATLKINPQIKIDAHQNRVGPEtetiFNDEFYEKLDVVINALDNVEARRYVD 536
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 30-131 1.06e-09

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 58.54  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  30 IIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGIPKVVAAKEKLTEIRHDIEIEAF------I 103
Cdd:cd01486    4 LLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCKGGKPKAEAAAERLKEIFPSIDATGIvlsipmP 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496843505 104 EHATPS----FLEKHLQKV-DLIID------ATDNFDTR 131
Cdd:cd01486   84 GHPISEsevpSTLKDVKRLeELIKDhdviflLTDSRESR 122
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 6-150 1.49e-08

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 53.83  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   6 YSRQV-LFKAinqEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEqaSNGIPKVV 84
Cdd:cd01492    4 YDRQIrLWGL---EAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAE--DLGQNRAE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843505  85 AAKEKLTEI--RHDIEIEA-FIEHATPSFLEKHlqkvDLIIDATDNFDTRLMINDFAYKHRIPWIYGGV 150
Cdd:cd01492   79 ASLERLRALnpRVKVSVDTdDISEKPEEFFSQF----DVVVATELSRAELVKINELCRKLGVKFYATGV 143
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 27-136 2.16e-08

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: 55.37  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  27 SVAIIGMGALGTHVAE-----GLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVAAKEKLTEIRHDIEIEA 101
Cdd:cd01490    1 KVFLVGAGAIGCELLKnfalmGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDV--GKPKSEVAAAAVKAMNPDLKITA 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496843505 102 FIEHATPS----FLEKHLQKVDLIIDATDNFDTRLMIND 136
Cdd:cd01490   79 LQNRVGPEtehiFNDEFWEKLDGVANALDNVDARMYVDR 117
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 6-144 2.74e-08

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 55.28  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505     6 YSRQVLfkAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVA 85
Cdd:TIGR01408    7 YSRQLY--VLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDV--GRNRAEA 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 496843505    86 AKEKLTEIRHDIEIEAfiehATPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIP 144
Cdd:TIGR01408   83 VVKKLAELNPYVHVSS----SSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPP 137
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 6-146 7.38e-08

Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 53.04  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   6 YSRQ--VL-FKAINQegqariMSKS-VAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIP 81
Cdd:cd01491    2 YSRQlyVLgHEAMKK------LQKSnVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDI--GKN 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496843505  82 KVVAAKEKLTEIRHDIEIEAFiehaTPSFLEKHLQKVDLIIDATDNFDTRLMINDFAYKHRIPWI 146
Cdd:cd01491   74 RAEASQARLAELNPYVPVTVS----TGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFI 134
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 5-147 1.58e-07

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 52.31  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   5 RYSRQV-LFKAinqEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQrQTLFTEEQaSNGIPKV 83
Cdd:cd01493    2 KYDRQLrLWGE---HGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLG-NNFFLDAS-SLGKSRA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  84 VAAKEKLTEIRHDIEIEAFIEHAT------PSFLEKHlqkvDLIIDATDNFDTRLMINDFAYKHRIPWIY 147
Cdd:cd01493   77 EATCELLQELNPDVNGSAVEESPEalldndPSFFSQF----TVVIATNLPESTLLRLADVLWSANIPLLY 142
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 28-159 6.01e-07

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 50.19  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505  28 VAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQAsnGIPKVVAAKEKLTEIRHDIEIEAFIEHAT 107
Cdd:PRK15116  33 ICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNV--GLAKAEVMAERIRQINPECRVTVVDDFIT 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496843505 108 PSFLEKHL-QKVDLIIDATDNFDTRLMINDFAYKHRIPWIY----GGVVQSTYVEAA 159
Cdd:PRK15116 111 PDNVAEYMsAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTtggaGGQIDPTQIQVV 167
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 22-102 4.90e-05

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 44.93  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   22 RIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQA-SNGIPKVVAAKEKLTEIRHDIEIE 100
Cdd:TIGR01381 335 RYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDClLGGRGKAETAQKALKRIFPSIQAT 414


                  ..
gi 496843505  101 AF 102
Cdd:TIGR01381 415 GH 416
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
 11-86 4.34e-04

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 38.51  E-value: 4.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496843505  11 LFKAINQEGQARIMSKSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRDYIETSNLQRQTLFTEEQASNGIPKVVAA 86
Cdd:cd05191    9 LLKAAGKVTNKSLKGKTVVVLGAGEVGKGIAKLLADEGGKKVVLCDRDILVTATPAGVPVLEEATAKINEGAVVID 84
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 28-134 1.92e-03

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 37.51  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843505   28 VAIIGMGALGTHVAEGLTRSGvkRIVMVDRDyietsnlqrqtlfteeqasngipkvvaaKEKLTEIRhDIEIEAFIEHAT 107
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG--DVVVIDKD----------------------------EERVEELR-EEGVPVVVGDAT 49

                          90       100
                  ....*....|....*....|....*....
gi 496843505  108 -PSFLEK-HLQKVDLIIDATDNFDTRLMI 134
Cdd:pfam02254  50 dEEVLEEaGIEEADAVIAATGDDEANILI 78
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 26-58 3.94e-03

Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 38.82  E-value: 3.94e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 496843505  26 KSVAIIGMGALGTHVAEGLTRSGVKRIVMVDRD 58
Cdd:cd08301  189 STVAIFGLGAVGLAVAEGARIRGASRIIGVDLN 221
 
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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