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Conserved domains on  [gi|41056017|ref|NP_956421|]
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adenylyltransferase and sulfurtransferase MOCS3 [Danio rerio]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 10091539)

HesA/MoeB/ThiF family protein with a Rhodanese Homology Domain (RHOD), similar to adenylyltransferase and sulfurtransferases MOCS3 and UBA4 that play a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln)

Graphical summary

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List of domain hits

 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 ...
 62-290 5.63e-126

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: 364.88  E-value: 5.63e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 142 AQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 222 CYRCLYPIPPPPEtVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL 290
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-459 1.29e-54

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


:

Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 177.89  E-value: 1.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 327 LHLLSREQRVSVQDYKGILDHSTPHLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLlkeaisdLQEHLNNQSPV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSL-------QELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 41056017 407 QVFVVCKLGNDSQKAVQLLEKMSGaeveAMTVKDIGGGLMAWAKKIDYCFPQY 459
Cdd:cd01526  74 PIYVVCRRGNDSQTAVRKLKELGL----ERFVRDIIGGLKAWADKVDPTFPLY 122
 
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 ...
 62-290 5.63e-126

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: 364.88  E-value: 5.63e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 142 AQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 222 CYRCLYPIPPPPEtVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL 290
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 56-302 3.58e-123

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: 358.29  E-value: 3.58e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  56 NNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQ 135
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 136 PKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVY 215
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 216 NYRGGPCYRCLYPIPPPPEtvTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRLRsRQK 295
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPG--PSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                ....*..
gi 41056017 296 ECVVCGE 302
Cdd:COG0476 238 DCPVCGE 244
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
46-459 2.07e-121

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 359.43  E-value: 2.07e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   46 LSPLRLNTSLNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQ 125
Cdd:PRK07411   2 LNPNLDEIQLSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  126 VLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASA 205
Cdd:PRK07411  82 VIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  206 LRMEGQLTVYNYRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRF 285
Cdd:PRK07411 162 FRFEGQATVFNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  286 RSIRLRSRQkecvvcgEKPTITELQDYEHFCG---SAATDKCRRLHLlsreQRVSVQDYKGILDHSTP-HLLLDVRPKVE 361
Cdd:PRK07411 242 RELKLRPNP-------ERPVIEKLIDYEQFCGipqAKAAEAAQKAEI----PEMTVTELKALLDSGADdFVLIDVRNPNE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  362 VDICRLSNSLHIPLASLEDkkpehitllKEAISDLQEHLNNQspvQVFVVCKLGNDSQKAVQLLEKmsgAEVEAMTVKdi 441
Cdd:PRK07411 311 YEIARIPGSVLVPLPDIEN---------GPGVEKVKELLNGH---RLIAHCKMGGRSAKALGILKE---AGIEGTNVK-- 373

                        410
                 ....*....|....*...
gi 41056017  442 gGGLMAWAKKIDYCFPQY 459
Cdd:PRK07411 374 -GGITAWSREVDPSVPQY 390
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 63-299 1.22e-99

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: 298.02  E-value: 1.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    63 YSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAA 142
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   143 QAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGPC 222
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41056017   223 YRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASG-QECSFAQQLLMFDGEQTRFRSIRLRSRQKECVV 299
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGkGEPNLAGRLLQFDALTMTFRELRLALKNPNCPV 238
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 62-262 5.58e-83

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: 254.20  E-value: 5.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSA 141
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   142 AQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRG-G 220
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGeG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 41056017   221 PCYRCLYpiPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLK 262
Cdd:TIGR02356 161 PCLRCLF--PDIADTGPSCATAGVIGPVVGVIGSLQALEALK 200
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-459 1.29e-54

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 177.89  E-value: 1.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 327 LHLLSREQRVSVQDYKGILDHSTPHLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLlkeaisdLQEHLNNQSPV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSL-------QELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 41056017 407 QVFVVCKLGNDSQKAVQLLEKMSGaeveAMTVKDIGGGLMAWAKKIDYCFPQY 459
Cdd:cd01526  74 PIYVVCRRGNDSQTAVRKLKELGL----ERFVRDIIGGLKAWADKVDPTFPLY 122
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 334-453 1.90e-11

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 60.75  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 334 QRVSVQDYKGILDHSTPhLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEhitLLKEAisdlqehlnnqspvQVFVVCK 413
Cdd:COG0607   4 KEISPAELAELLESEDA-VLLDVREPEEFAAGHIPGAINIPLGELAERLDE---LPKDK--------------PIVVYCA 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41056017 414 LGNDSQKAVQLLEKMsGAEveamTVKDIGGGLMAWAKKID 453
Cdd:COG0607  66 SGGRSAQAAALLRRA-GYT----NVYNLAGGIEAWKAAGL 100
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 351-453 2.73e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 59.78  E-value: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    351 HLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEhitLLKEAISDLQEHLNNQSPVQVFVVCKLGNDSQKAVQLLEKMsG 430
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGE---LDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL-G 80

                           90       100
                   ....*....|....*....|...
gi 41056017    431 AEveamTVKDIGGGLMAWAKKID 453
Cdd:smart00450  81 FK----NVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 347-449 7.24e-09

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 52.87  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   347 HSTPHLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLLKEaisdLQEHLNNQspvQVFVVCKLGNDSQKAVQLLE 426
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEK----LLELLKDK---PIVVYCNSGNRAAAAAALLK 74

                          90       100
                  ....*....|....*....|...
gi 41056017   427 KMSGAEveamtVKDIGGGLMAWA 449
Cdd:pfam00581  75 ALGYKN-----VYVLDGGFEAWK 92
 
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 ...
 62-290 5.63e-126

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: 364.88  E-value: 5.63e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 142 AQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 222 CYRCLYPIPPPPEtVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL 290
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 56-302 3.58e-123

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: 358.29  E-value: 3.58e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  56 NNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQ 135
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 136 PKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVY 215
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 216 NYRGGPCYRCLYPIPPPPEtvTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRLRsRQK 295
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPG--PSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                ....*..
gi 41056017 296 ECVVCGE 302
Cdd:COG0476 238 DCPVCGE 244
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
46-459 2.07e-121

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 359.43  E-value: 2.07e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   46 LSPLRLNTSLNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQ 125
Cdd:PRK07411   2 LNPNLDEIQLSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  126 VLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASA 205
Cdd:PRK07411  82 VIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  206 LRMEGQLTVYNYRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRF 285
Cdd:PRK07411 162 FRFEGQATVFNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  286 RSIRLRSRQkecvvcgEKPTITELQDYEHFCG---SAATDKCRRLHLlsreQRVSVQDYKGILDHSTP-HLLLDVRPKVE 361
Cdd:PRK07411 242 RELKLRPNP-------ERPVIEKLIDYEQFCGipqAKAAEAAQKAEI----PEMTVTELKALLDSGADdFVLIDVRNPNE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  362 VDICRLSNSLHIPLASLEDkkpehitllKEAISDLQEHLNNQspvQVFVVCKLGNDSQKAVQLLEKmsgAEVEAMTVKdi 441
Cdd:PRK07411 311 YEIARIPGSVLVPLPDIEN---------GPGVEKVKELLNGH---RLIAHCKMGGRSAKALGILKE---AGIEGTNVK-- 373

                        410
                 ....*....|....*...
gi 41056017  442 gGGLMAWAKKIDYCFPQY 459
Cdd:PRK07411 374 -GGITAWSREVDPSVPQY 390
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
48-320 1.21e-113

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 338.91  E-value: 1.21e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   48 PLRLNTSLNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVL 127
Cdd:PRK08762 101 PLERPRLLTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  128 HTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALR 207
Cdd:PRK08762 181 HTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  208 MEGQLTVYN----YRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQT 283
Cdd:PRK08762 261 FEGQVSVFDagrqRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAM 340

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 41056017  284 RFRSIRLRsRQKECVVCGEKPTITELQDYEHFCGSAA 320
Cdd:PRK08762 341 RFRELRLP-PDPHCPVCAPGRPFPGYIDYAAFCAGAA 376
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 55-297 1.66e-101

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 303.30  E-value: 1.66e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   55 LNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQG 134
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  135 QPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTV 214
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  215 YNYR-GGPCYRCLYPIPPPPEtvTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRLRsR 293
Cdd:PRK05690 165 FTYQdDEPCYRCLSRLFGENA--LTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK-R 241


                 ....
gi 41056017  294 QKEC 297
Cdd:PRK05690 242 DPGC 245
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 44-459 1.79e-100

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 305.86  E-value: 1.79e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   44 TSLSPL-RLNTSLNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNL 122
Cdd:PRK07878   3 TSLPPLvEPAAELTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  123 HRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVS 202
Cdd:PRK07878  83 QRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  203 ASALRMEGQLTVY----NYRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMF 278
Cdd:PRK07878 163 GSIYRFEGQASVFwedaPDGLGLNYRDLYPEPPPPGMVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLGRLMVY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  279 DGEQTRFRSIRLRsRQKECvvcgekPTITELQDYEHFCGSAATDKcrrlHLLSREQRVSVQDYKGILDHSTPHLLLDVRP 358
Cdd:PRK07878 243 DALEMTYRTIKIR-KDPST------PKITELIDYEAFCGVVSDEA----QQAAAGSTITPRELKEWLDSGKKIALIDVRE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  359 KVEVDIcrlsnsLHIPLASLedkKPEHITLLKEAISDLQEHLnnqspvQVFVVCKLGNDSQKAVQLLEKMSGAevEAMTV 438
Cdd:PRK07878 312 PVEWDI------VHIPGAQL---IPKSEILSGEALAKLPQDR------TIVLYCKTGVRSAEALAALKKAGFS--DAVHL 374

                        410       420
                 ....*....|....*....|.
gi 41056017  439 kdiGGGLMAWAKKIDYCFPQY 459
Cdd:PRK07878 375 ---QGGVVAWAKQVDPSLPMY 392
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 63-299 1.22e-99

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: 298.02  E-value: 1.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    63 YSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAA 142
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   143 QAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGPC 222
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41056017   223 YRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASG-QECSFAQQLLMFDGEQTRFRSIRLRSRQKECVV 299
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGkGEPNLAGRLLQFDALTMTFRELRLALKNPNCPV 238
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 62-262 5.58e-83

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: 254.20  E-value: 5.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSA 141
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   142 AQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRG-G 220
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGeG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 41056017   221 PCYRCLYpiPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLK 262
Cdd:TIGR02356 161 PCLRCLF--PDIADTGPSCATAGVIGPVVGVIGSLQALEALK 200
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 57-448 1.19e-67

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 220.13  E-value: 1.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   57 NDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQP 136
Cdd:PRK05597   3 NLDIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  137 KALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYN 216
Cdd:PRK05597  83 KAESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  217 YRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRLRSrqke 296
Cdd:PRK05597 163 AGHGPIYEDLFPTPPPPGSVPSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLIGKLGYYDSLDGTWEYIPVVG---- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  297 cvvcgeKPTITELQDYEHFCGSAATdkcrrlhllSREQRVSVQDYKGILDHSTphlLLDVRPKVEVDICRLSNSLHIPLA 376
Cdd:PRK05597 239 ------NPAVLERVRGSTPVHGISG---------GFGEVLDVPRVSALPDGVT---LIDVREPSEFAAYSIPGAHNVPLS 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056017  377 S-LEDKKPEHITLLKEAIsdlqehlnnqspvqvfVVCKLGNDSQKAVQLLEKmsgAEVEAMTVKDigGGLMAW 448
Cdd:PRK05597 301 AiREGANPPSVSAGDEVV----------------VYCAAGVRSAQAVAILER---AGYTGMSSLD--GGIEGW 352
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-459 1.29e-54

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 177.89  E-value: 1.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 327 LHLLSREQRVSVQDYKGILDHSTPHLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLlkeaisdLQEHLNNQSPV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSL-------QELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 41056017 407 QVFVVCKLGNDSQKAVQLLEKMSGaeveAMTVKDIGGGLMAWAKKIDYCFPQY 459
Cdd:cd01526  74 PIYVVCRRGNDSQTAVRKLKELGL----ERFVRDIIGGLKAWADKVDPTFPLY 122
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 45-423 3.82e-53

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 182.39  E-value: 3.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   45 SLSPlrlNTSLNNDDIMRYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHR 124
Cdd:PRK05600   7 TLSP---FMQLPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  125 QVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSAS 204
Cdd:PRK05600  84 QILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  205 ALRMEGQLTVYN---YRGGPCYRCLYPIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGE 281
Cdd:PRK05600 164 VLRFHGELAVFNsgpDHRGVGLRDLFPEQPSGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQPGTVLSYDAL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  282 QTRFRSIRLRSRQKECVVCGEKPTItelqdyehfcgSAATDKCRRLHLLSREQRVSvqdykgildhstphlLLDVRPKVE 361
Cdd:PRK05600 244 TATTRSFRVGADPARPLVTRLRPSY-----------EAARTDTTSLIDATLNGSAT---------------LLDVREPHE 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41056017  362 V---DICRLSNSLHIPLASLEDkkpehitllkeaISDLQEHLNNQSPVQVFVVCKLGNDSQKAVQ 423
Cdd:PRK05600 298 VllkDLPEGGASLKLPLSAITD------------DADILHALSPIDGDNVVVYCASGIRSADFIE 350
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 62-310 4.87e-43

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 154.77  E-value: 4.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTE--LTQGQPKAL 139
Cdd:PRK07688   4 RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTEsdVKNNLPKAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  140 SAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGqLTvYNYRG 219
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYG-LS-YTIIP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  220 G--PCYRCLYP-IPPPPETvtnCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL-RSRQK 295
Cdd:PRK07688 162 GktPCLRCLLQsIPLGGAT---CDTAGIISPAVQIVASYQVTEALKLLVGDYEALRDGLVSFDVWKNEYSCMNVqKLKKD 238

                        250
                 ....*....|....*
gi 41056017  296 ECVVCGEKPTITELQ 310
Cdd:PRK07688 239 NCPSCGEKALYPYLN 253
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 62-311 1.85e-40

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 147.95  E-value: 1.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   62 RYSRQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTE--LTQGQPKAL 139
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEedAKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  140 SAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRG 219
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  220 GPCYRCLypIPPPPETVTNCSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL-RSRQKECV 298
Cdd:PRK12475 164 TPCLRCL--MEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVEDFEALRETFLSFDIWNNQNMSIKVnKQKKDTCP 241

                        250
                 ....*....|...
gi 41056017  299 VCGEKPTITELQD 311
Cdd:PRK12475 242 SCGLTRTYPSLTF 254
PRK08328 PRK08328
hypothetical protein; Provisional
 55-290 3.89e-40

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 143.78  E-value: 3.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   55 LNNDDIMRYSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQG 134
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  135 Q-PKALSAAQAISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLT 213
Cdd:PRK08328  80 KnPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41056017  214 VYNYRGGPCYRCLYPIPPPPEtvtncSDGGVLGVVPGIMGCLQALEVLKIASGQECSFAQQLLMFDGEQTRFRSIRL 290
Cdd:PRK08328 160 TIVPGKTKRLREIFPKVKKKK-----GKFPILGATAGVIGSIQAMEVIKLITGYGEPLLNKLLIVDLANNVFEVVEL 231
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 85-214 8.24e-35

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: 126.61  E-value: 8.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  85 VLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRE 164
Cdd:cd01483   2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISED 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 41056017 165 NAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTV 214
Cdd:cd01483  82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQV 131
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 84-206 8.87e-24

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: 97.45  E-value: 8.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  84 SVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQvlHTELTQ-GQPKALSAAQAISRMNSTVQCVPYHLQLS 162
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ--QYFLSQiGEPKVEALKENLREINPFVKIEAINIKID 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 41056017 163 RENAIQLIQQYDIVADCSDNVPT-RYLVNDACVLTSRPLVSASAL 206
Cdd:cd01487  79 ENNLEGLFGDCDIVVEAFDNAETkAMLAESLLGNKNKPVVCASGM 123
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 85-232 7.07e-23

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: 98.61  E-value: 7.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  85 VLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQL-SR 163
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIkDP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 164 ENAIQLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGPCYRClYPIPPP 232
Cdd:cd01489  82 DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYEC-QPKETP 149
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
65-206 9.90e-23

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 95.69  E-value: 9.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   65 RQLLLPELGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQvlHTELTQ-GQPKALSAAQ 143
Cdd:PRK08644  11 EAMLASRHTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ--QYFISQiGMPKVEALKE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41056017  144 AISRMNSTVQCVPYHLQLSRENAIQLIQQYDIVADCSDNVPT-RYLVNDACVLTSRPLVSASAL 206
Cdd:PRK08644  89 NLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDNAETkAMLVETVLEHPGKKLVAASGM 152
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 84-240 4.11e-22

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: 94.57  E-value: 4.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  84 SVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSR 163
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 164 ENAIQL--IQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRGGPCYRClyPIPPPPETVTNCS 240
Cdd:cd01484  81 EQDFNDtfFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIEC--TLYPPQKNFPMCT 157
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 72-203 9.33e-20

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: 87.66  E-value: 9.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  72 LGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNST 151
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 41056017 152 VQCVPYHLQLSRENAIQLI-QQYDIVADCSDNVPTRYLVNDACVLTSRPLVSA 203
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLgGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISS 133
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 61-262 1.66e-19

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


Pssm-ID: 440792  Cd Length: 247  Bit Score: 87.44  E-value: 1.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  61 MRYSRQL----LLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQP 136
Cdd:COG1179   1 MDMERRFsrteRL--YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 137 KALSAAQAISRMNSTVQCVPYHLQLSRENAIQLI-QQYDIVADCSDNVPTRYLVNDACVLTSRPLVSA---------SAL 206
Cdd:COG1179  79 KVEVMAERIRDINPDCEVTAIDEFVTPENADELLsEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSmgaggkldpTKI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 207 R---------------MEGQLTVYNYRGGpcYRCLY----PIPP-PPETVTNCSDGG----VLG---VVPGIMGCLQALE 259
Cdd:COG1179 159 RvadlsktsncplaakVRKRLRKRGIPKG--VKVVYsteqPRKPqADGTVCDTGGTGlkcaGPGsisFVPAVFGLIAAGE 236


                ...
gi 41056017 260 VLK 262
Cdd:COG1179 237 VIR 239
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 84-215 1.55e-17

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: 84.26  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  84 SVLVVGCGGLGCPLAQYLAAAGI-----GRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYH 158
Cdd:cd01490   1 KVFLVGAGAIGCELLKNFALMGVgtgesGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41056017 159 LQLSREN-AI---QLIQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASALRMEGQLTVY 215
Cdd:cd01490  81 NRVGPETeHIfndEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVV 141
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 84-240 2.18e-17

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: 82.40  E-value: 2.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  84 SVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSR 163
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 164 ENaIQLIQQYDIVADCSDNVPTRYLVND-ACVLTS-------RPLVSASALRMEGQLTVYNYRGGPCYRCLYPIPPPPET 235
Cdd:cd01488  81 KD-EEFYRQFNIIICGLDSIEARRWINGtLVSLLLyedpesiIPLIDGGTEGFKGHARVILPGITACIECSLDLFPPQVT 159


                ....*
gi 41056017 236 VTNCS 240
Cdd:cd01488 160 FPLCT 164
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 80-206 2.58e-15

thiamine biosynthesis protein ThiF, family 2; 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 one the E. 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 divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 74.52  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    80 ISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTqGQPKALSAAQAISRMNSTVQCVPYHL 159
Cdd:TIGR02354  19 LEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQV-GEPKTEALKENISEINPYTEIEAYDE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 41056017   160 QLSRENAIQLIQQYDIVADCSDNVPTRYLVNDAcVLTSRP---LVSASAL 206
Cdd:TIGR02354  98 KITEENIDKFFKDADIVCEAFDNAEAKAMLVNA-VLEKYKdkyLIAASGL 146
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 41-214 2.66e-15

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: 78.78  E-value: 2.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017     41 EKVTSLSPLRLNTSLNNDDimRYSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGI-----GRLGLLDYD 115
Cdd:TIGR01408  382 ESLPSLGKPECEEFLPRGD--RYDAQIAV--FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPD 457

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    116 VVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRENAI----QLIQQYDIVADCSDNVPTRYLVND 191
Cdd:TIGR01408  458 LIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVGPETETifndEFYEKLDVVINALDNVEARRYVDS 537

                          170       180
                   ....*....|....*....|...
gi 41056017    192 ACVLTSRPLVSASALRMEGQLTV 214
Cdd:TIGR01408  538 RCLAFLKPLLESGTLGTKGNTQV 560
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 334-453 1.90e-11

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 60.75  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 334 QRVSVQDYKGILDHSTPhLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEhitLLKEAisdlqehlnnqspvQVFVVCK 413
Cdd:COG0607   4 KEISPAELAELLESEDA-VLLDVREPEEFAAGHIPGAINIPLGELAERLDE---LPKDK--------------PIVVYCA 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41056017 414 LGNDSQKAVQLLEKMsGAEveamTVKDIGGGLMAWAKKID 453
Cdd:COG0607  66 SGGRSAQAAALLRRA-GYT----NVYNLAGGIEAWKAAGL 100
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 351-453 2.73e-11

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 59.78  E-value: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    351 HLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEhitLLKEAISDLQEHLNNQSPVQVFVVCKLGNDSQKAVQLLEKMsG 430
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGE---LDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL-G 80

                           90       100
                   ....*....|....*....|...
gi 41056017    431 AEveamTVKDIGGGLMAWAKKID 453
Cdd:smart00450  81 FK----NVYLLDGGYKEWSAAGP 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 352-449 4.33e-10

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 56.15  E-value: 4.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 352 LLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHItLLKEAIsdlqehlnnqspvqVFVVCKLGNDSQKAVQLLEKMSGA 431
Cdd:cd00158  12 VLLDVREPEEYAAGHIPGAINIPLSELEERAALLE-LDKDKP--------------IVVYCRSGNRSARAAKLLRKAGGT 76

                        90
                ....*....|....*...
gi 41056017 432 EveamtVKDIGGGLMAWA 449
Cdd:cd00158  77 N-----VYNLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 347-449 7.24e-09

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 52.87  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   347 HSTPHLLLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLLKEaisdLQEHLNNQspvQVFVVCKLGNDSQKAVQLLE 426
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEK----LLELLKDK---PIVVYCNSGNRAAAAAALLK 74

                          90       100
                  ....*....|....*....|...
gi 41056017   427 KMSGAEveamtVKDIGGGLMAWA 449
Cdd:pfam00581  75 ALGYKN-----VYVLDGGFEAWK 92
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 37-188 2.54e-08

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: 56.10  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017    37 PELQEKVTSLSPLRL-NTSLN-NDDIMRYSrqlLLPELGVKgqiAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDY 114
Cdd:TIGR01381 297 PISVDLSKEFDPKRLaERSVDlNLKLMKWR---LHPDLQLE---RYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDN 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   115 DVVELSNLHRQVLHT---ELTQGQPKALSAAQAISRMNSTVQCVPYHLQ-------LSRENA----------IQLIQQYD 174
Cdd:TIGR01381 371 GKVSYSNPVRQSLSNfedCLLGGRGKAETAQKALKRIFPSIQATGHRLTvpmpghpIDEKDVpelekdiarlEQLIKDHD 450

                         170
                  ....*....|....
gi 41056017   175 IVADCSDNVPTRYL 188
Cdd:TIGR01381 451 VVFLLLDSREARWL 464
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 63-193 2.67e-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: 54.97  E-value: 2.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  63 YSRQLllpelGVKGQIAISNI---SVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKAL 139
Cdd:cd01491   2 YSRQL-----YVLGHEAMKKLqksNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAE 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 41056017 140 SAAQAISRMNSTVQCVPYHlqlsRENAIQLIQQYDIVADCSDNVPTRYLVNDAC 193
Cdd:cd01491  77 ASQARLAELNPYVPVTVST----GPLTTDELLKFQVVVLTDASLEDQLKINEFC 126
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 76-183 5.24e-08

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 54.04  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   76 GQIAISNIS---VLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNST- 151
Cdd:PRK15116  21 GEKALQLFAdahICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPEc 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 41056017  152 -VQCVPYHlqLSRENAIQLIQQ-YDIVADCSDNV 183
Cdd:PRK15116 101 rVTVVDDF--ITPDNVAEYMSAgFSYVIDAIDSV 132
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 84-188 1.08e-07

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: 53.15  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  84 SVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHT--ELTQGQPKALSAAQAISRMNSTVQC------- 154
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTfeDCKGGKPKAEAAAERLKEIFPSIDAtgivlsi 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 41056017 155 -VPYHLQLSRENAI---------QLIQQYDIVADCSDNVPTRYL 188
Cdd:cd01486  81 pMPGHPISESEVPStlkdvkrleELIKDHDVIFLLTDSRESRWL 124
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 353-453 1.12e-07

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 49.70  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 353 LLDVRPKVEVDICRLSNSLHIPLASLEDKKPEHITLLKEaisdlqehlnnqspVQVFVVCKLGNDSQKAVQLLEKMSGAE 432
Cdd:cd01528  20 LIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPD--------------KDIVVLCHHGGRSMQVAQWLLRQGFEN 85

                        90       100
                ....*....|....*....|.
gi 41056017 433 veamtVKDIGGGLMAWAKKID 453
Cdd:cd01528  86 -----VYNLQGGIDAWSLEVD 101
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 63-285 1.65e-07

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: 51.65  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  63 YSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVL--HTELTQGQPKALS 140
Cdd:cd01485   2 YDRQIRL--WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFldAEVSNSGMNRAAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 141 AAQAISRMNSTVQC-VPYHLQLSRENAI-QLIQQYD-IVADCSDNVPTrYLVNDACVLTSRPLVSASALRMEGQLtvyny 217
Cdd:cd01485  80 SYEFLQELNPNVKLsIVEEDSLSNDSNIeEYLQKFTlVIATEENYERT-AKVNDVCRKHHIPFISCATYGLIGYA----- 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056017 218 rggpcyRCLYPIppppetvtncsdggvlgvvPGIMGCLQALEVLKIASGQECSFaQQLLMFDG-EQTRF 285
Cdd:cd01485 154 ------FFDFPI-------------------AAFLGGVVAQEAIKSISGKFTPL-NNLYIYDGfESTGP 196
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 63-281 3.89e-07

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: 50.37  E-value: 3.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  63 YSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAA 142
Cdd:cd01492   4 YDRQIRL--WGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017 143 QAISRMNSTVQcvpyhLQLSRENAIQL----IQQYDIVADCSDNVPTRYLVNDACVLTSRPLVSASalrmegqltVYNYR 218
Cdd:cd01492  82 ERLRALNPRVK-----VSVDTDDISEKpeefFSQFDVVVATELSRAELVKINELCRKLGVKFYATG---------VHGLF 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056017 219 GgpcYRCLYPIPPppetvtncsdggVLGVVPGIMgclqALEVLKIASGQEcSFAQQLLMFDGE 281
Cdd:cd01492 148 G---FVFADLLAP------------VAAVVGGIL----AQDVINALSKRE-SPLNNFFVFDGE 190
PRK08223 PRK08223
hypothetical protein; Validated
 85-219 5.65e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 50.84  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   85 VLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAAQAISRMNSTVQCVPYHLQLSRE 164
Cdd:PRK08223  30 VAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKE 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41056017  165 NAIQLIQQYDIVADCSD--NVPTRYLVNDACVLTSRPLVSASALRMEGQLTVYNYRG 219
Cdd:PRK08223 110 NADAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDPGG 166
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 63-152 2.28e-06

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: 50.27  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017     63 YSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPKALSAA 142
Cdd:TIGR01408    7 YSRQLYV--LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90
                   ....*....|
gi 41056017    143 QAISRMNSTV 152
Cdd:TIGR01408   85 KKLAELNPYV 94
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 62-152 5.78e-06

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: 48.45  E-value: 5.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017  62 RYSRQLLLpeLGVKGQIAISNISVLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVE---LSN---LHRQVLhteltqGQ 135
Cdd:cd01493   2 KYDRQLRL--WGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDeedLGNnffLDASSL------GK 73

                        90
                ....*....|....*..
gi 41056017 136 PKALSAAQAISRMNSTV 152
Cdd:cd01493  74 SRAEATCELLQELNPDV 90
PRK07877 PRK07877
Rv1355c family protein;
77-192 6.25e-04

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 42.28  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   77 QIAISNISVLVVGCGgLGCPLAQYLAAAGI-GRLGLLDYDVVELSNLHRqVLHTELTQGQPKALSAAQAISRMNSTVQCV 155
Cdd:PRK07877 102 QERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDPYLPVE 179

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41056017  156 PYHLQLSRENAIQLIQQYDIVADCSDNVPTRYLVNDA 192
Cdd:PRK07877 180 VFTDGLTEDNVDAFLDGLDVVVEECDSLDVKVLLREA 216
PRK14851 PRK14851
hypothetical protein; Provisional
 85-206 1.98e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 40.61  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056017   85 VLVVGCGGLGCPLAQYLAAAGIGRLGLLDYDVVELSNLHRQVLHTELTQGQPK-ALSAAQAISrMNSTVQCVPYHLQLSR 163
Cdd:PRK14851  46 VAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKlAVMKEQALS-INPFLEITPFPAGINA 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41056017  164 ENAIQLIQQYDIVADCSDNVP---TRYLVNDAC-----VLTSRPLVSASAL 206
Cdd:PRK14851 125 DNMDAFLDGVDVVLDGLDFFQfeiRRTLFNMARekgipVITAGPLGYSSAM 175
 
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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