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Conserved domains on  [gi|332009204|gb|AED96587|]
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co-factor for nitrate, reductase and xanthine dehydrogenase 5 [Arabidopsis thaliana]

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 ...
 71-272 1.24e-102

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: 304.40  E-value: 1.24e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  71 RYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 123
Cdd:cd00757    1 RYSRQILLPEIGEEgqeklknarvlvvgagglgspaaeylaAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 124 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 203
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332009204 204 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:cd00757  161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 311-437 5.54e-57

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: 183.66  E-value: 5.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 311 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 390
Cdd:cd01526    1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 332009204 391 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 437
Cdd:cd01526   75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 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 ...
 71-272 1.24e-102

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: 304.40  E-value: 1.24e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  71 RYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 123
Cdd:cd00757    1 RYSRQILLPEIGEEgqeklknarvlvvgagglgspaaeylaAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 124 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 203
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332009204 204 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:cd00757  161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 65-284 7.96e-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: 298.20  E-value: 7.96e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  65 SPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGH 117
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEgqeklkaarvlvvgagglgspvalylaAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 118 PKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 197
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 198 NHNGGPCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRSS 277
Cdd:COG0476  161 IPGDTPCYRCLFPEPPEPGP--SCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                 ....*..
gi 332009204 278 QCTVCGD 284
Cdd:COG0476  238 DCPVCGE 244
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-301 5.72e-92

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 282.67  E-value: 5.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  64 LSPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 116
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEgqrrllearvlligagglgspaalylaAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 117 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 197 YN----HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:PRK08762 268 FDagrqRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRL 347

                        250       260
                 ....*....|....*....|....*....
gi 332009204 273 RgRSSQCTVCGDNSSFNKQTfkdfDYEDF 301
Cdd:PRK08762 348 P-PDPHCPVCAPGRPFPGYI----DYAAF 371
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-281 2.46e-83

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: 255.64  E-value: 2.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   72 YSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 124
Cdd:pfam00899   1 YSRQLALPLIGEDgqeklrnsrvlivgagglgseaakylaRAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  125 AACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPC 204
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332009204  205 YRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEP-LSERMLLFDALSARMRIVKIRGRSSQCTV 281
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnLAGRLLQFDALTMTFRELRLALKNPNCPV 238
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 71-245 4.83e-63

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: 202.20  E-value: 4.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   71 RYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 123
Cdd:TIGR02356   1 RYARQLLLPDIGEEgqqrllnshvliigagglgspaalylaGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  124 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYN-HNGG 202
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDpGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 332009204  203 PCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKL 245
Cdd:TIGR02356 161 PCLRCLFPDIADTGP--SCATAGVIGPVVGVIGSLQALEALKL 201
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 311-437 5.54e-57

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: 183.66  E-value: 5.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 311 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 390
Cdd:cd01526    1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 332009204 391 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 437
Cdd:cd01526   75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 122
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 319-432 2.99e-22

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: 90.80  E-value: 2.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 319 RISSKEFKEILQKkEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCRRG 398
Cdd:COG0607    5 EISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELP---KDK-------------PIVVYCASG 67

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332009204 399 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVNP 432
Cdd:COG0607   68 GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLP 101
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 331-432 2.24e-19

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: 82.89  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   331 KKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANteSCTNPSVFVVCRRGNDSQRAVQYLRE 410
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLG--LDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 332009204   411 SGFDSAKDIIGGLEAWAANVNP 432
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 330-427 3.68e-12

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: 62.12  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  330 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANTEsctnpsVFVVCRRGNDSQRAVQYLR 409
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP------IVVYCNSGNRAAAAAALLK 74

                          90
                  ....*....|....*...
gi 332009204  410 ESGFDSAKDIIGGLEAWA 427
Cdd:pfam00581  75 ALGYKNVYVLDGGFEAWK 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
336-432 2.42e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.24  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 336 VLLDVRPSHHYKIVSLPDSLNIPLANLETRLNEltsALKEKGNghantesctnpSVFVVCRRGNDSQRAVQYLRESGFDS 415
Cdd:PRK08762  19 VLIDVREAHERASGQAEGALRIPRGFLELRIET---HLPDRDR-----------EIVLICASGTRSAHAAATLRELGYTR 84

                         90
                 ....*....|....*..
gi 332009204 416 AKDIIGGLEAWAANVNP 432
Cdd:PRK08762  85 VASVAGGFSAWKDAGLP 101
 
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 ...
 71-272 1.24e-102

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: 304.40  E-value: 1.24e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  71 RYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 123
Cdd:cd00757    1 RYSRQILLPEIGEEgqeklknarvlvvgagglgspaaeylaAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 124 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 203
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332009204 204 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:cd00757  161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 65-284 7.96e-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: 298.20  E-value: 7.96e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  65 SPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGH 117
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEgqeklkaarvlvvgagglgspvalylaAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 118 PKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 197
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 198 NHNGGPCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRSS 277
Cdd:COG0476  161 IPGDTPCYRCLFPEPPEPGP--SCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                 ....*..
gi 332009204 278 QCTVCGD 284
Cdd:COG0476  238 DCPVCGE 244
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-301 5.72e-92

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 282.67  E-value: 5.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  64 LSPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 116
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEgqrrllearvlligagglgspaalylaAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 117 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 197 YN----HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:PRK08762 268 FDagrqRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRL 347

                        250       260
                 ....*....|....*....|....*....
gi 332009204 273 RgRSSQCTVCGDNSSFNKQTfkdfDYEDF 301
Cdd:PRK08762 348 P-PDPHCPVCAPGRPFPGYI----DYAAF 371
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
64-437 1.38e-91

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 282.39  E-value: 1.38e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  64 LSPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 116
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEgqkrlkaasvlcigtgglgsplllylaAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 117 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 197 YNHNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRS 276
Cdd:PRK07411 171 FNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKFRELKLR-PN 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 277 SQCTVCGdnssfnkqtfKDFDYEDFTQFP-LFAGPLNLLPAESRISSKEFKEILQK-KEQHVLLDVRPSHHYKIVSLPDS 354
Cdd:PRK07411 250 PERPVIE----------KLIDYEQFCGIPqAKAAEAAQKAEIPEMTVTELKALLDSgADDFVLIDVRNPNEYEIARIPGS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 355 LNIPLANLETrlNELTSALKEKGNGHantesctnpSVFVVCRRGNDSQRAVQYLRESGFdSAKDIIGGLEAWAANVNPNF 434
Cdd:PRK07411 320 VLVPLPDIEN--GPGVEKVKELLNGH---------RLIAHCKMGGRSAKALGILKEAGI-EGTNVKGGITAWSREVDPSV 387


                 ...
gi 332009204 435 PTY 437
Cdd:PRK07411 388 PQY 390
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 55-437 1.04e-83

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 261.95  E-value: 1.04e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  55 LTAPELEhgLSPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQ 107
Cdd:PRK07878   8 LVEPAAE--LTRDEVARYSRHLIIPDVGVDgqkrlknarvlvigagglgsptllylaAAGVGTLGIVEFDVVDESNLQRQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 108 IIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAA 187
Cdd:PRK07878  86 VIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 188 LGMEGQLTVY---NHNG-GPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDAL 263
Cdd:PRK07878 166 YRFEGQASVFwedAPDGlGLNYRDLYPEPPPPGMVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLGRLMVYDAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 264 SARMRIVKIRGRSSQCTVCgdnssfnkqtfKDFDYEDFTQfpLFAGPLNLLPAESRISSKEFKEILQKKEQHVLLDVRPS 343
Cdd:PRK07878 246 EMTYRTIKIRKDPSTPKIT-----------ELIDYEAFCG--VVSDEAQQAAAGSTITPRELKEWLDSGKKIALIDVREP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 344 HHYKIVSLPDSLNIPLANLETrlneltsalkekgnGHANTESCTNPSVFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGL 423
Cdd:PRK07878 313 VEWDIVHIPGAQLIPKSEILS--------------GEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQGGV 378

                        410
                 ....*....|....
gi 332009204 424 EAWAANVNPNFPTY 437
Cdd:PRK07878 379 VAWAKQVDPSLPMY 392
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-281 2.46e-83

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: 255.64  E-value: 2.46e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   72 YSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 124
Cdd:pfam00899   1 YSRQLALPLIGEDgqeklrnsrvlivgagglgseaakylaRAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  125 AACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPC 204
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332009204  205 YRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEP-LSERMLLFDALSARMRIVKIRGRSSQCTV 281
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnLAGRLLQFDALTMTFRELRLALKNPNCPV 238
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 64-279 4.28e-78

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 242.44  E-value: 4.28e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  64 LSPDQIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 116
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDgqeklkaarvlvvglgglgcaasqylaAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 117 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 197 YN-HNGGPCYRCLFPTPPPTSACqrCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgR 275
Cdd:PRK05690 165 FTyQDDEPCYRCLSRLFGENALT--CVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK-R 241


                 ....
gi 332009204 276 SSQC 279
Cdd:PRK05690 242 DPGC 245
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 68-428 2.01e-67

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 218.97  E-value: 2.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  68 QIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKV 120
Cdd:PRK05597   5 DIARYRRQIMLGEIGQQgqqslfdakvavigagglgspallylaGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 121 KSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHN 200
Cdd:PRK05597  85 ESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 201 GGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRGRSSqct 280
Cdd:PRK05597 165 HGPIYEDLFPTPPPPGSVPSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLIGKLGYYDSLDGTWEYIPVVGNPA--- 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 281 vcgdnssfnkqtfkdfdyedfTQFPLFAGPLNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLA 360
Cdd:PRK05597 242 ---------------------VLERVRGSTPVHGISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLS 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332009204 361 NLEtrlneltsalkekgNGHANTESCTNPSVFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 428
Cdd:PRK05597 301 AIR--------------EGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWLD 354
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 71-245 4.83e-63

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: 202.20  E-value: 4.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   71 RYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 123
Cdd:TIGR02356   1 RYARQLLLPDIGEEgqqrllnshvliigagglgspaalylaGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  124 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYN-HNGG 202
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDpGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 332009204  203 PCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKL 245
Cdd:TIGR02356 161 PCLRCLFPDIADTGP--SCATAGVIGPVVGVIGSLQALEALKL 201
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 311-437 5.54e-57

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: 183.66  E-value: 5.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 311 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 390
Cdd:cd01526    1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 332009204 391 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 437
Cdd:cd01526   75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 122
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 61-414 2.32e-39

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 145.02  E-value: 2.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  61 EHGLSPD------QIYRYSRQLLLPSFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQ 107
Cdd:PRK05600   5 EHTLSPFmqlptsELRRTARQLALPGFGIEqqerlhnarvlvigagglgcpamqslaSAGVGTITLIDDDTVDVSNIHRQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 108 IIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAA 187
Cdd:PRK05600  85 ILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 188 LGMEGQLTVYN---HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALS 264
Cdd:PRK05600 165 LRFHGELAVFNsgpDHRGVGLRDLFPEQPSGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQPGTVLSYDALT 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 265 ARMRIVKIRGRSSQCTVCGDNSSFNKQTFKDFDYEDFTqfplfagplnlLPAESrisskefkeilqkkeqhVLLDVRPSH 344
Cdd:PRK05600 245 ATTRSFRVGADPARPLVTRLRPSYEAARTDTTSLIDAT-----------LNGSA-----------------TLLDVREPH 296

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 345 HYKIVSLPDSlnipLANLETRLNELTSalkEKGNGHANTESCTNpSVFVVCRRGNDSQRAVQYLRESGFD 414
Cdd:PRK05600 297 EVLLKDLPEG----GASLKLPLSAITD---DADILHALSPIDGD-NVVVYCASGIRSADFIEKYSHLGHE 358
PRK08328 PRK08328
hypothetical protein; Provisional
 64-272 9.00e-32

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 121.06  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  64 LSPDQIYRYSRQLLLpsFAVE---------------------------ACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 116
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEgqeklkkakvavvgvgglgspvayylaAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 117 -HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLT 195
Cdd:PRK08328  80 kNPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332009204 196 VYNHNGGPCYRCLFPTPPptsacQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 272
Cdd:PRK08328 160 TIVPGKTKRLREIFPKVK-----KKKGKFPILGATAGVIGSIQAMEVIKLITGYGEPLLNKLLIVDLANNVFEVVEL 231
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 71-353 1.54e-27

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 112.01  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  71 RYSRQLLLPSFA----------------------------VEAcGVGQLGIIDHDVVELNNMHRQIIHTEAFI--GHPKV 120
Cdd:PRK07688   4 RYSRQELFSPIGeegqqklrekhvliigagalgtanaemlVRA-GVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 121 KSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHN 200
Cdd:PRK07688  83 VAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 201 GGPCYRCLFPTPPptSACQRCSDSGVLGVVPGVIGCLQALETIKLasLVG--EPLSERMLLFD---ALSARMRIVKIrgR 275
Cdd:PRK07688 163 KTPCLRCLLQSIP--LGGATCDTAGIISPAVQIVASYQVTEALKL--LVGdyEALRDGLVSFDvwkNEYSCMNVQKL--K 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 276 SSQCTVCGDnssfnKQTFKDFDYEDFTQFPLFAG-------PlnllPAESRISSKEFKEILQK-----KEQHVLLDVRpS 343
Cdd:PRK07688 237 KDNCPSCGE-----KALYPYLNYENTTKTAVLCGrntvqirP----PHKEEYDLEELAELLRDrgldvNVNPYLLSFS-L 306

                        330
                 ....*....|
gi 332009204 344 HHYKIVSLPD 353
Cdd:PRK07688 307 EEKRLVLFKD 316
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 71-293 2.39e-25

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 105.97  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  71 RYSRQLL------------------------LPSFAVEA---CGVGQLGIIDHDVVELNNMHRQIIHTE--AFIGHPKVK 121
Cdd:PRK12475   4 RYSRQILfsgigeegqrkirekhvlivgagaLGAANAEAlvrAGIGKLTIADRDYVEWSNLQRQQLYTEedAKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 122 SAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 201
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 202 GPCYRCLFPTPPPTSACqrCSDSGVLGVVPGVIGCLQALETIKLasLVG--EPLSERMLLFDALSARMRIVKI-RGRSSQ 278
Cdd:PRK12475 164 TPCLRCLMEHVPVGGAT--CDTAGIIQPAVQIVVAYQVTEALKI--LVEdfEALRETFLSFDIWNNQNMSIKVnKQKKDT 239

                        250
                 ....*....|....*
gi 332009204 279 CTVCGDNSSFNKQTF 293
Cdd:PRK12475 240 CPSCGLTRTYPSLTF 254
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 87-196 2.82e-24

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: 97.72  E-value: 2.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPP 166
Cdd:cd01483   22 GVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFLDGVDLVIDAIDNIA 101

                         90       100       110
                 ....*....|....*....|....*....|
gi 332009204 167 SRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:cd01483  102 VRRALNRACKELGIPVIDAGGLGLGGDIQV 131
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 319-432 2.99e-22

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: 90.80  E-value: 2.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 319 RISSKEFKEILQKkEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCRRG 398
Cdd:COG0607    5 EISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELP---KDK-------------PIVVYCASG 67

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332009204 399 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVNP 432
Cdd:COG0607   68 GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLP 101
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 80-187 3.14e-21

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: 91.90  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  80 SFAVEA---CGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILS-QY 155
Cdd:cd00755   24 SWAAEAlarSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTPDNSEDLLGgDP 103

                         90       100       110
                 ....*....|....*....|....*....|....
gi 332009204 156 DIIVDATDNPPSRYMISDCCVLLGKPLVS--GAA 187
Cdd:cd00755  104 DFVVDAIDSIRAKVALIAYCRKRKIPVISsmGAG 137
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 80-187 6.36e-20

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: 88.60  E-value: 6.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  80 SFAVEA---CGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQ-Y 155
Cdd:COG1179   37 SWAAEAlarSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELLSEdY 116

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 332009204 156 DIIVDATDN-PPSRYMISdCCVLLGKPLVS--GAA 187
Cdd:COG1179  117 DYVIDAIDSvSAKAALIA-WCRRRGIPIISsmGAG 150
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 331-432 2.24e-19

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: 82.89  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204   331 KKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANteSCTNPSVFVVCRRGNDSQRAVQYLRE 410
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLG--LDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 332009204   411 SGFDSAKDIIGGLEAWAANVNP 432
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
86-192 1.29e-16

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 78.36  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  86 CGVGQLGIIDHDVVELNNMHRQ---IIHteafIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDAT 162
Cdd:PRK08644  50 SGVGNLKLVDFDVVEPSNLNRQqyfISQ----IGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAF 125

                         90       100       110
                 ....*....|....*....|....*....|.
gi 332009204 163 DNPPSRYMISDCCV-LLGKPLVsgAALGMEG 192
Cdd:PRK08644 126 DNAETKAMLVETVLeHPGKKLV--AASGMAG 154
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 320-431 6.33e-16

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: 73.20  E-value: 6.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 320 ISSKEFKEILQK-KEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKgnghantesctnpSVFVVCRRG 398
Cdd:cd01528    2 ISVAELAEWLADeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPDK-------------DIVVLCHHG 68

                         90       100       110
                 ....*....|....*....|....*....|...
gi 332009204 399 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVN 431
Cdd:cd01528   69 GRSMQVAQWLLRQGFENVYNLQGGIDAWSLEVD 101
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 324-427 9.94e-16

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: 71.95  E-value: 9.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 324 EFKEiLQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELtsalkekgNGHANTEsctnpsVFVVCRRGNDSQR 403
Cdd:cd00158    1 ELKE-LLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALL--------ELDKDKP------IVVYCRSGNRSAR 65

                         90       100
                 ....*....|....*....|....
gi 332009204 404 AVQYLRESGFDSAKDIIGGLEAWA 427
Cdd:cd00158   66 AAKLLRKAGGTNVYNLEGGMLAWK 89
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 87-192 7.95e-15

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: 72.03  E-value: 7.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAfIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPP 166
Cdd:cd01487   22 GVGNLKLVDFDVVEPSNLNRQQYFLSQ-IGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGDCDIVVEAFDNAE 100

                         90       100
                 ....*....|....*....|....*..
gi 332009204 167 SRYMISDCCV-LLGKPLVSGAalGMEG 192
Cdd:cd01487  101 TKAMLAESLLgNKNKPVVCAS--GMAG 125
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 87-218 1.17e-14

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: 73.00  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSN--ALEILSQYDIIVDATDN 164
Cdd:cd01484   22 GFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQdfNDTFFEQFHIIVNALDN 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332009204 165 PPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPCYRC-LFPTPPPTSAC 218
Cdd:cd01484  102 IIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECtLYPPQKNFPMC 156
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 87-216 8.46e-14

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: 71.64  E-value: 8.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALR-TSNALEILSQYDIIVDATDNP 165
Cdd:cd01489   22 GFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKdPDFNVEFFKQFDLVFNALDNL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332009204 166 PSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPCYRCLfPTPPPTS 216
Cdd:cd01489  102 AARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQ-PKETPKT 151
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 330-427 3.68e-12

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: 62.12  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  330 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANTEsctnpsVFVVCRRGNDSQRAVQYLR 409
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP------IVVYCNSGNRAAAAAALLK 74

                          90
                  ....*....|....*...
gi 332009204  410 ESGFDSAKDIIGGLEAWA 427
Cdd:pfam00581  75 ALGYKNVYVLDGGFEAWK 92
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 77-197 1.37e-10

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: 62.69  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  77 LLPSFA---VEACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEAL--RTSNAL-- 149
Cdd:cd01490   14 LLKNFAlmgVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpETEHIFnd 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 332009204 150 EILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 197
Cdd:cd01490   94 EFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVV 141
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 319-428 1.67e-10

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 57.66  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 319 RISSKEFKEILQKKEQHVLLDVRPSHHY--KIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCR 396
Cdd:cd01444    1 RISVDELAELLAAGEAPVLLDVRDPASYaaLPDHIPGAIHLDEDSLDDWLGDLD---RDR-------------PVVVYCY 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 332009204 397 RGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 428
Cdd:cd01444   65 HGNSSAQLAQALREAGFTDVRSLAGGFEAWRR 96
PRK08223 PRK08223
hypothetical protein; Validated
 87-201 1.80e-10

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 61.62  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATD--N 164
Cdd:PRK08223  50 GIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDffE 129

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332009204 165 PPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 201
Cdd:PRK08223 130 FDARRLVFAACQQRGIPALTAAPLGMGTALLVFDPGG 166
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 77-196 5.78e-10

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: 61.44  E-value: 5.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204    77 LLPSFAVEACGVGQLGII---DHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEAL--RTSNAL-- 149
Cdd:TIGR01408  434 MLKNFALMGVGTGKKGMItvtDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpETETIFnd 513

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 332009204   150 EILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 196
Cdd:TIGR01408  514 EFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNTQV 560
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 87-214 2.02e-09

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: 58.52  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNaLEILSQYDIIVDATDN-P 165
Cdd:cd01488   22 GFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKD-EEFYRQFNIIICGLDSiE 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332009204 166 PSRYMISDCCVLLG-------KPLVSGAALGMEGQLTVYNHNGGPCYRCLFPTPPP 214
Cdd:cd01488  101 ARRWINGTLVSLLLyedpesiIPLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 330-426 9.34e-07

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 46.49  E-value: 9.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 330 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKGnghantesctnpsVFVVCRRGNDSQRAVQYLR 409
Cdd:cd01524    9 YRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELP---KDKE-------------IIVYCAVGLRGYIAARILT 72

                         90
                 ....*....|....*..
gi 332009204 410 ESGFDsAKDIIGGLEAW 426
Cdd:cd01524   73 QNGFK-VKNLDGGYKTY 88
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
336-432 2.42e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.24  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 336 VLLDVRPSHHYKIVSLPDSLNIPLANLETRLNEltsALKEKGNghantesctnpSVFVVCRRGNDSQRAVQYLRESGFDS 415
Cdd:PRK08762  19 VLIDVREAHERASGQAEGALRIPRGFLELRIET---HLPDRDR-----------EIVLICASGTRSAHAAATLRELGYTR 84

                         90
                 ....*....|....*..
gi 332009204 416 AKDIIGGLEAWAANVNP 432
Cdd:PRK08762  85 VASVAGGFSAWKDAGLP 101
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
391-428 2.93e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.78  E-value: 2.93e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 332009204 391 VFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 428
Cdd:PRK00162  61 VMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAWRR 98
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 80-174 1.24e-05

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 46.72  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  80 SFAVEA---CGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKV---DEYVEAlrtSNALEILS 153
Cdd:PRK15116  43 SWAAEAlarTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVtvvDDFITP---DNVAEYMS 119

                         90       100
                 ....*....|....*....|...
gi 332009204 154 Q-YDIIVDATDN-PPSRYMISDC 174
Cdd:PRK15116 120 AgFSYVIDAIDSvRPKAALIAYC 142
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 336-428 9.30e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 41.49  E-value: 9.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 336 VLLDVRPSHHYKIVSLPDSLNIPLANLETRLNeLTSALKEKGNGHANTESCTNpsVFVVCRRGNDSQRAVQYLRESGFDS 415
Cdd:cd01519   17 VLIDVREPEELKTGKIPGAINIPLSSLPDALA-LSEEEFEKKYGFPKPSKDKE--LIFYCKAGVRSKAAAELARSLGYEN 93

                         90
                 ....*....|...
gi 332009204 416 AKDIIGGLEAWAA 428
Cdd:cd01519   94 VGNYPGSWLDWAA 106
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 85-232 3.54e-04

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: 42.36  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  85 ACGVGQLGIIDHDVVELNNMHRQIIHT--EAFIGHPKVKSAAAACRSINSTIKVD----------------EYVEALRTS 146
Cdd:cd01486   20 GWGVRHITFVDSGKVSYSNPVRQSLFTfeDCKGGKPKAEAAAERLKEIFPSIDATgivlsipmpghpisesEVPSTLKDV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 147 NALEIL-SQYDIIVDATDNPPSRYMISDCCVLLGKpLVSGAALGMEGQLTVYNHNGGPCYRCLFP-----TPPPTSACQR 220
Cdd:cd01486  100 KRLEELiKDHDVIFLLTDSRESRWLPTLLSAAKNK-LVINAALGFDSYLVMRHGAGPQSQSGSGDsssdsIPGSRLGCYF 178

                        170
                 ....*....|..
gi 332009204 221 CSDSgvlgVVPG 232
Cdd:cd01486  179 CNDV----VAPG 186
PRK14851 PRK14851
hypothetical protein; Provisional
 87-201 1.36e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 41.00  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204  87 GVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATD--N 164
Cdd:PRK14851  66 GIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDffQ 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 332009204 165 PPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 201
Cdd:PRK14851 146 FEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFTPQG 182
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 319-369 2.31e-03

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 37.44  E-value: 2.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332009204 319 RISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNEL 369
Cdd:cd01533   11 SVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGEL 61
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 320-424 4.45e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 36.92  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332009204 320 ISSKEFKEILQKKEQHVLLDVRP-SHHYKIVSLPDSLNIPLANLET--RLNELTSALKEKGNGHAntesctnpSVFVVCR 396
Cdd:cd01522    1 LTPAEAWALLQADPQAVLVDVRTeAEWKFVGGVPDAVHVAWQVYPDmeINPNFLAELEEKVGKDR--------PVLLLCR 72

                         90       100
                 ....*....|....*....|....*...
gi 332009204 397 RGNDSQRAVQYLRESGFDSAKDIIGGLE 424
Cdd:cd01522   73 SGNRSIAAAEAAAQAGFTNVYNVLEGFE 100
 
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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