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Conserved domains on  [gi|7657339|ref|NP_055299|]
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adenylyltransferase and sulfurtransferase MOCS3 [Homo sapiens]

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 ...
 62-285 2.84e-112

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: 329.82  E-value: 2.84e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  142 AASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7657339  222 CYRCIFPQPPPAEtVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHF 285
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSF 223
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-460 8.86e-58

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: 186.36  E-value: 8.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  327 LQLLSPEERVSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLkeaiweeKQGTQEGAAV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQ-------ELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 7657339  407 PIYVICKLGNDSQKAVKILQSLSAaqeldPLTVRDVVGGLMAWAAKIDGTFPQY 460
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 ...
 62-285 2.84e-112

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: 329.82  E-value: 2.84e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  142 AASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7657339  222 CYRCIFPQPPPAEtVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHF 285
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSF 223
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
55-460 6.66e-108

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 324.77  E-value: 6.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    55 LSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAG 134
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   135 QAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITV 214
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   215 YHYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSRR 294
Cdd:PRK07411 171 FNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKFRELKLRPNP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   295 ldcaacgERPTVTDLLDYEAFCGSSATDKCRSLQLLSPEErVSVTDYKRLLDSGAF-HLLLDVRPQVEVDICRLPHALHI 373
Cdd:PRK07411 251 -------ERPVIEKLIDYEQFCGIPQAKAAEAAQKAEIPE-MTVTELKALLDSGADdFVLIDVRNPNEYEIARIPGSVLV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   374 PLKHLERRDAeslkllKEAIWEEKQGTQegaavpIYVICKLGNDSQKAVKILQSLSaaqeldpLTVRDVVGGLMAWAAKI 453
Cdd:PRK07411 323 PLPDIENGPG------VEKVKELLNGHR------LIAHCKMGGRSAKALGILKEAG-------IEGTNVKGGITAWSREV 383


                 ....*..
gi 7657339   454 DGTFPQY 460
Cdd:PRK07411 384 DPSVPQY 390
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 56-302 1.59e-107

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: 318.61  E-value: 1.59e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   56 SRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQ 135
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  136 AKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVY 215
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  216 HYDGGPCYRCIFPQPPPAEtvTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFrSIRLRSRRL 295
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPG--PSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEF-RTIKLPRDP 237


                ....*..
gi 7657339  296 DCAACGE 302
Cdd:COG0476 238 DCPVCGE 244
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 63-297 2.24e-86

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: 264.12  E-value: 2.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     63 YSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAA 142
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    143 ASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPC 222
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657339    223 YRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLG-PSYSGSLLLFDALRGHFRSIRLRSRRLDC 297
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGePNLAGRLLQFDALTMTFRELRLALKNPNC 236
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 62-262 5.09e-72

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


Pssm-ID: 274094  Cd Length: 202  Bit Score: 226.09  E-value: 5.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSA 141
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    142 AASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDG-G 220
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGeG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 7657339    221 PCYRCIFPQPPpaETVTNCADGGVLGVVTGVLGCLQALEVLK 262
Cdd:TIGR02356 161 PCLRCLFPDIA--DTGPSCATAGVIGPVVGVIGSLQALEALK 200
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-460 8.86e-58

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: 186.36  E-value: 8.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  327 LQLLSPEERVSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLkeaiweeKQGTQEGAAV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQ-------ELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 7657339  407 PIYVICKLGNDSQKAVKILQSLSAaqeldPLTVRDVVGGLMAWAAKIDGTFPQY 460
Cdd:cd01526  74 PIYVVCRRGNDSQTAVRKLKELGL-----ERFVRDIIGGLKAWADKVDPTFPLY 122
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 351-454 8.39e-15

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: 69.80  E-value: 8.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     351 HLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEAIWEEKQGTQEgaaVPIYVICKLGNDSQKAVKILqslsa 430
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKD---KPVVVYCRSGNRSAKAAWLL----- 76

                           90       100
                   ....*....|....*....|....
gi 7657339     431 aQELDPLTVRDVVGGLMAWAAKID 454
Cdd:smart00450  77 -RELGFKNVYLLDGGYKEWSAAGP 99
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 334-454 9.08e-14

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: 67.30  E-value: 9.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  334 ERVSVTDYKRLLDSGAFhLLLDVRPQVEVDICRLPHALHIPLKHLERRDAEslkLLKEAiweekqgtqegaavPIYVICK 413
Cdd:COG0607   4 KEISPAELAELLESEDA-VLLDVREPEEFAAGHIPGAINIPLGELAERLDE---LPKDK--------------PIVVYCA 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7657339  414 LGNDSQKAVKILQSLSAAQeldpltVRDVVGGLMAWAAKID 454
Cdd:COG0607  66 SGGRSAQAAALLRRAGYTN------VYNLAGGIEAWKAAGL 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 352-450 1.14e-10

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: 57.88  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    352 LLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEaiWEEKQGTQegaavPIYVICKLGNDSQKAVKILQSLSAA 431
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEK--LLELLKDK-----PIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|....*....
gi 7657339    432 QeldpltVRDVVGGLMAWA 450
Cdd:pfam00581  80 N------VYVLDGGFEAWK 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
335-451 5.25e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 48.47  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   335 RVSVTDYKRLLDSGAfhLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKllkeaiweekqgtqeGAAVPIYVICKL 414
Cdd:PRK08762   4 EISPAEARARAAQGA--VLIDVREAHERASGQAEGALRIPRGFLELRIETHLP---------------DRDREIVLICAS 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 7657339   415 GNDSQKAVKILQSLSAAQeldpltVRDVVGGLMAWAA 451
Cdd:PRK08762  67 GTRSAHAAATLRELGYTR------VASVAGGFSAWKD 97
 
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 ...
 62-285 2.84e-112

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: 329.82  E-value: 2.84e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSA 141
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  142 AASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGP 221
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7657339  222 CYRCIFPQPPPAEtVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHF 285
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSF 223
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
55-460 6.66e-108

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 324.77  E-value: 6.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    55 LSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAG 134
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   135 QAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITV 214
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   215 YHYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSRR 294
Cdd:PRK07411 171 FNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKFRELKLRPNP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   295 ldcaacgERPTVTDLLDYEAFCGSSATDKCRSLQLLSPEErVSVTDYKRLLDSGAF-HLLLDVRPQVEVDICRLPHALHI 373
Cdd:PRK07411 251 -------ERPVIEKLIDYEQFCGIPQAKAAEAAQKAEIPE-MTVTELKALLDSGADdFVLIDVRNPNEYEIARIPGSVLV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   374 PLKHLERRDAeslkllKEAIWEEKQGTQegaavpIYVICKLGNDSQKAVKILQSLSaaqeldpLTVRDVVGGLMAWAAKI 453
Cdd:PRK07411 323 PLPDIENGPG------VEKVKELLNGHR------LIAHCKMGGRSAKALGILKEAG-------IEGTNVKGGITAWSREV 383


                 ....*..
gi 7657339   454 DGTFPQY 460
Cdd:PRK07411 384 DPSVPQY 390
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 56-302 1.59e-107

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: 318.61  E-value: 1.59e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   56 SRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQ 135
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  136 AKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVY 215
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  216 HYDGGPCYRCIFPQPPPAEtvTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFrSIRLRSRRL 295
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPG--PSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEF-RTIKLPRDP 237


                ....*..
gi 7657339  296 DCAACGE 302
Cdd:COG0476 238 DCPVCGE 244
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 47-460 2.08e-98

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 300.47  E-value: 2.08e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    47 SPLPP----KAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNL 122
Cdd:PRK07878   3 TSLPPlvepAAELTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   123 ARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVS 202
Cdd:PRK07878  83 QRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   203 ASALRFEGQITVYHYDG----GPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLF 278
Cdd:PRK07878 163 GSIYRFEGQASVFWEDApdglGLNYRDLYPEPPPPGMVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLGRLMVY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   279 DALRGHFRSIRLRSRRldcaacgERPTVTDLLDYEAFCGSSATDKcrslQLLSPEERVSVTDYKRLLDSGAFHLLLDVRP 358
Cdd:PRK07878 243 DALEMTYRTIKIRKDP-------STPKITELIDYEAFCGVVSDEA----QQAAAGSTITPRELKEWLDSGKKIALIDVRE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   359 QVEVDICRLPHALHIPlkhlerrdaESLKLLKEAIWEEKQGTqegaavPIYVICKLGNDSQKAvkiLQSLSAAQELDPLT 438
Cdd:PRK07878 312 PVEWDIVHIPGAQLIP---------KSEILSGEALAKLPQDR------TIVLYCKTGVRSAEA---LAALKKAGFSDAVH 373

                        410       420
                 ....*....|....*....|..
gi 7657339   439 VRdvvGGLMAWAAKIDGTFPQY 460
Cdd:PRK07878 374 LQ---GGVVAWAKQVDPSLPMY 392
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
48-320 1.62e-96

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 295.38  E-value: 1.62e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    48 PLPPKAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVL 127
Cdd:PRK08762 101 PLERPRLLTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   128 HGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALR 207
Cdd:PRK08762 181 HTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   208 FEGQITVY----HYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRG 283
Cdd:PRK08762 261 FEGQVSVFdagrQRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAM 340

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 7657339   284 HFrSIRLRSRRLDCAACGERPTVTDLLDYEAFCGSSA 320
Cdd:PRK08762 341 RF-RELRLPPDPHCPVCAPGRPFPGYIDYAAFCAGAA 376
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 55-285 5.15e-89

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 271.33  E-value: 5.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    55 LSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAG 134
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   135 QAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITV 214
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657339   215 YHY-DGGPCYRCIFPQPPPAEtvTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHF 285
Cdd:PRK05690 165 FTYqDDEPCYRCLSRLFGENA--LTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQF 234
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 63-297 2.24e-86

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: 264.12  E-value: 2.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     63 YSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAA 142
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    143 ASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPC 222
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657339    223 YRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLG-PSYSGSLLLFDALRGHFRSIRLRSRRLDC 297
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGePNLAGRLLQFDALTMTFRELRLALKNPNC 236
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 62-262 5.09e-72

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


Pssm-ID: 274094  Cd Length: 202  Bit Score: 226.09  E-value: 5.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSA 141
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    142 AASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDG-G 220
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGeG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 7657339    221 PCYRCIFPQPPpaETVTNCADGGVLGVVTGVLGCLQALEVLK 262
Cdd:TIGR02356 161 PCLRCLFPDIA--DTGPSCATAGVIGPVVGVIGSLQALEALK 200
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 56-451 2.69e-59

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 198.17  E-value: 2.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    56 SRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQ 135
Cdd:PRK05597   2 KNLDIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   136 AKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVY 215
Cdd:PRK05597  82 PKAESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   216 HYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSrrl 295
Cdd:PRK05597 162 HAGHGPIYEDLFPTPPPPGSVPSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLIGKLGYYDSLDGTWEYIPVVG--- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   296 dcaacgeRPTVTDLLDYEAfcgssatdkCRSLQLLSPEERVSVTDYKRLLDSGAfhlLLDVRPQVEVDICRLPHALHIPL 375
Cdd:PRK05597 239 -------NPAVLERVRGST---------PVHGISGGFGEVLDVPRVSALPDGVT---LIDVREPSEFAAYSIPGAHNVPL 299

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657339   376 khlerrdaeslkllkEAIWEEKQGTQEGAAVPIYVICKLGNDSQKAVKILQSLSaaqeldpltVRDVV---GGLMAWAA 451
Cdd:PRK05597 300 ---------------SAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAG---------YTGMSsldGGIEGWLD 354
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 327-460 8.86e-58

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: 186.36  E-value: 8.86e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  327 LQLLSPEERVSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLkeaiweeKQGTQEGAAV 406
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQ-------ELPLDNDKDS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 7657339  407 PIYVICKLGNDSQKAVKILQSLSAaqeldPLTVRDVVGGLMAWAAKIDGTFPQY 460
Cdd:cd01526  74 PIYVVCRRGNDSQTAVRKLKELGL-----ERFVRDIIGGLKAWADKVDPTFPLY 122
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 45-281 3.36e-51

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 177.38  E-value: 3.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    45 PVSPLPPKAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLAR 124
Cdd:PRK05600   4 SEHTLSPFMQLPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   125 QVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSAS 204
Cdd:PRK05600  84 QILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   205 ALRFEGQITVYH---YDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDAL 281
Cdd:PRK05600 164 VLRFHGELAVFNsgpDHRGVGLRDLFPEQPSGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQPGTVLSYDAL 243
PRK08328 PRK08328
hypothetical protein; Provisional
 55-279 1.78e-37

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 136.85  E-value: 1.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    55 LSRDEILRYSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEA-LA 133
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEdLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   134 GQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQIT 213
Cdd:PRK08328  80 KNPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657339   214 VYHYDGGPCYRCIFPQPPPAEtvtncADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFD 279
Cdd:PRK08328 160 TIVPGKTKRLREIFPKVKKKK-----GKFPILGATAGVIGSIQAMEVIKLITGYGEPLLNKLLIVD 220
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 62-305 3.93e-36

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 136.28  E-value: 3.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQA--KAF 139
Cdd:PRK07688   4 RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNNlpKAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   140 SAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDG 219
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   220 GPCYRCIFPQ-PPPAETvtnCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGH-FRSIRLRSRRLDC 297
Cdd:PRK07688 164 TPCLRCLLQSiPLGGAT---CDTAGIISPAVQIVASYQVTEALKLLVGDYEALRDGLVSFDVWKNEySCMNVQKLKKDNC 240


                 ....*...
gi 7657339   298 AACGERPT 305
Cdd:PRK07688 241 PSCGEKAL 248
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 84-214 2.30e-34

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: 125.46  E-value: 2.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   84 CVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTP 163
Cdd:cd01483   1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7657339  164 ATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITV 214
Cdd:cd01483  81 DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQV 131
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 62-375 1.57e-32

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 126.38  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    62 RYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQ--AKAF 139
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   140 SAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDG 219
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   220 GPCYRCIFPQpPPAETVTnCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRG-HFRSIRLRSRRLDCA 298
Cdd:PRK12475 164 TPCLRCLMEH-VPVGGAT-CDTAGIIQPAVQIVVAYQVTEALKILVEDFEALRETFLSFDIWNNqNMSIKVNKQKKDTCP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   299 ACGERPTVTDL-----LDYEAFCGSSaTDKCRS--LQLLSPEERVsvtdyKRLldsgafhllldvrpQVEVDICRLPHAL 371
Cdd:PRK12475 242 SCGLTRTYPSLtfenqTKTEVLCGRN-TVQIRPgvRRRLNLEEIK-----KRL--------------QKIGKVDANPYLL 301


                 ....
gi 7657339   372 HIPL 375
Cdd:PRK12475 302 SFQL 305
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
79-206 3.01e-22

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 94.54  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    79 RLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALaGQAKAFSAAASLRRLNSAVECVPYT 158
Cdd:PRK08644  25 KLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQI-GMPKVEALKENLLEINPFVEIEAHN 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 7657339   159 QALTPATALDLVRRYDVVADCSDNVPT-RYLVNDACVLAGRPLVSASAL 206
Cdd:PRK08644 104 EKIDEDNIEELFKDCDIVVEAFDNAETkAMLVETVLEHPGKKLVAASGM 152
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 85-232 3.47e-22

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: 96.68  E-value: 3.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALT-P 163
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKdP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  164 ATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVyHYDG-GPCYRCIfPQPPP 232
Cdd:cd01489  82 DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQV-IKKGkTECYECQ-PKETP 149
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 72-203 4.29e-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: 86.29  E-value: 4.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   72 LGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQvLHgeALA---GQAKAFSAAASLRRL 148
Cdd:COG1179  14 YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQ-LH--ALDstvGRPKVEVMAERIRDI 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657339  149 NSAVECVPYTQALTPATALDLV-RRYDVVADCSDNVPTRYLVNDACVLAGRPLVSA 203
Cdd:COG1179  91 NPDCEVTAIDEFVTPENADELLsEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISS 146
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 72-203 5.59e-18

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: 82.65  E-value: 5.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   72 LGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSA 151
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 7657339  152 VECVPYTQALTPATALDLVRR-YDVVADCSDNVPTRYLVNDACVLAGRPLVSA 203
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGdPDFVVDAIDSIRAKVALIAYCRKRKIPVISS 133
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 85-206 5.99e-18

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: 81.27  E-value: 5.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALaGQAKAFSAAASLRRLNSAVECVPYTQALTPA 164
Cdd:cd01487   2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQI-GEPKVEALKENLREINPFVKIEAINIKIDEN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7657339  165 TALDLVRRYDVVADCSDNVPT-RYLVNDACVLAGRPLVSASAL 206
Cdd:cd01487  81 NLEGLFGDCDIVVEAFDNAETkAMLAESLLGNKNKPVVCASGM 123
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 85-239 1.49e-17

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: 81.47  E-value: 1.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPA 164
Cdd:cd01484   2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657339  165 T--ALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPCYRCifPQPPPAETVTNC 239
Cdd:cd01484  82 QdfNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIEC--TLYPPQKNFPMC 156
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 85-215 1.04e-15

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: 78.87  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGV-----GRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQ 159
Cdd:cd01490   2 VFLVGAGAIGCELLKNFALMGVgtgesGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  160 ALTPATAL----DLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVY 215
Cdd:cd01490  82 RVGPETEHifndEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVV 141
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 351-454 8.39e-15

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: 69.80  E-value: 8.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     351 HLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEAIWEEKQGTQEgaaVPIYVICKLGNDSQKAVKILqslsa 430
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKD---KPVVVYCRSGNRSAKAAWLL----- 76

                           90       100
                   ....*....|....*....|....
gi 7657339     431 aQELDPLTVRDVVGGLMAWAAKID 454
Cdd:smart00450  77 -RELGFKNVYLLDGGYKEWSAAGP 99
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 58-206 5.49e-14

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: 70.67  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     58 DEILRYSRQLVLPElgVHGQLRLGTacVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALaGQAK 137
Cdd:TIGR02354   1 EEFRRALVARHTPK--IVQKLEQAT--VAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQV-GEPK 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657339    138 AFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDAcVLAGRP---LVSASAL 206
Cdd:TIGR02354  76 TEALKENISEINPYTEIEAYDEKITEENIDKFFKDADIVCEAFDNAEAKAMLVNA-VLEKYKdkyLIAASGL 146
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 334-454 9.08e-14

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: 67.30  E-value: 9.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  334 ERVSVTDYKRLLDSGAFhLLLDVRPQVEVDICRLPHALHIPLKHLERRDAEslkLLKEAiweekqgtqegaavPIYVICK 413
Cdd:COG0607   4 KEISPAELAELLESEDA-VLLDVREPEEFAAGHIPGAINIPLGELAERLDE---LPKDK--------------PIVVYCA 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7657339  414 LGNDSQKAVKILQSLSAAQeldpltVRDVVGGLMAWAAKID 454
Cdd:COG0607  66 SGGRSAQAAALLRRAGYTN------VYNLAGGIEAWKAAGL 100
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 62-216 1.10e-13

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: 73.38  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339      62 RYSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGV-----GRLGLVDYDVVEMSNLARQVLHGEALAGQA 136
Cdd:TIGR01408  401 RYDAQIAV--FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKP 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     137 KAFSAAASLRRLNSAVECVPYTQALTPATAL----DLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEG-- 210
Cdd:TIGR01408  479 KSYTAADATLKINPQIKIDAHQNRVGPETETifndEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGnt 558


                   ....*.
gi 7657339     211 QITVYH 216
Cdd:TIGR01408  559 QVVVPH 564
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 85-239 1.55e-13

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: 70.85  E-value: 1.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPA 164
Cdd:cd01488   2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  165 TaLDLVRRYDVVADCSDNVPTRYLVN------------DACVlagrPLVSASALRFEGQITVYHYDGGPCYRCIFPQPPP 232
Cdd:cd01488  82 D-EEFYRQFNIIICGLDSIEARRWINgtlvslllyedpESII----PLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156


                ....*..
gi 7657339  233 AETVTNC 239
Cdd:cd01488 157 QVTFPLC 163
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 63-225 3.48e-12

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: 66.91  E-value: 3.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   63 YSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAA 142
Cdd:cd01491   2 YSRQLYV--LGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  143 ASLRRLNSAVECVPYTQALTpataLDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVyhyDGGPC 222
Cdd:cd01491  80 ARLAELNPYVPVTVSTGPLT----TDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFC---DFGDE 152


                ...
gi 7657339  223 YRC 225
Cdd:cd01491 153 FTV 155
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 340-450 3.94e-12

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: 61.93  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  340 DYKRLLDSGAFhLLLDVRPQVEVDICRLPHALHIPLKHLERRDAEsLKLLKEAiweekqgtqegaavPIYVICKLGNDSQ 419
Cdd:cd00158   1 ELKELLDDEDA-VLLDVREPEEYAAGHIPGAINIPLSELEERAAL-LELDKDK--------------PIVVYCRSGNRSA 64

                        90       100       110
                ....*....|....*....|....*....|.
gi 7657339  420 KAVKILQSLSAAQeldpltVRDVVGGLMAWA 450
Cdd:cd00158  65 RAAKLLRKAGGTN------VYNLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 352-450 1.14e-10

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: 57.88  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    352 LLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEaiWEEKQGTQegaavPIYVICKLGNDSQKAVKILQSLSAA 431
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEK--LLELLKDK-----PIVVYCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|....*....
gi 7657339    432 QeldpltVRDVVGGLMAWA 450
Cdd:pfam00581  80 N------VYVLDGGFEAWK 92
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 63-204 1.39e-10

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: 60.38  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   63 YSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAA 142
Cdd:cd01492   4 YDRQIRL--WGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657339  143 ASLRRLNSAVECVPYTQALTPATAlDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSAS 204
Cdd:cd01492  82 ERLRALNPRVKVSVDTDDISEKPE-EFFSQFDVVVATELSRAELVKINELCRKLGVKFYATG 142
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 336-454 3.50e-09

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: 53.94  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  336 VSVTDYKRLLDSGAFH-LLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEaiweekqgtqegaaVPIYVICKL 414
Cdd:cd01528   2 ISVAELAEWLADEREEpVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPD--------------KDIVVLCHH 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7657339  415 GNDSQKAVKILQSlsaaQELDplTVRDVVGGLMAWAAKID 454
Cdd:cd01528  68 GGRSMQVAQWLLR----QGFE--NVYNLQGGIDAWSLEVD 101
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 56-219 4.35e-09

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: 58.80  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339     56 SRDEILRYSRQLVLPELGVHgqlRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHG--EALA 133
Cdd:TIGR01381 315 SVDLNLKLMKWRLHPDLQLE---RYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNfeDCLL 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    134 GQA-KAFSAAASLRRLNSAVECVPYTQALT----PATALD-------------LVRRYDVVADCSDNVPTRYLVNDACVL 195
Cdd:TIGR01381 392 GGRgKAETAQKALKRIFPSIQATGHRLTVPmpghPIDEKDvpelekdiarleqLIKDHDVVFLLLDSREARWLPTVLCSR 471

                         170       180
                  ....*....|....*....|....
gi 7657339    196 AGRPLVSAsALRFEGQITVYHYDG 219
Cdd:TIGR01381 472 HKKIAISA-ALGFDSYVVMRHGIG 494
PRK08223 PRK08223
hypothetical protein; Validated
 77-219 1.94e-08

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 55.46  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    77 QLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVP 156
Cdd:PRK08223  22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657339   157 YTQALTPATALDLVRRYDVVADCSD--NVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDG 219
Cdd:PRK08223 102 FPEGIGKENADAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDPGG 166
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 85-153 2.02e-08

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: 55.46  E-value: 2.02e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7657339   85 VLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVL--HGEALAGQAKAFSAAASLRRLNSAVE 153
Cdd:cd01486   2 CLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLftFEDCKGGKPKAEAAAERLKEIFPSID 72
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 63-152 2.02e-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: 51.27  E-value: 2.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   63 YSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVL--HGEALAGQAKAFS 140
Cdd:cd01485   2 YDRQIRL--WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFldAEVSNSGMNRAAA 79

                        90
                ....*....|..
gi 7657339  141 AAASLRRLNSAV 152
Cdd:cd01485  80 SYEFLQELNPNV 91
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 58-193 3.16e-07

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: 52.97  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339      58 DEILrYSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAK 137
Cdd:TIGR01408    3 DEAL-YSRQLYV--LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNR 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657339     138 AFSAAASLRRLNSAvecVPYTQALTPATALDLvRRYDVVADCSDNVPTRYLVNDAC 193
Cdd:TIGR01408   80 AEAVVKKLAELNPY---VHVSSSSVPFNEEFL-DKFQCVVLTEMSLPLQKEINDFC 131
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 62-153 5.32e-07

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


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 51.54  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   62 RYSRQLVLpeLGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQ-VLHGEALaGQAKAFS 140
Cdd:cd01493   2 KYDRQLRL--WGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNfFLDASSL-GKSRAEA 78

                        90
                ....*....|...
gi 7657339  141 AAASLRRLNSAVE 153
Cdd:cd01493  79 TCELLQELNPDVN 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
335-451 5.25e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 48.47  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   335 RVSVTDYKRLLDSGAfhLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKllkeaiweekqgtqeGAAVPIYVICKL 414
Cdd:PRK08762   4 EISPAEARARAAQGA--VLIDVREAHERASGQAEGALRIPRGFLELRIETHLP---------------DRDREIVLICAS 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 7657339   415 GNDSQKAVKILQSLSAAQeldpltVRDVVGGLMAWAA 451
Cdd:PRK08762  67 GTRSAHAAATLRELGYTR------VASVAGGFSAWKD 97
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 83-183 1.10e-05

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 46.72  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    83 ACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALT 162
Cdd:PRK15116  31 AHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFIT 110

                         90       100
                 ....*....|....*....|..
gi 7657339   163 P-ATALDLVRRYDVVADCSDNV 183
Cdd:PRK15116 111 PdNVAEYMSAGFSYVIDAIDSV 132
PRK14852 PRK14852
hypothetical protein; Provisional
 61-234 1.00e-04

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 45.07  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    61 LRYSRQLVLPELGvhGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFS 140
Cdd:PRK14852 313 IAFSRNLGLVDYA--GQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDV 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339   141 AAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVP---TRYLVNDACVLaGRPLVSASALRFEGQITVYHY 217
Cdd:PRK14852 391 MTERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFAldiRRRLFNRALEL-GIPVITAGPLGYSCALLVFMP 469

                        170
                 ....*....|....*....
gi 7657339   218 DGG--PCYRCIFPQPPPAE 234
Cdd:PRK14852 470 GGMnfDSYFGIDDDTPPME 488
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 336-428 2.73e-04

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: 40.33  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339  336 VSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLErrdaESLKL----LKEAIWEEKQGTQEgaavPIYVI 411
Cdd:cd01519   1 YSFEEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSSLP----DALALseeeFEKKYGFPKPSKDK----ELIFY 72

                        90
                ....*....|....*..
gi 7657339  412 CKLGNDSQKAVKILQSL 428
Cdd:cd01519  73 CKAGVRSKAAAELARSL 89
PRK14851 PRK14851
hypothetical protein; Provisional
 77-219 9.74e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 38.30  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657339    77 QLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVP 156
Cdd:PRK14851  38 QERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITP 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657339   157 YTQALTpATALDL-VRRYDVVADCSDNVP---TRYLVNDACVLaGRPLVSASALRFEGQITVYHYDG 219
Cdd:PRK14851 118 FPAGIN-ADNMDAfLDGVDVVLDGLDFFQfeiRRTLFNMAREK-GIPVITAGPLGYSSAMLVFTPQG 182
 
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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