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Conserved domains on  [gi|657202705|ref|WP_029317165|]
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nucleoside triphosphate pyrophosphohydrolase [Bacillus subtilis]

Protein Classification

YabN family protein( domain architecture ID 11467694)

YabN family protein contains an N-terminal S-AdoMet-dependent tetrapyrrole methylase domain and a MazG family nucleoside triphosphate pyrophosphohydrolase domain, similar to Bacillus subtilis protein YabN

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 230-487 3.77e-141

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


:

Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 406.03  E-value: 3.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 230 YHEFSTFRSIIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTI 309
Cdd:COG3956    8 LYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFDF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 310 DDVIKGISEKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKN---TSESSLLDSVPKTLPALSKAAKLQKKAAKVGFDW 386
Cdd:COG3956   88 DDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAekgEGRKSVLDGVPRSLPALMRAYKLQKKAARVGFDW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 387 EDVSDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVE 466
Cdd:COG3956  168 PDVEGVLDKVEEELAELKEALASGDQEA-IEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                        250       260
                 ....*....|....*....|.
gi 657202705 467 LADMSLEDMDKLWNEAKETER 487
Cdd:COG3956  247 LEDLSLEEMDALWQEAKKAEK 267
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 5-223 6.08e-115

N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.


:

Pssm-ID: 381177  Cd Length: 218  Bit Score: 337.54  E-value: 6.08e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   5 ITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPLIEELEKETKNIRFFDDIYEKHDQFEAVYEEIADILFEAARRED 84
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKVYLRTARHPVVEELKEEGIEFESFDDLYEEAEDFEEVYEAIAERLLEAAEHGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  85 VVYAVPGHPFVAEKTVQLLTERQEkENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADELELRHHLIICQVYD 164
Cdd:cd11723   81 VVYAVPGHPLVAERTVQLLLERAE-EGIEVEIIPGVSFLDAALAALGIDPIEGLQILDALDLDAEDLDPRLPLLITQVYN 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657202705 165 QMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELDRNVALNNLTSVYIPPI 223
Cdd:cd11723  160 RLVASDVKLTLMEVYPDEHEVTVVRAAGLGDEKVEEVPLYELDRQEDIDHLTSLYVPPL 218
 
Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 230-487 3.77e-141

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 406.03  E-value: 3.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 230 YHEFSTFRSIIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTI 309
Cdd:COG3956    8 LYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFDF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 310 DDVIKGISEKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKN---TSESSLLDSVPKTLPALSKAAKLQKKAAKVGFDW 386
Cdd:COG3956   88 DDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAekgEGRKSVLDGVPRSLPALMRAYKLQKKAARVGFDW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 387 EDVSDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVE 466
Cdd:COG3956  168 PDVEGVLDKVEEELAELKEALASGDQEA-IEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                        250       260
                 ....*....|....*....|.
gi 657202705 467 LADMSLEDMDKLWNEAKETER 487
Cdd:COG3956  247 LEDLSLEEMDALWQEAKKAEK 267
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 239-483 3.33e-135

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 390.34  E-value: 3.33e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  239 IIRELRGP-NGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVIKGIS 317
Cdd:TIGR00444   1 IIAQLRDPeNGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  318 EKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKNTSES-SLLDSVPKTLPALSKAAKLQKKAAKVGFDWEDVSDIWEKV 396
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAQtSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  397 SEEMKEFSSEVSEAPHEHN-LKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVELADMSLEDM 475
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEQNkLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVDLEEM 240


                  ....*...
gi 657202705  476 DKLWNEAK 483
Cdd:TIGR00444 241 EELWQQVK 248
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 231-488 2.23e-121

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 355.63  E-value: 2.23e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 231 HEFSTFRSIIRELRGP-NGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTI 309
Cdd:PRK09562   7 EAIDRLLEIMARLRDPeGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAFDF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 310 DDVIKGISEKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKNtsESSLLDSVPKTLPALSKAAKLQKKAAKVGFDWEDV 389
Cdd:PRK09562  87 ADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERA--ESSVLDGIPRGLPALMRAYKIQKKAARVGFDWESL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 390 SDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVELAD 469
Cdd:PRK09562 165 EPVLDKVEEEIDELKEALAQGDQAK-IEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKTLED 243

                        250
                 ....*....|....*....
gi 657202705 470 MSLEDMDKLWNEAKETERR 488
Cdd:PRK09562 244 ASLEEMDALWQEAKRQEKA 262
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 5-223 6.08e-115

N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.


Pssm-ID: 381177  Cd Length: 218  Bit Score: 337.54  E-value: 6.08e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   5 ITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPLIEELEKETKNIRFFDDIYEKHDQFEAVYEEIADILFEAARRED 84
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKVYLRTARHPVVEELKEEGIEFESFDDLYEEAEDFEEVYEAIAERLLEAAEHGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  85 VVYAVPGHPFVAEKTVQLLTERQEkENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADELELRHHLIICQVYD 164
Cdd:cd11723   81 VVYAVPGHPLVAERTVQLLLERAE-EGIEVEIIPGVSFLDAALAALGIDPIEGLQILDALDLDAEDLDPRLPLLITQVYN 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657202705 165 QMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELDRNVALNNLTSVYIPPI 223
Cdd:cd11723  160 RLVASDVKLTLMEVYPDEHEVTVVRAAGLGDEKVEEVPLYELDRQEDIDHLTSLYVPPL 218
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 234-347 2.89e-64

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 203.51  E-value: 2.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 234 STFRSIIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVI 313
Cdd:cd11528    1 ERLVEIVARLRGPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDVI 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 657202705 314 KGISEKMVRRHPHVFKDVKVQDENDVLANWEDIK 347
Cdd:cd11528   81 DGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 255-328 1.17e-32

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 118.85  E-value: 1.17e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657202705  255 QTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVIKGISEKMVRRHPHVF 328
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 4-207 6.24e-26

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 105.12  E-value: 6.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705    4 KITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHP-LIEELEKEtkniRFFDDIYEKHDQFEAVYEEIADILFEAARR 82
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALeILLDLLPE----DLYFPMTEDKEPLEEAYEEIAEALAAALRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   83 -EDVVYAVPGHPFVAEkTVQLLTERQEKENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADELELRHHL---- 157
Cdd:pfam00590  77 gKDVARLVSGDPLVYG-TGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLeall 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657202705  158 ----IICQVYDQMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELD 207
Cdd:pfam00590 156 angdTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
3-200 3.18e-04

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 42.21  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   3 GKITVVGLGAGDMDQLTIGIHKLLTKADTLYV----RTKD---HPLIEE-LEKETKnirffddIYEKH-------DQFEA 67
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVVYApasrKGGGslaLNIVRPyLKEETE-------IVELHfpmskdeEEKEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  68 VYEEIADILFEAARR-EDVVYAVPGHPFVAEKTVQLLtERQEKENVQVK-VAGGQSF----------LDATFNALQIDPi 135
Cdd:PRK05576  75 VWKENAEEIAAEAEEgKNVAFITLGDPNLYSTFSHLL-EYLKCHDIEVEtVPGISSFtaiasragvpLAMGDESLAIIP- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657202705 136 egfqfVDAGTLSADELELRHHLIICQVYDqmtASEVKLTLMEKLPDDYevVIVTAAGSRGEEIRT 200
Cdd:PRK05576 153 -----ATREALIEQALTDFDSVVLMKVYK---NFALIEELLEEGYLDA--LYVRRAYMEGEQILR 207
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 1-95 8.62e-04

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 40.85  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   1 MAGKITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKD-------HPLIEELEKETKnIRFFDDIYEK-HDQFEAVYEEI 72
Cdd:COG2243    1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGagkaslaREIVAPYLPPAR-IVELVFPMTTdYEALVAAWDEA 79

                         90       100
                 ....*....|....*....|....
gi 657202705  73 ADILFEAARR-EDVVYAVPGHPFV 95
Cdd:COG2243   80 AARIAEELEAgRDVAFLTEGDPSL 103
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 5-125 4.73e-03

diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]


Pssm-ID: 273117  Cd Length: 257  Bit Score: 38.64  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705    5 ITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPL----IEELEketkniRFFDDIYEKHDQFEAVYEEIadILFEAA 80
Cdd:TIGR00522   2 LYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLlgssIEEIE------EFFGKRVVVLERSDVEENSF--RLIERA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 657202705   81 RREDVVYAVPGHPFVAEKTVQLLTErQEKENVQVKVAGGQSFLDA 125
Cdd:TIGR00522  74 KSKDVALLVAGDPMVATTHTDLKLE-AKRKGIETRIIHGASISSA 117
 
Name Accession Description Interval E-value
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 230-487 3.77e-141

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 406.03  E-value: 3.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 230 YHEFSTFRSIIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTI 309
Cdd:COG3956    8 LYAFERLLEIMARLRDPDGCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFDF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 310 DDVIKGISEKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKN---TSESSLLDSVPKTLPALSKAAKLQKKAAKVGFDW 386
Cdd:COG3956   88 DDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAekgEGRKSVLDGVPRSLPALMRAYKLQKKAARVGFDW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 387 EDVSDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVE 466
Cdd:COG3956  168 PDVEGVLDKVEEELAELKEALASGDQEA-IEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQGKS 246

                        250       260
                 ....*....|....*....|.
gi 657202705 467 LADMSLEDMDKLWNEAKETER 487
Cdd:COG3956  247 LEDLSLEEMDALWQEAKKAEK 267
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 239-483 3.33e-135

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 390.34  E-value: 3.33e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  239 IIRELRGP-NGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVIKGIS 317
Cdd:TIGR00444   1 IIAQLRDPeNGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  318 EKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKNTSES-SLLDSVPKTLPALSKAAKLQKKAAKVGFDWEDVSDIWEKV 396
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAQtSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  397 SEEMKEFSSEVSEAPHEHN-LKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVELADMSLEDM 475
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEQNkLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVDLEEM 240


                  ....*...
gi 657202705  476 DKLWNEAK 483
Cdd:TIGR00444 241 EELWQQVK 248
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 231-488 2.23e-121

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 355.63  E-value: 2.23e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 231 HEFSTFRSIIRELRGP-NGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTI 309
Cdd:PRK09562   7 EAIDRLLEIMARLRDPeGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAFDF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 310 DDVIKGISEKMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKNtsESSLLDSVPKTLPALSKAAKLQKKAAKVGFDWEDV 389
Cdd:PRK09562  87 ADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERA--ESSVLDGIPRGLPALMRAYKIQKKAARVGFDWESL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 390 SDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEGVELAD 469
Cdd:PRK09562 165 EPVLDKVEEEIDELKEALAQGDQAK-IEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKTLED 243

                        250
                 ....*....|....*....
gi 657202705 470 MSLEDMDKLWNEAKETERR 488
Cdd:PRK09562 244 ASLEEMDALWQEAKRQEKA 262
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 5-223 6.08e-115

N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.


Pssm-ID: 381177  Cd Length: 218  Bit Score: 337.54  E-value: 6.08e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   5 ITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPLIEELEKETKNIRFFDDIYEKHDQFEAVYEEIADILFEAARRED 84
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKVYLRTARHPVVEELKEEGIEFESFDDLYEEAEDFEEVYEAIAERLLEAAEHGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  85 VVYAVPGHPFVAEKTVQLLTERQEkENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADELELRHHLIICQVYD 164
Cdd:cd11723   81 VVYAVPGHPLVAERTVQLLLERAE-EGIEVEIIPGVSFLDAALAALGIDPIEGLQILDALDLDAEDLDPRLPLLITQVYN 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657202705 165 QMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELDRNVALNNLTSVYIPPI 223
Cdd:cd11723  160 RLVASDVKLTLMEVYPDEHEVTVVRAAGLGDEKVEEVPLYELDRQEDIDHLTSLYVPPL 218
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 234-347 2.89e-64

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 203.51  E-value: 2.89e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 234 STFRSIIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVI 313
Cdd:cd11528    1 ERLVEIVARLRGPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDVI 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 657202705 314 KGISEKMVRRHPHVFKDVKVQDENDVLANWEDIK 347
Cdd:cd11528   81 DGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 8-221 1.52e-55

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 184.90  E-value: 1.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   8 VGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPLIEEleKETKNIRFFDDIYEKHDQFeaVYEEIADILFEAAR-REDVV 86
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSL--VLRAILKDGKRIYDLHDPN--VEEEMAELLLEEARqGKDVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  87 YAVPGHPFVAEkTVQLLTERQEKENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADE--------LELRHHLI 158
Cdd:cd09815   77 FLSPGDPGVAG-TGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGESFLFVTASDLLENPrllvlkalAKERRHLV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657202705 159 ICQVYDqMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELD--RNVALNNLTSVYIP 221
Cdd:cd09815  156 LFLDGH-RFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRaeRTERGKPLTTILVG 219
PRK12333 PRK12333
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 239-442 2.56e-54

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237064 [Multi-domain]  Cd Length: 204  Bit Score: 181.16  E-value: 2.56e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 239 IIRELRGPNGCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVIKGISE 318
Cdd:PRK12333   7 VMRRLRGPDGCPWDREQTHESLRPYLLEEAAEAVDALSEGDPQELAEELGDVLLQVAFHSVIAEEEGRFTYPDVERGIVE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 319 KMVRRHPHVFKDVKVQDENDVLANWEDIKKAEKNTSESSLLDSVPKTLPALSKAAKLQKKAAkvgfdwedvsdiWEKVSE 398
Cdd:PRK12333  87 KLIRRHPHVFGDVQVSGPEEVVANWQAIKAAERGGGPRSAAERVPASLGALARAAELQKKLG------------REAGSR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 657202705 399 EmkefssEVSEAPHEhnlkAEFGDILFALVNVARFYKIEPEEAL 442
Cdd:PRK12333 155 E------GVIAALEE----GGVAEALWAVVAWARAEGIDPEIAL 188
PRK12334 PRK12334
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 242-464 9.06e-53

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237065 [Multi-domain]  Cd Length: 277  Bit Score: 179.48  E-value: 9.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 242 ELRGPngCPWDKKQTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGY--FTIDDVIKGISEK 319
Cdd:PRK12334  73 RLRSP--GPWESEQTHRSLARYLLEETYELLDAIESGDRDELREELGDVLLQVLFHARIAEEAPEdpFDIDDVAATLVAK 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 320 MVRRHPHVFKDVKVQDENDVLANWEDIKKAEKntSESSLLDSVPKTLPALSKAAKLQKKAAKVGFDwedvsdiwekvsee 399
Cdd:PRK12334 151 LVRRHPHVFADGEAISLEEQLAQWEARKAAEK--ARTSVLDGVPLGQPALALAAKVLSRARKAGLP-------------- 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657202705 400 mkefssevSEAPHEHNLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAKEEG 464
Cdd:PRK12334 215 --------VPLAPAEDSEDELGALLLALVAVAVAAGVDAEAALRAAVRDFRDRIRAAERAAAADG 271
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 382-483 6.80e-47

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress.


Pssm-ID: 212136  Cd Length: 116  Bit Score: 158.40  E-value: 6.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705 382 VGFDWEDVSDIWEKVSEEMKEFSSEVSEAPHEHnLKAEFGDILFALVNVARFYKIEPEEALTMTNDKFRRRFSYIEETAK 461
Cdd:cd11529   16 VGFDWPDAEGVLDKVEEELAELKEALASGDKEE-IEEELGDLLFSLVNLARFLGVDPEEALRRANRKFERRFRYMEELAA 94

                         90       100
                 ....*....|....*....|..
gi 657202705 462 EEGVELADMSLEDMDKLWNEAK 483
Cdd:cd11529   95 EQGKDLEDLSLEELDALWEEAK 116
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 255-328 1.17e-32

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 118.85  E-value: 1.17e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657202705  255 QTHQSLKQYMIEECYELLEAIDEEDTDHMIEELGDVLLQVLLHAQIGEDEGYFTIDDVIKGISEKMVRRHPHVF 328
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 4-207 6.24e-26

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 105.12  E-value: 6.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705    4 KITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHP-LIEELEKEtkniRFFDDIYEKHDQFEAVYEEIADILFEAARR 82
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALeILLDLLPE----DLYFPMTEDKEPLEEAYEEIAEALAAALRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   83 -EDVVYAVPGHPFVAEkTVQLLTERQEKENVQVKVAGGQSFLDATFNALQIDPIEGFQFVDAGTLSADELELRHHL---- 157
Cdd:pfam00590  77 gKDVARLVSGDPLVYG-TGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLeall 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657202705  158 ----IICQVYDQMTASEVKLTLMEKLPDDYEVVIVTAAGSRGEEIRTVPLFELD 207
Cdd:pfam00590 156 angdTVVLLYGPRRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
OphMA_like cd19916
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ...
 3-222 1.41e-19

tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA; OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A.


Pssm-ID: 381179  Cd Length: 237  Bit Score: 87.53  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   3 GKITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPLIEELEKETKNIRFFDDIYEKHDQFEAVYEEIADILFEAARR 82
Cdd:cd19916    1 GSLVVVGTGIKGIGHLTLEAESAIEQADKVFYLVADPLTEEWLRELNPNAEDLYDLYGEGKPRLDTYREMAERILEAVRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  83 E-DVVYAVPGHPFVAEKTVQLLTERQEKENVQVKVAGGQSFLDATFNALQIDP-IEGFQFVDAGTLSADELEL--RHHLI 158
Cdd:cd19916   81 GkPVCAAFYGHPGVFVSPSHLAIRIARREGYRARMLPGISAEDCLFADLGIDPgRPGCQSYEATDFLLRRRPLdpSAHLI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657202705 159 ICQV-------YDQMTASEVKLT-LMEKL----PDDYEVVIVTAAGSRGEE--IRTVPLFELdRNVALNNLTSVYIPP 222
Cdd:cd19916  161 LWQVgvvgdltFTRFGYDNRGLElLVEYLlkfyPPDHEVILYEAATYPGCEprIERIPLSDL-AEAELTGISTLYIPP 237
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 8-116 2.35e-04

diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.


Pssm-ID: 381174  Cd Length: 241  Bit Score: 42.79  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   8 VGLGAGDMDQLTIGIHKLLTKADTLYVR--TKDHP--LIEELEKET-KNIRFFD--DIyekhdqfeavyEEIADILFEAA 80
Cdd:cd11647    5 IGLGLGDEKDITLEGLEALKKADKVYLEayTSILPgsKLEELEKLIgKKIILLDreDL-----------EEESEEILEEA 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 657202705  81 RREDVVYAVPGHPFVAekT--VQLLTeRQEKENVQVKV 116
Cdd:cd11647   74 KKKDVALLVPGDPLIA--TthIDLRL-EAKKRGIKVKV 108
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
3-200 3.18e-04

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 42.21  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   3 GKITVVGLGAGDMDQLTIGIHKLLTKADTLYV----RTKD---HPLIEE-LEKETKnirffddIYEKH-------DQFEA 67
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVVYApasrKGGGslaLNIVRPyLKEETE-------IVELHfpmskdeEEKEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705  68 VYEEIADILFEAARR-EDVVYAVPGHPFVAEKTVQLLtERQEKENVQVK-VAGGQSF----------LDATFNALQIDPi 135
Cdd:PRK05576  75 VWKENAEEIAAEAEEgKNVAFITLGDPNLYSTFSHLL-EYLKCHDIEVEtVPGISSFtaiasragvpLAMGDESLAIIP- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657202705 136 egfqfVDAGTLSADELELRHHLIICQVYDqmtASEVKLTLMEKLPDDYevVIVTAAGSRGEEIRT 200
Cdd:PRK05576 153 -----ATREALIEQALTDFDSVVLMKVYK---NFALIEELLEEGYLDA--LYVRRAYMEGEQILR 207
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 1-95 8.62e-04

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 40.85  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705   1 MAGKITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKD-------HPLIEELEKETKnIRFFDDIYEK-HDQFEAVYEEI 72
Cdd:COG2243    1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGagkaslaREIVAPYLPPAR-IVELVFPMTTdYEALVAAWDEA 79

                         90       100
                 ....*....|....*....|....
gi 657202705  73 ADILFEAARR-EDVVYAVPGHPFV 95
Cdd:COG2243   80 AARIAEELEAgRDVAFLTEGDPSL 103
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 5-125 4.73e-03

diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]


Pssm-ID: 273117  Cd Length: 257  Bit Score: 38.64  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657202705    5 ITVVGLGAGDMDQLTIGIHKLLTKADTLYVRTKDHPL----IEELEketkniRFFDDIYEKHDQFEAVYEEIadILFEAA 80
Cdd:TIGR00522   2 LYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLlgssIEEIE------EFFGKRVVVLERSDVEENSF--RLIERA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 657202705   81 RREDVVYAVPGHPFVAEKTVQLLTErQEKENVQVKVAGGQSFLDA 125
Cdd:TIGR00522  74 KSKDVALLVAGDPMVATTHTDLKLE-AKRKGIETRIIHGASISSA 117
 
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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