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Conserved domains on  [gi|1942005446|ref|WP_197185664|]
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tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE [Pseudoalteromonas sp. NSLLW218]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ferritin_like super family cl00264
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
5-248 4.89e-99

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


The actual alignment was detected with superfamily member pfam06175:

Pssm-ID: 469698  Cd Length: 199  Bit Score: 287.45  E-value: 4.89e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446   5 QLLEPINNFLLCTTPEQWVQQAIKKENLSVILIDHLICELKAAQSAMFLIRRYAvdkegsdallewlkpfetliykregn 84
Cdd:pfam06175   1 QLLPPIINFLKCPTPQAWVEQAREIANLDVLLLDHSHCELKAAQTAMNLMRRYA-------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  85 wrdlaaknkltksiipksssPYGQGLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALV 164
Cdd:pfam06175  55 --------------------PSNQDLVNKLTRLAKEELHHFEQVLEILEARNIPYAPISASRYAKGLLAAVRTHEPQRLL 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446 165 DKLIVGAYIEARSCERFAKLAPHVDKRLGDFYISLLRSEARHYQDYLTLAQEIAD-FDITERVNFFGEKEKELISTTDTD 243
Cdd:pfam06175 115 DKLIVGAYIEARSCERFALLAPHLDAELAKFYVSLLRSEARHFQDYLKLAYQYFDeEDVSERVAYFGAVEAELISTPDPE 194

                  ....*
gi 1942005446 244 FKFHS 248
Cdd:pfam06175 195 FRFHS 199
 
Name Accession Description Interval E-value
MiaE pfam06175
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
5-248 4.89e-99

tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO(6)A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.


Pssm-ID: 114868  Cd Length: 199  Bit Score: 287.45  E-value: 4.89e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446   5 QLLEPINNFLLCTTPEQWVQQAIKKENLSVILIDHLICELKAAQSAMFLIRRYAvdkegsdallewlkpfetliykregn 84
Cdd:pfam06175   1 QLLPPIINFLKCPTPQAWVEQAREIANLDVLLLDHSHCELKAAQTAMNLMRRYA-------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  85 wrdlaaknkltksiipksssPYGQGLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALV 164
Cdd:pfam06175  55 --------------------PSNQDLVNKLTRLAKEELHHFEQVLEILEARNIPYAPISASRYAKGLLAAVRTHEPQRLL 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446 165 DKLIVGAYIEARSCERFAKLAPHVDKRLGDFYISLLRSEARHYQDYLTLAQEIAD-FDITERVNFFGEKEKELISTTDTD 243
Cdd:pfam06175 115 DKLIVGAYIEARSCERFALLAPHLDAELAKFYVSLLRSEARHFQDYLKLAYQYFDeEDVSERVAYFGAVEAELISTPDPE 194

                  ....*
gi 1942005446 244 FKFHS 248
Cdd:pfam06175 195 FRFHS 199
MiaE COG4445
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
5-248 4.43e-97

tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]; tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443544  Cd Length: 198  Bit Score: 282.40  E-value: 4.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446   5 QLLEPINNFLLCTTPEQWVQQAIkkENLSVILIDHLICELKAAQSAMFLIRRYavdkegsdallewlkpfetliykregn 84
Cdd:COG4445     2 SLLTPIMLFLKCPTPPAWVEAAL--ANLDELLIDHAHCEKKAASTAMSLIFRY--------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  85 wrdlaaknkltksiipksssPYGQGLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALV 164
Cdd:COG4445    53 --------------------PDKPELVRKMSALAREELEHFEQVLEIMKKRGITLGRLRADRYANGLRKLVRTSEPERLL 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446 165 DKLIVGAYIEARSCERFAKLAPHV-DKRLGDFYISLLRSEARHYQDYLTLAQEIAD-FDITERVNFFGEKEKELISTTDT 242
Cdd:COG4445   113 DRLLVGALIEARSCERFALLAPHLpDEELAKFYRSLLRSEARHYQDYLKLARQYFDeEDVDERLEELLEAEAELIASLDP 192

                  ....*.
gi 1942005446 243 DFKFHS 248
Cdd:COG4445   193 EFRFHS 198
MiaE cd07910
MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is ...
12-237 8.19e-67

MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.


Pssm-ID: 153119  Cd Length: 180  Bit Score: 204.72  E-value: 8.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  12 NFLLCTTPEQWVQQAikKENLSVILIDHLICELKAAQSAMFLIRRYAVDKEgsdallewlkpfetliykregnwrdlaak 91
Cdd:cd07910     1 LFLKSPTPPAWLDAA--LANLDEILIDHAHCEKKAASSAMSLIFRYPEKPE----------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  92 nkltksiipkssspygqgLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALVDKLIVGA 171
Cdd:cd07910    50 ------------------LVEAMSDLAREELQHFEQVLKIMKKRGIPLGPDSKDPYASGLRKLVRKGEPERLLDRLLVAA 111
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942005446 172 YIEARSCERFAKLAPHV-DKRLGDFYISLLRSEARHYQDYLTLAQEIADF-DITERVNFFGEKEKELI 237
Cdd:cd07910   112 LIEARSCERFALLAPALpDPELKKFYRGLLESEARHYELFLDLARKYFDEeDVDARLDELLAAEAEII 179
 
Name Accession Description Interval E-value
MiaE pfam06175
tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO ...
5-248 4.89e-99

tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); This family consists of several bacterial tRNA-(MS(2)IO(6)A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.


Pssm-ID: 114868  Cd Length: 199  Bit Score: 287.45  E-value: 4.89e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446   5 QLLEPINNFLLCTTPEQWVQQAIKKENLSVILIDHLICELKAAQSAMFLIRRYAvdkegsdallewlkpfetliykregn 84
Cdd:pfam06175   1 QLLPPIINFLKCPTPQAWVEQAREIANLDVLLLDHSHCELKAAQTAMNLMRRYA-------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  85 wrdlaaknkltksiipksssPYGQGLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALV 164
Cdd:pfam06175  55 --------------------PSNQDLVNKLTRLAKEELHHFEQVLEILEARNIPYAPISASRYAKGLLAAVRTHEPQRLL 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446 165 DKLIVGAYIEARSCERFAKLAPHVDKRLGDFYISLLRSEARHYQDYLTLAQEIAD-FDITERVNFFGEKEKELISTTDTD 243
Cdd:pfam06175 115 DKLIVGAYIEARSCERFALLAPHLDAELAKFYVSLLRSEARHFQDYLKLAYQYFDeEDVSERVAYFGAVEAELISTPDPE 194

                  ....*
gi 1942005446 244 FKFHS 248
Cdd:pfam06175 195 FRFHS 199
MiaE COG4445
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) ...
5-248 4.43e-97

tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) [Translation, ribosomal structure and biogenesis]; tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE (synthesis of 2-methylthio-cis-ribozeatin) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443544  Cd Length: 198  Bit Score: 282.40  E-value: 4.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446   5 QLLEPINNFLLCTTPEQWVQQAIkkENLSVILIDHLICELKAAQSAMFLIRRYavdkegsdallewlkpfetliykregn 84
Cdd:COG4445     2 SLLTPIMLFLKCPTPPAWVEAAL--ANLDELLIDHAHCEKKAASTAMSLIFRY--------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  85 wrdlaaknkltksiipksssPYGQGLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALV 164
Cdd:COG4445    53 --------------------PDKPELVRKMSALAREELEHFEQVLEIMKKRGITLGRLRADRYANGLRKLVRTSEPERLL 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446 165 DKLIVGAYIEARSCERFAKLAPHV-DKRLGDFYISLLRSEARHYQDYLTLAQEIAD-FDITERVNFFGEKEKELISTTDT 242
Cdd:COG4445   113 DRLLVGALIEARSCERFALLAPHLpDEELAKFYRSLLRSEARHYQDYLKLARQYFDeEDVDERLEELLEAEAELIASLDP 192

                  ....*.
gi 1942005446 243 DFKFHS 248
Cdd:COG4445   193 EFRFHS 198
MiaE cd07910
MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is ...
12-237 8.19e-67

MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain; MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.


Pssm-ID: 153119  Cd Length: 180  Bit Score: 204.72  E-value: 8.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  12 NFLLCTTPEQWVQQAikKENLSVILIDHLICELKAAQSAMFLIRRYAVDKEgsdallewlkpfetliykregnwrdlaak 91
Cdd:cd07910     1 LFLKSPTPPAWLDAA--LANLDEILIDHAHCEKKAASSAMSLIFRYPEKPE----------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942005446  92 nkltksiipkssspygqgLIDKMVLLIKEELHHFYQVLEIMDEYGVEYRSITPCRYAKGMLRHVKTFEPDALVDKLIVGA 171
Cdd:cd07910    50 ------------------LVEAMSDLAREELQHFEQVLKIMKKRGIPLGPDSKDPYASGLRKLVRKGEPERLLDRLLVAA 111
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942005446 172 YIEARSCERFAKLAPHV-DKRLGDFYISLLRSEARHYQDYLTLAQEIADF-DITERVNFFGEKEKELI 237
Cdd:cd07910   112 LIEARSCERFALLAPALpDPELKKFYRGLLESEARHYELFLDLARKYFDEeDVDARLDELLAAEAEII 179
 
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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