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Conserved domains on  [gi|5911963|emb|CAB55956|]
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hypothetical protein, partial [Homo sapiens]

Protein Classification

THUMP_AdoMetMT and UPF0020 domain-containing protein( domain architecture ID 10659632)

THUMP_AdoMetMT and UPF0020 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 150-335 2.07e-70

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


:

Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 217.99  E-value: 2.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    150 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 228
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    229 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 308
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 5911963    309 TKALSGMRhvWRKVDTVWVNVGGLRAA 335
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 83-140 2.44e-13

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


:

Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 64.99  E-value: 2.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 5911963      83 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 140
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 150-335 2.07e-70

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 217.99  E-value: 2.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    150 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 228
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    229 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 308
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 5911963    309 TKALSGMRhvWRKVDTVWVNVGGLRAA 335
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 154-305 2.65e-20

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 86.93  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  154 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCfhIAGDNNPLAVNRAANNIASLLTKSqikegk 233
Cdd:COG1041   4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRV--IGSDIDPKMVEGARENLEHYGYED------ 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911963  234 pswglpIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNW-NLYPACLREMSRVcTPTTGRAVLLTQDT 305
Cdd:COG1041  76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARV-LKPGGRVVIVTPRD 141
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 83-140 2.44e-13

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 64.99  E-value: 2.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 5911963      83 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 140
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 83-140 1.02e-10

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 59.37  E-value: 1.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5911963     83 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 140
Cdd:pfam02926  84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 83-143 2.07e-10

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 58.36  E-value: 2.07e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963   83 KFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLNIHDNEVIVGIALT 143
Cdd:cd11715  87 TFAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSLDLS 151
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 117-300 8.21e-10

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 59.37  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    117 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 188
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    189 AIPIEGATewsdcfhiagdnnpLAVNRAANNIAslltkSQIKEGKPS----WGLP-IDAVQWDICNLPLRTGSVDIIVTD 263
Cdd:TIGR01177 195 GFLIEAGL--------------MGAKVIGCDID-----WKMVAGARInlehYGIEdFFVKRGDATKLPLSSESVDAIATD 255

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 5911963    264 LPFGkRMGSKKRNWN--LYPACLREMSRVCTPTTGRAVL 300
Cdd:TIGR01177 256 PPYG-RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 95-195 1.35e-08

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 56.35  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    95 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 160
Cdd:PRK11783  94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 5911963   161 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIEGA 195
Cdd:PRK11783 174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 84-138 3.41e-07

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 51.63  E-value: 3.41e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963   84 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 138
Cdd:COG0301 103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 150-335 2.07e-70

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 217.99  E-value: 2.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    150 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQ 228
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    229 IKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPtTGRAVLLTQDTKCF 308
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRG-GGWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 5911963    309 TKALSGMRhvWRKVDTVWVNVGGLRAA 335
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 154-305 2.65e-20

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 86.93  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  154 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCfhIAGDNNPLAVNRAANNIASLLTKSqikegk 233
Cdd:COG1041   4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRV--IGSDIDPKMVEGARENLEHYGYED------ 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911963  234 pswglpIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNW-NLYPACLREMSRVcTPTTGRAVLLTQDT 305
Cdd:COG1041  76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARV-LKPGGRVVIVTPRD 141
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 84-316 6.02e-18

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 84.00  E-value: 6.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963   84 FRVTCNRAGEKHcFTSNEAARDFGGAVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRN---ITH 154
Cdd:COG0116  90 FAVDATSVKSKL-FHSQFAALRVKDAIVDRFREKYgarpsvDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGyreAQG 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  155 FGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGA----------------TEWSDC----------------- 201
Cdd:COG0116 169 EAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEKWPDFdaelwqelreeaearik 246

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  202 ----FHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLP--IDAVQWDICNLPlRTGSVDIIVTDLPFGKRMGSKK 274
Cdd:COG0116 247 rdppLPIFGsDIDPRAIEAARENAERA-------------GVAdlIEFEQADFRDLE-PPAEPGLIITNPPYGERLGEEE 312

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 5911963  275 RNWNLYpaclREMSRVCTP--TTGRAVLLTQDTKcFTKALsGMR 316
Cdd:COG0116 313 ELEALY----RELGDVLKQrfKGWSAYILTSDPE-LEKAI-GLK 350
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 83-140 2.44e-13

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 64.99  E-value: 2.44e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 5911963      83 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 140
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 83-140 1.02e-10

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 59.37  E-value: 1.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5911963     83 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 140
Cdd:pfam02926  84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 83-143 2.07e-10

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 58.36  E-value: 2.07e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963   83 KFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLNIHDNEVIVGIALT 143
Cdd:cd11715  87 TFAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSLDLS 151
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 117-300 8.21e-10

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 59.37  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    117 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 188
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    189 AIPIEGATewsdcfhiagdnnpLAVNRAANNIAslltkSQIKEGKPS----WGLP-IDAVQWDICNLPLRTGSVDIIVTD 263
Cdd:TIGR01177 195 GFLIEAGL--------------MGAKVIGCDID-----WKMVAGARInlehYGIEdFFVKRGDATKLPLSSESVDAIATD 255

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 5911963    264 LPFGkRMGSKKRNWN--LYPACLREMSRVCTPTTGRAVL 300
Cdd:TIGR01177 256 PPYG-RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 95-195 1.35e-08

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 56.35  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    95 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 160
Cdd:PRK11783  94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 5911963   161 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIEGA 195
Cdd:PRK11783 174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 84-138 1.99e-08

THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212585  Cd Length: 166  Bit Score: 53.22  E-value: 1.99e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963   84 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 138
Cdd:cd11716 102 FKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 84-138 3.41e-07

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 51.63  E-value: 3.41e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963   84 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 138
Cdd:COG0301 103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 168-302 1.06e-06

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 47.68  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  168 MLRLCDPLPYDIIVDPMCGTGAIPIEGAtewSDCFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWD 246
Cdd:COG2226  14 LLAALGLRPGARVLDLGCGTGRLALALA---ERGARVTGvDISPEMLELARERAAEA-------------GLNVEFVVGD 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5911963  247 ICNLPLRTGSVDIIVTDLPFgkrmgskkRNWNLYPACLREMSRVCTPtTGRAVLLT 302
Cdd:COG2226  78 AEDLPFPDGSFDLVISSFVL--------HHLPDPERALAEIARVLKP-GGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 180-293 4.18e-05

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 41.78  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963    180 IVDPMCGTGAIPIEGATEWSdcFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWDICNLPLRTGSVD 258
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGvDLSPEMLERARERAAEA-------------GLNVEFVQGDAEDLPFPDGSFD 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 5911963    259 IIVTDLPFGkrmgskKRNWNLYPACLREMSRVCTP 293
Cdd:pfam13649  66 LVVSSGVLH------HLPDPDLEAALREIARVLKP 94
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
180-268 2.42e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 39.55  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911963  180 IVDPMCGTGAIPIEGATEWSDCFHIAG-DNNPLAVNRAANNIASLltksqikegkpswGLPIDAVQWDICNlPLRTGSVD 258
Cdd:COG0827 119 ILDPAVGTGNLLTTVLNQLKKKVNAYGvEVDDLLIRLAAVLANLQ-------------GHPVELFHQDALQ-PLLIDPVD 184

                        90
                ....*....|
gi 5911963  259 IIVTDLPFGK 268
Cdd:COG0827 185 VVISDLPVGY 194
 
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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