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Conserved domains on  [gi|881014577|ref|WP_048735286|]
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MULTISPECIES: tRNA 2-thiouridine(34) synthase MnmA [Corynebacterium]

Protein Classification

tRNA 2-thiouridine(34) synthase MnmA( domain architecture ID 10791795)

tRNA 2-thiouridine(34) synthase MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln) to form 5-taurinomethyl-2-thiouridine (tm5s2U)

CATH:  2.30.30.280|3.40.50.620
EC:  2.8.1.13
Gene Symbol:  mnmA
Gene Ontology:  GO:0005524|GO:0016783|GO:0000049|GO:0006400
PubMed:  3298234|16387657|16871210|12012333
SCOP:  4007171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 1-369 5.28e-180

tRNA-specific 2-thiouridylase MnmA; Reviewed


:

Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 503.45  E-value: 5.28e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRagSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETG--KGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDGLLRRGRDAKKDQSYVLGVLDREQLQR 160
Cdd:PRK00143  79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGRELLRGVDPNKDQSYFLYQLTQEQLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 161 SMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDKEtGDTVAEHDGVYGFTIGQRK 240
Cdd:PRK00143 159 LLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLD-GKVLGEHKGLMYYTIGQRK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 241 GIGLAGpmpDGKPRYVTGIDAETGTVTIGTAADLNVNVLEADRAIWLANPdevlAASEAGKLQVQVRAHGRPIDCRIEVl 320
Cdd:PRK00143 238 GLGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGE----PPEEPFECTAKIRYRQKPVPATVEL- 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 881014577 321 agpdddvtgRGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTI 369
Cdd:PRK00143 310 ---------EDDRVEVEFDEPQRAVTPGQAAVFYD----GDRVLGGGII 345
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 1-369 5.28e-180

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 503.45  E-value: 5.28e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRagSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETG--KGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDGLLRRGRDAKKDQSYVLGVLDREQLQR 160
Cdd:PRK00143  79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGRELLRGVDPNKDQSYFLYQLTQEQLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 161 SMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDKEtGDTVAEHDGVYGFTIGQRK 240
Cdd:PRK00143 159 LLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLD-GKVLGEHKGLMYYTIGQRK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 241 GIGLAGpmpDGKPRYVTGIDAETGTVTIGTAADLNVNVLEADRAIWLANPdevlAASEAGKLQVQVRAHGRPIDCRIEVl 320
Cdd:PRK00143 238 GLGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGE----PPEEPFECTAKIRYRQKPVPATVEL- 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 881014577 321 agpdddvtgRGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTI 369
Cdd:PRK00143 310 ---------EDDRVEVEFDEPQRAVTPGQAAVFYD----GDRVLGGGII 345
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 1-374 1.76e-176

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 494.57  E-value: 1.76e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSvrAGSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:COG0482    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDG---LLRRGRDAKKDQSYVLGVLDREQ 157
Cdd:COG0482   79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDgryELLRGVDPNKDQSYFLYRLTQEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 158 LQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDkETGDTVAEHDGVYGFTIG 237
Cdd:COG0482  159 LSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVD-LDGKVLGEHDGLHYYTIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 238 QRKGIGLAGpmpdGKPRYVTGIDAETGTVTIGTAADLNVNVLEADRAIWLANPDevlaASEAGKLQVQVRAHGRPIDCRI 317
Cdd:COG0482  238 QRKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEP----PEEPLRCTAKIRYRQPPVPATL 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 881014577 318 EVLAgpdddvtgrGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTIVSTAR 374
Cdd:COG0482  310 TPLE---------DGRVRVEFDEPQRAVTPGQSAVFYD----GDRVLGGGIIERTER 353
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 2-369 1.54e-139

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 400.73  E-value: 1.54e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDpqsVRAGSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEEV 81
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDD---EDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  82 MDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDG----LLRRGRDAKKDQSYVLGVLDREQ 157
Cdd:cd01998   78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNrgryRLLRAVDPNKDQSYFLSRLSQEQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 158 LQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIG-RRPGTIVDKEtGDTVAEHDGVYGFTI 236
Cdd:cd01998  158 LSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDID-GKVLGEHKGLWFYTI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 237 GQRKGIGLAgpmpDGKPRYVTGIDAETGTVTIGTAA-DLNVNVLEADRAIWLANPDEvlaaSEAGKLQVQVRAHGRPIDC 315
Cdd:cd01998  237 GQRKGLGIA----AGEPLYVVKKDPEKNIVVVGPGHpALFSDTLRASDLNWISPEPP----LEPLECEAKIRYRQPPVPC 308

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 881014577 316 RIEVLAgpdddvtgrGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTI 369
Cdd:cd01998  309 TVTPLD---------DGRLKVEFDEPQRAVTPGQAAVFYD----GDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 1-369 6.95e-94

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 284.66  E-value: 6.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577    1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRAGsrGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:TIGR00420   1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGH--GCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGI-ALGFDAVVTGHYALLGDD---GLLRRGRDAKKDQSYVLGVLDRE 156
Cdd:TIGR00420  79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEIegkSLLLRALDKNKDQSYFLYHLSHE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  157 QLQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDKETGDTVAEHDGVYGFTI 236
Cdd:TIGR00420 159 QLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  237 GQRKGIGLAGPMpdgKPRYVTGIDAETGTVTIGTA-ADLNVNVLEADRAIWLANPDEvlaaSEAGKLQVQVRAHGRPIDC 315
Cdd:TIGR00420 239 GQRKGLGIGGAA---EPWFVVEKDLETNELVVSHGkPDLASRGLLAQQFHWLDDEPN----PFEMRCTVKIRYRQVPVQC 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 881014577  316 RIEVLagpDDDVtgrggaFRLHLSDPLRGVAPGQAAVLYhtdtAGDYVLGSGTI 369
Cdd:TIGR00420 312 KLKLL---DDNL------IEVIFDEPQAGVTPGQSAVLY----KGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 1-198 1.45e-92

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 276.06  E-value: 1.45e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577    1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRAGSRgCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIA-LGFDAVVTGHYALLGDDG----LLRRGRDAKKDQSYVLGVLDR 155
Cdd:pfam03054  80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKdggsELLRALDKNKDQSYFLSTLSQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 881014577  156 EQLQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPD 198
Cdd:pfam03054 160 EQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
 
Name Accession Description Interval E-value
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 1-369 5.28e-180

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 503.45  E-value: 5.28e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRagSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDDDDETG--KGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDGLLRRGRDAKKDQSYVLGVLDREQLQR 160
Cdd:PRK00143  79 VIDYFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARELGADYIATGHYARIRDGRELLRGVDPNKDQSYFLYQLTQEQLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 161 SMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDKEtGDTVAEHDGVYGFTIGQRK 240
Cdd:PRK00143 159 LLFPLGELTKPEVREIAEEAGLPVAKKKDSQGICFIGERDYRDFLKRYLPAQPGEIVDLD-GKVLGEHKGLMYYTIGQRK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 241 GIGLAGpmpDGKPRYVTGIDAETGTVTIGTAADLNVNVLEADRAIWLANPdevlAASEAGKLQVQVRAHGRPIDCRIEVl 320
Cdd:PRK00143 238 GLGIGG---DGEPWYVVGKDPETNTVVVGQGEALYSRELIASDLNWVGGE----PPEEPFECTAKIRYRQKPVPATVEL- 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 881014577 321 agpdddvtgRGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTI 369
Cdd:PRK00143 310 ---------EDDRVEVEFDEPQRAVTPGQAAVFYD----GDRVLGGGII 345
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 1-374 1.76e-176

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 494.57  E-value: 1.76e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSvrAGSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:COG0482    1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDDDDA--SGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDG---LLRRGRDAKKDQSYVLGVLDREQ 157
Cdd:COG0482   79 VIDYFLDEYLAGRTPNPCVLCNREIKFGALLEKALELGADYIATGHYARVEEKDgryELLRGVDPNKDQSYFLYRLTQEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 158 LQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDkETGDTVAEHDGVYGFTIG 237
Cdd:COG0482  159 LSKTLFPLGELTKPEVREIAEELGLPVADKKDSQGICFIGDGDYRDFLERYLPEKPGDIVD-LDGKVLGEHDGLHYYTIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 238 QRKGIGLAGpmpdGKPRYVTGIDAETGTVTIGTAADLNVNVLEADRAIWLANPDevlaASEAGKLQVQVRAHGRPIDCRI 317
Cdd:COG0482  238 QRKGLGIGG----GEPLYVVGKDPETNTVIVGQGEALYSRELTAEDVNWISGEP----PEEPLRCTAKIRYRQPPVPATL 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 881014577 318 EVLAgpdddvtgrGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTIVSTAR 374
Cdd:COG0482  310 TPLE---------DGRVRVEFDEPQRAVTPGQSAVFYD----GDRVLGGGIIERTER 353
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 2-369 1.54e-139

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 400.73  E-value: 1.54e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDpqsVRAGSRGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEEV 81
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDD---EDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  82 MDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDG----LLRRGRDAKKDQSYVLGVLDREQ 157
Cdd:cd01998   78 FDPFLEEYKAGRTPNPDVLCNREIKFGALLDAAKKLGADYIATGHYARIEEDNrgryRLLRAVDPNKDQSYFLSRLSQEQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 158 LQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIG-RRPGTIVDKEtGDTVAEHDGVYGFTI 236
Cdd:cd01998  158 LSRTLFPLGHLTKSEVREIAREAGLPVAEKKDSQGICFIGKRDFRDFLKEYLPeKLPGPIVDID-GKVLGEHKGLWFYTI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 237 GQRKGIGLAgpmpDGKPRYVTGIDAETGTVTIGTAA-DLNVNVLEADRAIWLANPDEvlaaSEAGKLQVQVRAHGRPIDC 315
Cdd:cd01998  237 GQRKGLGIA----AGEPLYVVKKDPEKNIVVVGPGHpALFSDTLRASDLNWISPEPP----LEPLECEAKIRYRQPPVPC 308

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 881014577 316 RIEVLAgpdddvtgrGGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTI 369
Cdd:cd01998  309 TVTPLD---------DGRLKVEFDEPQRAVTPGQAAVFYD----GDEVLGGGII 349
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 1-369 6.95e-94

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 284.66  E-value: 6.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577    1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRAGsrGCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:TIGR00420   1 KKVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGH--GCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGI-ALGFDAVVTGHYALLGDD---GLLRRGRDAKKDQSYVLGVLDRE 156
Cdd:TIGR00420  79 VFEPFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAeLLGNDKIATGHYARIAEIegkSLLLRALDKNKDQSYFLYHLSHE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  157 QLQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPDGNTKAFLGAKIGRRPGTIVDKETGDTVAEHDGVYGFTI 236
Cdd:TIGR00420 159 QLAKLLFPLGELLKPEVRQIAKNAGLPTAEKKDSQGICFIGERKFRDFLKKYLPVKPGVIITVDGQSVIGEHDGLWFYTI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  237 GQRKGIGLAGPMpdgKPRYVTGIDAETGTVTIGTA-ADLNVNVLEADRAIWLANPDEvlaaSEAGKLQVQVRAHGRPIDC 315
Cdd:TIGR00420 239 GQRKGLGIGGAA---EPWFVVEKDLETNELVVSHGkPDLASRGLLAQQFHWLDDEPN----PFEMRCTVKIRYRQVPVQC 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 881014577  316 RIEVLagpDDDVtgrggaFRLHLSDPLRGVAPGQAAVLYhtdtAGDYVLGSGTI 369
Cdd:TIGR00420 312 KLKLL---DDNL------IEVIFDEPQAGVTPGQSAVLY----KGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 1-198 1.45e-92

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 276.06  E-value: 1.45e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577    1 MRVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRAGSRgCCSLEDSGDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEQSLDEEGK-CCSEEDLADAQRVCEQLGIPLYVVNFEKEYWED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIA-LGFDAVVTGHYALLGDDG----LLRRGRDAKKDQSYVLGVLDR 155
Cdd:pfam03054  80 VFEPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALEnLGADYVATGHYARVSLNKdggsELLRALDKNKDQSYFLSTLSQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 881014577  156 EQLQRSMFPVGNTEKPEIREEARGMGLGTANKPDSYDICFIPD 198
Cdd:pfam03054 160 EQLEKLLFPLGELTKEEVRKIAKEAGLATAKKKDSQGICFIGK 202
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 2-371 6.07e-60

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 197.87  E-value: 6.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKD-PQsvragsrgccsledsgDARRVCDELGIPFYVWDFSERFKEE 80
Cdd:PRK14664   7 RVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDePQ----------------DARELAARMGIEHYVADERVPFKDT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYALLGDDG---LLRRGRDAKKDQSYVLGVLDREQ 157
Cdd:PRK14664  71 IVKNFIDEYRQGRTPNPCVMCNPLFKFRMLIEWADKLGCAWIATGHYSRLEERNghiYIVAGDDDKKDQSYFLWRLGQDI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 158 LQRSMFPVGNTEKPEIREEARGMGL-GTANKPDSYDICFIpDGNTKAFL-------GAKIGrrPGTIVDKEtGDTVAEHD 229
Cdd:PRK14664 151 LRRCIFPLGNYTKQTVREYLREKGYeAKSKEGESMEVCFI-KGDYRDFLreqcpelDTEVG--PGWFVNSE-GVKLGQHK 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 230 GVYGFTIGQRKGIGLAgpmpDGKPRYVTGIDAETGTVTIGTAADLNVN--VLEADRaiwLANPDEVLAASEagkLQVQVR 307
Cdd:PRK14664 227 GFPYYTIGQRKGLEIA----LGKPAYVLKINPQKNTVMLGDAEQLKAEymLAEQDN---IVDEQELFACPD---LAVRIR 296

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881014577 308 AHGRPIDCRIEVLagpDDdvtgrgGAFRLHLSDPLRGVAPGQAAVLYHtdtaGDYVLGSGTIVS 371
Cdd:PRK14664 297 YRSRPIPCRVKRL---ED------GRLLVRFLAEASAIAPGQSAVFYE----GRRVLGGAFIAS 347
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 2-370 3.84e-47

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 164.34  E-value: 3.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSVRagsrgccSLEDsgdARRVCDELGIPFYVWDFSERFKEEV 81
Cdd:PRK14665   7 RVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEFNGSTE-------YLED---ARALAERLGIGHITYDARKVFRKQI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  82 MDDFYDSYERGETPNPCLRCNERIKFAALLERGIALGFDAVVTGHYA---LLGDDGLLRRGRDAKKDQSYVLGVLDREQL 158
Cdd:PRK14665  77 IDYFIDEYMSGHTPVPCTLCNNYLKWPLLAKIADEMGIFYLATGHYVrkqWIDGNYYITPAEDVDKDQSFFLWGLRQEIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 159 QRSMFPVGNTEKPEIREEARGMG-LGTANKPDSYDICFIPdGNTKAFL-----------GAKIGR--RPGTIVDkETGDT 224
Cdd:PRK14665 157 QRMLLPMGGMTKSEARAYAAERGfEKVAKKRDSLGVCFCP-MDYRSFLkkclcdesgdkNRNIYRkvERGRFLD-ESGNF 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577 225 VAEHDGVYGFTIGQRKGIGLAgpmpDGKPRYVTGIDAETGTVTIgtaADLnvNVLEADRaIWLANPDEVLAASEAGKLQV 304
Cdd:PRK14665 235 IAWHEGYPFYTIGQRRGLGIQ----LNRAVFVKEIHPETNEVVL---ASL--KALEKTE-MWLKDWNIVNESRLLGCDDI 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881014577 305 QVRAHGRPIDCRIEVLAGPDddvtgrgGAFRLHLSDPLRGVAPGQAAVLYHTDTagdyVLGSGTIV 370
Cdd:PRK14665 305 IVKIRYRKQENHCTVTITPD-------NLLHVQLHEPLTAIAEGQAAAFYKDGL----LLGGGIIT 359
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 202-269 7.47e-20

tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466410 [Multi-domain]  Cd Length: 66  Bit Score: 82.27  E-value: 7.47e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881014577  202 KAFLGAKIGRRPGTIVDKETGDTVAEHDGVYGFTIGQRKGIGLAGpmpDGKPRYVTGIDAETGTVTIG 269
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIDIDTGEVLGEHEGIWFYTIGQRKGLGIGG---YGEPWYVVEKDPKKNTVYVG 65
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 279-369 2.38e-14

Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466409 [Multi-domain]  Cd Length: 77  Bit Score: 67.69  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  279 LEADRAIWLANPDEvlaaSEAGKLQVQVRAHGRPIDCRIEVLagpDDDVtgrggaFRLHLSDPLRGVAPGQAAVLYhtdt 358
Cdd:pfam20258   4 LRAKDPNWLGDKPP----TEPLECTVKVRHRQPPVPCVVELI---DDET------VEVHFDEPVRAVTPGQAAVFY---- 66

                          90
                  ....*....|.
gi 881014577  359 AGDYVLGSGTI 369
Cdd:pfam20258  67 DGDRCLGGGII 77
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 2-188 1.17e-08

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 54.96  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSS-VAAARALAAGHEVVGVHLALSKDPQSVragsrgccsLEdsgDARRVCDELGIpfyvwdfseRFKEE 80
Cdd:cd01990    1 KVVVAFSGGVDSSlLAKLAKEVLGDNVVAVTADSPLVPREE---------LE---EAKRIAEEIGI---------RHEII 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 VMDDFYDSYERGETPNPCLRCNERIkFAALLERGIALGFDAVVTGHYAllgDD-GLLRRGRDAKKDqsyvLGVldreqlq 159
Cdd:cd01990   60 KTDELDDEEYVANDPDRCYHCKKAL-YSTLKEIAKERGYDVVLDGTNA---DDlKDYRPGLLAAAE----LGI------- 124

                        170       180
                 ....*....|....*....|....*....
gi 881014577 160 RSMFPVGNTEKPEIREEARGMGLGTANKP 188
Cdd:cd01990  125 RSPLPELGLTKSEIRELARELGLPNWDKP 153
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
2-188 2.03e-08

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 54.73  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARalaaGHEVVGVH-LALSKDPQSVRAgsrgccslEDSGDARRVCDELGIPFYVWDFSErfkee 80
Cdd:COG1606   17 SVLVAFSGGVDSTLLAKV----AHDVLGDRvLAVTADSPSLPE--------RELEEAKELAKEIGIRHEVIETDE----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577  81 vMDDfyDSYERGeTPNPCLRC-NERikFAALLERGIALGFDAVVTG-HYALLGDDgllRRGRDAKKDqsyvLGVldreql 158
Cdd:COG1606   80 -LED--PEFVAN-PPDRCYHCkKEL--FSKLKELAKELGYAVVADGtNADDLGDY---RPGLRAAKE----LGV------ 140

                        170       180       190
                 ....*....|....*....|....*....|...
gi 881014577 159 qRSmfP---VGNTeKPEIREEARGMGLGTANKP 188
Cdd:COG1606  141 -RS--PlaeAGLT-KAEIRELARELGLPTWDKP 169
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-126 6.61e-08

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 52.91  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSV----AAARALAAGHEVVGVHLalskDPQsVRAGSRgccslEDSGDARRVCDELGIPFYVwdfsERF 77
Cdd:COG0037   17 RILVAVSGGKDSLAllhlLAKLRRRLGFELVAVHV----DHG-LREESD-----EDAEFVAELCEELGIPLHV----VRV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 881014577  78 KEEvmddfYDSYERGEtpNPCLRCNeRIKFAALLERGIALGFDAVVTGH 126
Cdd:COG0037   83 DVP-----AIAKKEGK--SPEAAAR-RARYGALYELARELGADKIATGH 123
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 2-126 4.11e-06

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 46.93  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881014577   2 RVLAAMSGGVDSSVAAARALAAGHEVVGVHLALSKDPQSvragsrgccslEDSGD-ARRVCDELGIPFYVWDFSERFK-- 78
Cdd:cd01993   10 KILVAVSGGKDSLALLAVLKKLGYNVEALYINLGIGEYS-----------EKSEEvVKKLAEKLNLPLHVVDLKEEYGlg 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 881014577  79 -EEVMDDFydsyERGetpnPCLRC--------NeriKFAALlergiaLGFDAVVTGH 126
Cdd:cd01993   79 iPELAKKS----RRP----PCSVCglvkryimN---KFAVE------NGFDVVATGH 118
 
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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