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Conserved domains on  [gi|157388919|ref|NP_060426|]
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tRNA wybutosine-synthesizing protein 2 homolog [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase family protein( domain architecture ID 1001310)

class I SAM-dependent methyltransferase family protein that catalyzes the transfer of the methyl or the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine (SAM or AdoMet) to one or more specific substrates; similar to tRNA (guanine(37)-N1)-methyltransferase and tRNA wybutosine-synthesizing protein 2 homolog

EC:  2.-.-.-
Gene Ontology:  GO:0008175|GO:0030488
PubMed:  12826405|12504684

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Trm5 super family cl34477
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
30-441 1.47e-56

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


The actual alignment was detected with superfamily member COG2520:

Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 190.07  E-value: 1.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  30 TQRYREYLQRQKLFDTQHRVEKmPDGSVALPVlgetlpeqhlqelrNRVAPGSPCMLTQLPDPVPSKRAqgcspaqklcl 109
Cdd:COG2520   10 AERVRRRLREEGLLDKDRKIKV-DGDYVYIPV--------------TEPPEDGEVVEQEFPEREPPSLK----------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 110 evsrwvEGRGVKWSAELEADLPRSWQRHGNLLLLSEDCFQAKQWKNLGPELWE------TValalgvqrLAKRGRVSPDg 183
Cdd:COG2520   64 ------ELLEGGLPEELLELLPSSYDIIGDIAIIKIPDELEEYKEEIAEAILEshpnvkTV--------LAKASGVEGE- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 184 TRTPAVTLLLGDHG-WVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGaAFVH 262
Cdd:COG2520  129 FRVPELELLAGEGRtETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKRSG-AKVV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 263 ACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKL--KLSNIADRVILGLIPSSEEGWPIACQVLRqdAGGILHIHQNVE 340
Cdd:COG2520  208 AIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVapELEGKADRIIMNLPHSADEFLDAALRALK--PGGVIHYYEIVP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 341 sfpgknlqalgvskvEKEHWlypqqittnqwkngatrdsrgkmlspatkpewqrwaESAETRIATLLQqvhGKPWKTQIL 420
Cdd:COG2520  286 ---------------EEDPF------------------------------------ERAEERIEEAAE---EAGYEVEIL 311
                        410       420
                 ....*....|....*....|.
gi 157388919 421 HIQPVKSYAPHVDHIVLDLEC 441
Cdd:COG2520  312 EKRRVKSYSPGVYHVVVDVRV 332
 
Name Accession Description Interval E-value
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
30-441 1.47e-56

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 190.07  E-value: 1.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  30 TQRYREYLQRQKLFDTQHRVEKmPDGSVALPVlgetlpeqhlqelrNRVAPGSPCMLTQLPDPVPSKRAqgcspaqklcl 109
Cdd:COG2520   10 AERVRRRLREEGLLDKDRKIKV-DGDYVYIPV--------------TEPPEDGEVVEQEFPEREPPSLK----------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 110 evsrwvEGRGVKWSAELEADLPRSWQRHGNLLLLSEDCFQAKQWKNLGPELWE------TValalgvqrLAKRGRVSPDg 183
Cdd:COG2520   64 ------ELLEGGLPEELLELLPSSYDIIGDIAIIKIPDELEEYKEEIAEAILEshpnvkTV--------LAKASGVEGE- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 184 TRTPAVTLLLGDHG-WVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGaAFVH 262
Cdd:COG2520  129 FRVPELELLAGEGRtETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKRSG-AKVV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 263 ACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKL--KLSNIADRVILGLIPSSEEGWPIACQVLRqdAGGILHIHQNVE 340
Cdd:COG2520  208 AIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVapELEGKADRIIMNLPHSADEFLDAALRALK--PGGVIHYYEIVP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 341 sfpgknlqalgvskvEKEHWlypqqittnqwkngatrdsrgkmlspatkpewqrwaESAETRIATLLQqvhGKPWKTQIL 420
Cdd:COG2520  286 ---------------EEDPF------------------------------------ERAEERIEEAAE---EAGYEVEIL 311
                        410       420
                 ....*....|....*....|.
gi 157388919 421 HIQPVKSYAPHVDHIVLDLEC 441
Cdd:COG2520  312 EKRRVKSYSPGVYHVVVDVRV 332
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
184-334 5.65e-35

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 128.62  E-value: 5.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  184 TRTPAVTLLLGDHGWVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGAAFVHA 263
Cdd:pfam02475  49 FRTPRYEVLAGSDTETIHKENGCRFKVDVAKVYWSPRLIAERERIAKLVEPGEVVVDMFAGIGPFSIPIAKHSKARRVYA 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157388919  264 CEWNPHAVVALRNNLEINGVADRCQIHFGDNRKLKLSNIADRVILGLIPSSEEGWPIACQVLRQdaGGILH 334
Cdd:pfam02475 129 IELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDVADRVVMNLPGSAHEFLDKAFAAVRD--GGVIH 197
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
238-336 8.09e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 38.95  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 238 LVDLYAGIGYFTLPfLVHAGAAFVHACEWNPHAVVALRNNlEINGVADRCQIHFGDNRKLKLSNI--ADRVIL-GLIPSS 314
Cdd:cd02440    2 VLDLGCGTGALALA-LASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADesFDVIISdPPLHHL 79
                         90       100
                 ....*....|....*....|....*..
gi 157388919 315 EEGWPiacQVLRQ-----DAGGILHIH 336
Cdd:cd02440   80 VEDLA---RFLEEarrllKPGGVLVLT 103
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
149-285 1.36e-03

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 40.96  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  149 QAKQWKNLGPELWETVALALGVQRlAKRGRVSPDGTRTpavtlLLGDHGWVEhVDNGIRYKFD----------VTQCMFs 218
Cdd:TIGR00479 210 KEELDLYLQPDSPDVKSICQNINP-EKTNVIFGEETEV-----IAGEMPIYD-KSGDLSFTFSardfiqvnsgQNEKLV- 281
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157388919  219 fgniTEKLRVASLSCAgEVLVDLYAGIGYFTLPflVHAGAAFVHACEWNPHAVVALRNNLEINGVAD 285
Cdd:TIGR00479 282 ----DRALEWLELQGE-ERVLDAYCGMGTFTLP--LAKQAKSVVGVEGVPESVEKAQQNAELNGIAN 341
 
Name Accession Description Interval E-value
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
30-441 1.47e-56

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 190.07  E-value: 1.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  30 TQRYREYLQRQKLFDTQHRVEKmPDGSVALPVlgetlpeqhlqelrNRVAPGSPCMLTQLPDPVPSKRAqgcspaqklcl 109
Cdd:COG2520   10 AERVRRRLREEGLLDKDRKIKV-DGDYVYIPV--------------TEPPEDGEVVEQEFPEREPPSLK----------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 110 evsrwvEGRGVKWSAELEADLPRSWQRHGNLLLLSEDCFQAKQWKNLGPELWE------TValalgvqrLAKRGRVSPDg 183
Cdd:COG2520   64 ------ELLEGGLPEELLELLPSSYDIIGDIAIIKIPDELEEYKEEIAEAILEshpnvkTV--------LAKASGVEGE- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 184 TRTPAVTLLLGDHG-WVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGaAFVH 262
Cdd:COG2520  129 FRVPELELLAGEGRtETIHRENGCRFKLDVAKVYFSPRLATERLRIAELVKPGERVLDMFAGVGPFSIPIAKRSG-AKVV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 263 ACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKL--KLSNIADRVILGLIPSSEEGWPIACQVLRqdAGGILHIHQNVE 340
Cdd:COG2520  208 AIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVapELEGKADRIIMNLPHSADEFLDAALRALK--PGGVIHYYEIVP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 341 sfpgknlqalgvskvEKEHWlypqqittnqwkngatrdsrgkmlspatkpewqrwaESAETRIATLLQqvhGKPWKTQIL 420
Cdd:COG2520  286 ---------------EEDPF------------------------------------ERAEERIEEAAE---EAGYEVEIL 311
                        410       420
                 ....*....|....*....|.
gi 157388919 421 HIQPVKSYAPHVDHIVLDLEC 441
Cdd:COG2520  312 EKRRVKSYSPGVYHVVVDVRV 332
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
184-334 5.65e-35

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 128.62  E-value: 5.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  184 TRTPAVTLLLGDHGWVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGAAFVHA 263
Cdd:pfam02475  49 FRTPRYEVLAGSDTETIHKENGCRFKVDVAKVYWSPRLIAERERIAKLVEPGEVVVDMFAGIGPFSIPIAKHSKARRVYA 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157388919  264 CEWNPHAVVALRNNLEINGVADRCQIHFGDNRKLKLSNIADRVILGLIPSSEEGWPIACQVLRQdaGGILH 334
Cdd:pfam02475 129 IELNPESYKYLKENIKLNKVEDVVKPILGDVREVILEDVADRVVMNLPGSAHEFLDKAFAAVRD--GGVIH 197
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
234-308 2.85e-07

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 52.49  E-value: 2.85e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157388919 234 AGEVLVDLYAGIGYFTLPFLvhAGAAFVHACEWNPHAVVALRNNLEINGVaDRCQIHFGD----NRKLKLSNIADRVIL 308
Cdd:COG2265  233 GGERVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDleevLPELLWGGRPDVVVL 308
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
235-307 3.45e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.11  E-value: 3.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157388919 235 GEVLVDLYAGIGYFTLpFLVHAGAAFVHACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKLKLSNIADRVI 307
Cdd:COG4076   36 GDVVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVII 107
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
239-323 6.43e-04

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 41.33  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 239 VDLYAGIGYFTLPFlVHAGAAFVHACEWNPHAVVALRNNLeingvaDRCQIHFGDNRKLKLSNIADR--VILGlipssee 316
Cdd:COG0270    7 IDLFAGAGGLSLGF-EKAGFEVVFAVEIDPDACETYRANF------PEAKVIEGDIRDIDPEELIPDvdLLIG------- 72

                 ....*..
gi 157388919 317 GWPiaCQ 323
Cdd:COG0270   73 GPP--CQ 77
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
238-336 8.09e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 38.95  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919 238 LVDLYAGIGYFTLPfLVHAGAAFVHACEWNPHAVVALRNNlEINGVADRCQIHFGDNRKLKLSNI--ADRVIL-GLIPSS 314
Cdd:cd02440    2 VLDLGCGTGALALA-LASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADesFDVIISdPPLHHL 79
                         90       100
                 ....*....|....*....|....*..
gi 157388919 315 EEGWPiacQVLRQ-----DAGGILHIH 336
Cdd:cd02440   80 VEDLA---RFLEEarrllKPGGVLVLT 103
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
149-285 1.36e-03

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 40.96  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388919  149 QAKQWKNLGPELWETVALALGVQRlAKRGRVSPDGTRTpavtlLLGDHGWVEhVDNGIRYKFD----------VTQCMFs 218
Cdd:TIGR00479 210 KEELDLYLQPDSPDVKSICQNINP-EKTNVIFGEETEV-----IAGEMPIYD-KSGDLSFTFSardfiqvnsgQNEKLV- 281
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157388919  219 fgniTEKLRVASLSCAgEVLVDLYAGIGYFTLPflVHAGAAFVHACEWNPHAVVALRNNLEINGVAD 285
Cdd:TIGR00479 282 ----DRALEWLELQGE-ERVLDAYCGMGTFTLP--LAKQAKSVVGVEGVPESVEKAQQNAELNGIAN 341
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
238-308 2.65e-03

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 39.62  E-value: 2.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157388919  238 LVDLYAGIGYFTLPFLVhAGAAFVHACEWNPHAVVALRNNLEIngvadrcQIHFGDNRKLKLSNIADRVIL 308
Cdd:TIGR00675   1 FIDLFAGIGGIRLGFEQ-AGFKCVFASEIDKYAQKTYEANFGN-------KVPFGDITKISPSDIPDFDIL 63
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
237-283 7.95e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 36.90  E-value: 7.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 157388919  237 VLVDLYAGIGYFTLPFLVHAGAAFVHACEWNPHAVVALRNNLEINGV 283
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNL 47
 
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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