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Conserved domains on  [gi|398366571|ref|NP_010696|]
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phosphoribosylglycinamide formyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core super family cl00395
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 2-214 3.24e-89

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


The actual alignment was detected with superfamily member TIGR00639:

Pssm-ID: 444886 [Multi-domain]  Cd Length: 190  Bit Score: 260.38  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571    2 ARIVVLISGSGSNLQALIDAQKQGqlGEDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYTKgiakedkaarakaRS 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEG--KIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPS-------------RE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   82 QFENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSVpILNLHPALPGCFDGTtHAIEMAWRKCQDEnkpltAGCMVHY 161
Cdd:TIGR00639  66 AFDQAIIEELRAHEVDLVVLAGFMRILGPTFLSRFAGR-ILNIHPSLLPAFPGL-HAVEQALEAGVKE-----SGCTVHY 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366571  162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEATYKVLQQLHK 214
Cdd:TIGR00639 139 VDEEVDTGPIIAQAKVPILP-EDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
 
Name Accession Description Interval E-value
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-214 3.24e-89

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 260.38  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571    2 ARIVVLISGSGSNLQALIDAQKQGqlGEDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYTKgiakedkaarakaRS 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEG--KIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPS-------------RE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   82 QFENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSVpILNLHPALPGCFDGTtHAIEMAWRKCQDEnkpltAGCMVHY 161
Cdd:TIGR00639  66 AFDQAIIEELRAHEVDLVVLAGFMRILGPTFLSRFAGR-ILNIHPSLLPAFPGL-HAVEQALEAGVKE-----SGCTVHY 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366571  162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEATYKVLQQLHK 214
Cdd:TIGR00639 139 VDEEVDTGPIIAQAKVPILP-EDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-205 5.52e-70

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 211.38  E-value: 5.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571    2 ARIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYTkgiakedkaarakARS 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQ--DADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLT-------------PRS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   82 QFENDLAKLVLEEKPDVIICAGWLLILGSTFLsQLQSVPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVHY 161
Cdd:pfam00551  66 LFDQELADALRALAADVIVLAGYMRILPPEFL-QAPPGGILNIHPSLLPRFRG-AAPIQRALEAGDKE-----TGVTIHF 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 398366571  162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEAT 205
Cdd:pfam00551 139 VDEGLDTGPILAQKAVPILP-DDTAETLYNRVADLEHKALPRVL 181
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-208 6.54e-69

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 208.78  E-value: 6.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   3 RIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYtkgiakedkaaraKARSQ 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKL--NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDF-------------PSREE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  83 FENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSvPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVHYV 162
Cdd:cd08645   66 FDEALLELLKEYKVDLIVLAGFMRILSPEFLEAFPG-RIINIHPSLLPKFYG-LHAHEAALEAGVKV-----TGCTVHFV 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 398366571 163 IEEVDKGEPLVVKKLEIIPGeETLEQYEQRVHDAEHIAIVEATYKV 208
Cdd:cd08645  139 DEEVDTGPIIAQAAVPVLPG-DTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-211 2.31e-55

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 174.84  E-value: 2.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   1 MARIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYtkgiakEDKAArakar 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDL--PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDF------PSREA----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  81 sqFENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSvPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVH 160
Cdd:COG0299   68 --FDAALLEALDAYGPDLVVLAGFMRILTPEFVRAFPG-RIINIHPSLLPAFPG-LHAHRQALEAGVKV-----TGCTVH 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366571 161 YVIEEVDKGEPLVVKKLEIIPGeETLEQYEQRVHDAEHIAIVEATYKVLQQ 211
Cdd:COG0299  139 FVDEEVDTGPIIAQAAVPVLPD-DTEETLAARILEQEHRLYPEAIRLLAEG 188
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-205 1.86e-13

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 66.25  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   3 RIVVLISGSGSNLQALIDAQKQGQLGEDahIVSVISSSKKAYGLTRAADNNIPTKVcslYPYTKGiakEDKAARAkarsq 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGD--VVVVVTNKPGCGGAEYARENGIPVLV---YPKTKG---EPDGLSP----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  83 feNDLAKLVLEEKPDVIICAGWLLILGSTfLSQLQSVPILNLHPALPGCFDGT-THAIEMawRKCQDENKPLTAGCMVHY 161
Cdd:PLN02331  68 --DELVDALRGAGVDFVLLAGYLKLIPVE-LVRAYPRSILNIHPALLPAFGGKgYYGIKV--HKAVIASGARYSGPTVHF 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 398366571 162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEAT 205
Cdd:PLN02331 143 VDEHYDTGRILAQRVVPVLA-TDTPEELAARVLHEEHQLYVEVV 185
 
Name Accession Description Interval E-value
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 2-214 3.24e-89

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 260.38  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571    2 ARIVVLISGSGSNLQALIDAQKQGqlGEDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYTKgiakedkaarakaRS 81
Cdd:TIGR00639   1 KRIVVLISGNGSNLQAIIDACKEG--KIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPS-------------RE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   82 QFENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSVpILNLHPALPGCFDGTtHAIEMAWRKCQDEnkpltAGCMVHY 161
Cdd:TIGR00639  66 AFDQAIIEELRAHEVDLVVLAGFMRILGPTFLSRFAGR-ILNIHPSLLPAFPGL-HAVEQALEAGVKE-----SGCTVHY 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 398366571  162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEATYKVLQQLHK 214
Cdd:TIGR00639 139 VDEEVDTGPIIAQAKVPILP-EDTEETLEQRIHKQEHRIYPLAIAWFAQGRLK 190
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 2-205 5.52e-70

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 211.38  E-value: 5.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571    2 ARIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYTkgiakedkaarakARS 81
Cdd:pfam00551   1 MKIAVLISGTGSNLQALIDALRKGGQ--DADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLT-------------PRS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   82 QFENDLAKLVLEEKPDVIICAGWLLILGSTFLsQLQSVPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVHY 161
Cdd:pfam00551  66 LFDQELADALRALAADVIVLAGYMRILPPEFL-QAPPGGILNIHPSLLPRFRG-AAPIQRALEAGDKE-----TGVTIHF 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 398366571  162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEAT 205
Cdd:pfam00551 139 VDEGLDTGPILAQKAVPILP-DDTAETLYNRVADLEHKALPRVL 181
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 3-208 6.54e-69

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 208.78  E-value: 6.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   3 RIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYtkgiakedkaaraKARSQ 82
Cdd:cd08645    1 RIAVLASGSGSNLQALIDAIKSGKL--NAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDF-------------PSREE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  83 FENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSvPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVHYV 162
Cdd:cd08645   66 FDEALLELLKEYKVDLIVLAGFMRILSPEFLEAFPG-RIINIHPSLLPKFYG-LHAHEAALEAGVKV-----TGCTVHFV 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 398366571 163 IEEVDKGEPLVVKKLEIIPGeETLEQYEQRVHDAEHIAIVEATYKV 208
Cdd:cd08645  139 DEEVDTGPIIAQAAVPVLPG-DTPETLAERIHALEHRLYPEAIKLL 183
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 1-211 2.31e-55

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 174.84  E-value: 2.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   1 MARIVVLISGSGSNLQALIDAQKQGQLgeDAHIVSVISSSKKAYGLTRAADNNIPTKVCSLYPYtkgiakEDKAArakar 80
Cdd:COG0299    1 MKRIAVLISGRGSNLQALIDAIEAGDL--PAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDF------PSREA----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  81 sqFENDLAKLVLEEKPDVIICAGWLLILGSTFLSQLQSvPILNLHPALPGCFDGtTHAIEMAWRKCQDEnkpltAGCMVH 160
Cdd:COG0299   68 --FDAALLEALDAYGPDLVVLAGFMRILTPEFVRAFPG-RIINIHPSLLPAFPG-LHAHRQALEAGVKV-----TGCTVH 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366571 161 YVIEEVDKGEPLVVKKLEIIPGeETLEQYEQRVHDAEHIAIVEATYKVLQQ 211
Cdd:COG0299  139 FVDEEVDTGPIIAQAAVPVLPD-DTEETLAARILEQEHRLYPEAIRLLAEG 188
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 3-205 1.86e-13

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 66.25  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571   3 RIVVLISGSGSNLQALIDAQKQGQLGEDahIVSVISSSKKAYGLTRAADNNIPTKVcslYPYTKGiakEDKAARAkarsq 82
Cdd:PLN02331   1 KLAVFVSGGGSNFRAIHDACLDGRVNGD--VVVVVTNKPGCGGAEYARENGIPVLV---YPKTKG---EPDGLSP----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366571  83 feNDLAKLVLEEKPDVIICAGWLLILGSTfLSQLQSVPILNLHPALPGCFDGT-THAIEMawRKCQDENKPLTAGCMVHY 161
Cdd:PLN02331  68 --DELVDALRGAGVDFVLLAGYLKLIPVE-LVRAYPRSILNIHPALLPAFGGKgYYGIKV--HKAVIASGARYSGPTVHF 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 398366571 162 VIEEVDKGEPLVVKKLEIIPgEETLEQYEQRVHDAEHIAIVEAT 205
Cdd:PLN02331 143 VDEHYDTGRILAQRVVPVLA-TDTPEELAARVLHEEHQLYVEVV 185
 
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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