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Conserved domains on  [gi|930173893|ref|WP_054175770|]
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Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC [Mycoplasmoides pneumoniae]

Protein Classification

PRK12821 family protein( domain architecture ID 11486219)

PRK12821 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
1-479 0e+00

aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional


:

Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 671.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893   1 MDKLinKPQPLTSDISTSGFIYFAVVFVAIMGYLLFKNLLFLFFFKRYPKNTPKIGVGNITTIAMIIAVAVSIVLVLMAL 80
Cdd:PRK12821   1 MGEI--KTESFTSDISTSGFIYFAVVFGLILVYLLFKNLLFLFFFKRYPKNTPKIGVINITTIAMIIAVAVSIVLVLMAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  81 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIVGIFSAATIDFLTVIFSGGVFNVGYVLGAILTGMIAGILREVLIST 160
Cdd:PRK12821  79 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIIGIFSAATIDFLTVIFSGGVFNYGYVLGAILTGMIAGILREVLIST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 161 ALLHNRNLSDFAYLVLSIGMVIAAFLITQFFVLGISNNLKEIKGDEEFRLKFNAPPIVFELSLTQYANILLYFTIAIVIA 240
Cdd:PRK12821 159 KYLKNRNLSDFAYLVLSVGMVIASFLLTQFFVISVTTNLPEIRINGGFDLSFNAVSQTFKISLVVYTWIILYFGIGIIIF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 241 MLVLYIVLLVKQRHLSFEHSRFFYRSYKHANHQFTLFVLTKENWFYLILNVITLASTSLLMINIAFIPIFDTQTTGQTYE 320
Cdd:PRK12821 239 MWVLYLVWKLKQPHNAYSLSGFFHRRYKHANHQFTLFVLTKENWFYLILNVITLAGTSLLMINIAFIPIFDTQTTGQTYA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 321 FWLLARLLFAPVIFLLDIIVIYPILLLLTPLMLKGFKTAVSKNQRKTLKQSFTDLQSVVLPIINKRKHQQLRQEELKRLA 400
Cdd:PRK12821 319 FWLLIRLLFAPAIFLLDIIVIYPILLLLTPIMLKGFKTELSETQTKGIKKSFSDLQSPLFPKHWTSKKQQLNKDELKKLA 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930173893 401 RATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSPTPLRKDKVIVEKHPEKLLANCKEMSVGFVKV 479
Cdd:PRK12821 399 RLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKPMYAPFSNSPTPLRKDKDVVQKHQKILLKNCKETLGGFVKV 477
 
Name Accession Description Interval E-value
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
1-479 0e+00

aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional


Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 671.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893   1 MDKLinKPQPLTSDISTSGFIYFAVVFVAIMGYLLFKNLLFLFFFKRYPKNTPKIGVGNITTIAMIIAVAVSIVLVLMAL 80
Cdd:PRK12821   1 MGEI--KTESFTSDISTSGFIYFAVVFGLILVYLLFKNLLFLFFFKRYPKNTPKIGVINITTIAMIIAVAVSIVLVLMAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  81 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIVGIFSAATIDFLTVIFSGGVFNVGYVLGAILTGMIAGILREVLIST 160
Cdd:PRK12821  79 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIIGIFSAATIDFLTVIFSGGVFNYGYVLGAILTGMIAGILREVLIST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 161 ALLHNRNLSDFAYLVLSIGMVIAAFLITQFFVLGISNNLKEIKGDEEFRLKFNAPPIVFELSLTQYANILLYFTIAIVIA 240
Cdd:PRK12821 159 KYLKNRNLSDFAYLVLSVGMVIASFLLTQFFVISVTTNLPEIRINGGFDLSFNAVSQTFKISLVVYTWIILYFGIGIIIF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 241 MLVLYIVLLVKQRHLSFEHSRFFYRSYKHANHQFTLFVLTKENWFYLILNVITLASTSLLMINIAFIPIFDTQTTGQTYE 320
Cdd:PRK12821 239 MWVLYLVWKLKQPHNAYSLSGFFHRRYKHANHQFTLFVLTKENWFYLILNVITLAGTSLLMINIAFIPIFDTQTTGQTYA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 321 FWLLARLLFAPVIFLLDIIVIYPILLLLTPLMLKGFKTAVSKNQRKTLKQSFTDLQSVVLPIINKRKHQQLRQEELKRLA 400
Cdd:PRK12821 319 FWLLIRLLFAPAIFLLDIIVIYPILLLLTPIMLKGFKTELSETQTKGIKKSFSDLQSPLFPKHWTSKKQQLNKDELKKLA 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930173893 401 RATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSPTPLRKDKVIVEKHPEKLLANCKEMSVGFVKV 479
Cdd:PRK12821 399 RLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKPMYAPFSNSPTPLRKDKDVVQKHQKILLKNCKETLGGFVKV 477
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
394-479 1.00e-15

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this model does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This model has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129241 [Multi-domain]  Cd Length: 93  Bit Score: 72.33  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  394 EELKRLARATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMS 473
Cdd:TIGR00135   4 EEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEIS-NVLREDEPEEPLSRDDILKNAPEKE 82

                  ....*.
gi 930173893  474 VGFVKV 479
Cdd:TIGR00135  83 DGFIKV 88
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
394-479 2.01e-13

Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440485 [Multi-domain]  Cd Length: 95  Bit Score: 65.89  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 394 EELKRLARATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMS 473
Cdd:COG0721    6 EEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAPETE 84

                 ....*.
gi 930173893 474 VGFVKV 479
Cdd:COG0721   85 DGYFKV 90
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
409-479 2.19e-12

Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C subunits. The Glu-tRNA Gln amidotransferase enzyme itself is an important translational fidelity mechanism replacing incorrectly charged Glu-tRNAGln with the correct Gln-tRANGln via transmidation of the misacylated Glu-tRNAGln. This activity supplements the lack of glutaminyl-tRNA synthetase activity in gram-positive eubacterteria, cyanobacteria, Archaea, and organelles.


Pssm-ID: 460651 [Multi-domain]  Cd Length: 70  Bit Score: 62.14  E-value: 2.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930173893  409 EGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMSVGFVKV 479
Cdd:pfam02686   1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLT-NVLREDEVTESLDREEALANAPETEDGFFKV 70
 
Name Accession Description Interval E-value
PRK12821 PRK12821
aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional
1-479 0e+00

aspartyl/glutamyl-tRNA amidotransferase subunit C-like protein; Provisional


Pssm-ID: 237216 [Multi-domain]  Cd Length: 477  Bit Score: 671.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893   1 MDKLinKPQPLTSDISTSGFIYFAVVFVAIMGYLLFKNLLFLFFFKRYPKNTPKIGVGNITTIAMIIAVAVSIVLVLMAL 80
Cdd:PRK12821   1 MGEI--KTESFTSDISTSGFIYFAVVFGLILVYLLFKNLLFLFFFKRYPKNTPKIGVINITTIAMIIAVAVSIVLVLMAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  81 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIVGIFSAATIDFLTVIFSGGVFNVGYVLGAILTGMIAGILREVLIST 160
Cdd:PRK12821  79 AGGLAAALFRGYPGFRVTLELILVKISGLLFGPIIGIFSAATIDFLTVIFSGGVFNYGYVLGAILTGMIAGILREVLIST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 161 ALLHNRNLSDFAYLVLSIGMVIAAFLITQFFVLGISNNLKEIKGDEEFRLKFNAPPIVFELSLTQYANILLYFTIAIVIA 240
Cdd:PRK12821 159 KYLKNRNLSDFAYLVLSVGMVIASFLLTQFFVISVTTNLPEIRINGGFDLSFNAVSQTFKISLVVYTWIILYFGIGIIIF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 241 MLVLYIVLLVKQRHLSFEHSRFFYRSYKHANHQFTLFVLTKENWFYLILNVITLASTSLLMINIAFIPIFDTQTTGQTYE 320
Cdd:PRK12821 239 MWVLYLVWKLKQPHNAYSLSGFFHRRYKHANHQFTLFVLTKENWFYLILNVITLAGTSLLMINIAFIPIFDTQTTGQTYA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 321 FWLLARLLFAPVIFLLDIIVIYPILLLLTPLMLKGFKTAVSKNQRKTLKQSFTDLQSVVLPIINKRKHQQLRQEELKRLA 400
Cdd:PRK12821 319 FWLLIRLLFAPAIFLLDIIVIYPILLLLTPIMLKGFKTELSETQTKGIKKSFSDLQSPLFPKHWTSKKQQLNKDELKKLA 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930173893 401 RATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSPTPLRKDKVIVEKHPEKLLANCKEMSVGFVKV 479
Cdd:PRK12821 399 RLVMFDLDDAELEKLQVEFKDITSSFKQVEKIDTTNVKPMYAPFSNSPTPLRKDKDVVQKHQKILLKNCKETLGGFVKV 477
PRK09609 PRK09609
hypothetical protein; Provisional
53-344 3.32e-18

hypothetical protein; Provisional


Pssm-ID: 181988  Cd Length: 312  Bit Score: 85.09  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  53 PKIGVGNITTIAMIIAVAVSIVLVLmalaggLAAALFRGYPGFRVTLELILVKISGLLFGPIVGIFSAATIDFLTVIFSG 132
Cdd:PRK09609   2 PKWTIKKISFVAILIAISVVFLIIG------VRLAPFRALPTFKISFIGLPIKITGFIFGPIVGFFTGLLSDLISFLFVP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 133 GVFNVGYVLGAILTGMIAGILREVLISTallhNRNLSDFAYLVLSIGMVIAAFLITQFFVLGISNNLKEIKGDEEFrLKF 212
Cdd:PRK09609  76 GVYHPYYTLAAMVYGFIPGIVGWFFFKF----GKKFFGKESRIKRYDNKIFKQKEQYDFALENPNSEKIQKIKQKI-ILL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 213 NAPPIVFELSLTQ--YANILLYFTIAIVIAMLVLYIVLLVKQRHLSFEHSRFFYRS----YKHANHQFTLFV-------- 278
Cdd:PRK09609 151 EKKKKKLEKTNEEksLLNFSWIAALIILVIIILFIYFVVGFLDPDFFIQSFSFIKNkrslMILIISGFILMIifviwarf 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 930173893 279 LTKENWFYLILNVITLaSTSLLMINIAFIPIFDTQTTGQTYEFWLLARLLFAPVIFLLDIIVIYPI 344
Cdd:PRK09609 231 FIKPKRFLTIAPIVIF-SALLEPINVILLSSADAQSLGLDFDTWLFIHIITSPIKIWFNLSIIYFT 295
gatC TIGR00135
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many ...
394-479 1.00e-15

aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Archaea, organelles, and many bacteria charge Gln-tRNA by first misacylating it with Glu and then amidating Glu to Gln. This small protein is part of the amidotransferase heterotrimer and appears to be important to the stability of the amidase subunit encode by gatA, but its function may not be required in every organism that expresses gatA and gatB. The seed alignment for this model does not include any eukaryotic sequence and is not guaranteed to find eukaryotic examples, although it does find some. Saccharomyces cerevisiae, which expresses the amidotransferase for mitochondrial protein translation, seems to lack a gatC ortholog. This model has been revised to remove the candidate sequence from Methanococcus jannaschii, now part of a related model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129241 [Multi-domain]  Cd Length: 93  Bit Score: 72.33  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  394 EELKRLARATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMS 473
Cdd:TIGR00135   4 EEVKHLAKLARLELSEEEAESFAGDLDKILGFVEQLNEVDTENVEPMTHPLEIS-NVLREDEPEEPLSRDDILKNAPEKE 82

                  ....*.
gi 930173893  474 VGFVKV 479
Cdd:TIGR00135  83 DGFIKV 88
GatC COG0721
Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and ...
394-479 2.01e-13

Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit [Translation, ribosomal structure and biogenesis]; Asp-tRNAAsn/Glu-tRNAGln amidotransferase C subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440485 [Multi-domain]  Cd Length: 95  Bit Score: 65.89  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 394 EELKRLARATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMS 473
Cdd:COG0721    6 EEVEHIAKLARLELSEEELERLAGQLNDILDYVEQLNEVDTEGVEPTAHPLDLT-NVLREDEVTESLDREEALANAPETE 84

                 ....*.
gi 930173893 474 VGFVKV 479
Cdd:COG0721   85 DGYFKV 90
Glu-tRNAGln pfam02686
Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C ...
409-479 2.19e-12

Glu-tRNAGln amidotransferase C subunit; This is a family of Glu-tRNAGln amidotransferase C subunits. The Glu-tRNA Gln amidotransferase enzyme itself is an important translational fidelity mechanism replacing incorrectly charged Glu-tRNAGln with the correct Gln-tRANGln via transmidation of the misacylated Glu-tRNAGln. This activity supplements the lack of glutaminyl-tRNA synthetase activity in gram-positive eubacterteria, cyanobacteria, Archaea, and organelles.


Pssm-ID: 460651 [Multi-domain]  Cd Length: 70  Bit Score: 62.14  E-value: 2.19e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930173893  409 EGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANCKEMSVGFVKV 479
Cdd:pfam02686   1 EEELEEFAKQLNDILDYVEQLNEVDTEGVEPTSHPLDLT-NVLREDEVTESLDREEALANAPETEDGFFKV 70
gatC PRK00034
Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;
390-479 2.69e-11

Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC;


Pssm-ID: 178810 [Multi-domain]  Cd Length: 95  Bit Score: 59.83  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893 390 QLRQEELKRLARATHFDLTEGEMEKLLVEFKTITQSFDRVMNIDTTSVEPMYAPFNTSpTPLRKDKVIVEKHPEKLLANC 469
Cdd:PRK00034   2 AITREEVKHLAKLARLELSEEELEKFAGQLNKILDFVEQLNEVDTEGVEPTTHPLDMK-NVLREDVVTESLPREEALKNA 80
                         90
                 ....*....|
gi 930173893 470 KEMSVGFVKV 479
Cdd:PRK00034  81 PESEDGYFKV 90
ECF_S_folT_fam TIGR04518
ECF transporter S component, folate family; Members of this model are the multiple ...
54-188 1.49e-07

ECF transporter S component, folate family; Members of this model are the multiple membrane-spanning S (specificity) component of ECF (energy coupling factor) type uptake transporters. All seed members were found in the vicinity of the bifunctional enzyme folC, involved in making active cofactor from imported folate. However, some species have multiple members of this family, suggesting some diversity of function. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275311 [Multi-domain]  Cd Length: 162  Bit Score: 51.03  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893   54 KIGVGNITTIAMIIAVAV--SIVLVLMAlagglaaalfrgyPGFRVTLELILVKISGLLFGPIVGIFSAATIDFLTVIFS 131
Cdd:TIGR04518   1 KFTVKNLTILALLVALSIilSRFLSIQT-------------GNLRISFGFLPVILAGMLFGPVAGAIVGAVADLLGCMLF 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 930173893  132 G-GVFNVGYVLGAILTGMIAGILREvlistallHNRNLSDFAYLVLS--IGMVIAAFLIT 188
Cdd:TIGR04518  68 GyGTFFPGFTLSAALTGLIYGLFFY--------KKKNKKLFLRLAAAvvIVQIIISLVLT 119
 
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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