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Conserved domains on  [gi|446950885|ref|WP_001028141|]
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MULTISPECIES: bifunctional aminoglycoside N-acetyltransferase AAC(6')-Ie/aminoglycoside O-phosphotransferase APH(2'')-Ia [Bacteria]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 203-415 3.95e-32

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


:

Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 120.10  E-value: 3.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 203 DSIEIIGSGYDSVAYLVNN--EYIFKTKFSTNKKkGYAKEKAIYNFLNTNleTNVKIPNIEYSYISDELSILGYKEIKGT 280
Cdd:cd05120    1 ISVKLIKEGGDNKVYLLGDprEYVLKIGPPRLKK-DLEKEAAMLQLLAGK--LSLPVPKVYGFGESDGWEYLLMERIEGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 281 FLTPEIYStMSEEEQNLLKRDIASFLRQMHGLDYTdisectidnkqnvleeyillretiyndltdiekdyiesfmerlna 360
Cdd:cd05120   78 TLSEVWPR-LSEEEKEKIADQLAEILAALHRIDSS--------------------------------------------- 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446950885 361 ttvfegkkCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEE 415
Cdd:cd05120  112 --------VLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-181 1.27e-19

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 85.82  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  10 IRTLIDDDFPLMLKWLTDERVLEFYDGRDkkYTLESLK---KHYTEPWEDE---VFRVIIEYNNVPIGYGQIYKMydely 83
Cdd:COG1670   10 LRPLRPEDAEALAELLNDPEVARYLPGPP--YSLEEARawlERLLADWADGgalPFAIEDKEDGELIGVVGLYDI----- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  84 tDYHYPKTdEIVYGMDqfigePNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHE 163
Cdd:COG1670   83 -DRANRSA-EIGYWLA-----PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155

                        170
                 ....*....|....*...
gi 446950885 164 LHEGKKEDCYLMEYRYDD 181
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 302-441 7.26e-11

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05150:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 244  Bit Score: 62.21  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 302 IASFLRQMHGLDYTDiseCTIDNKqnvLEEYI-LLRETIYNDLTDiEKDYIESF--------MERLNATTVFEGKKCLCH 372
Cdd:cd05150   95 LAEALRALHSLPIAD---CPFDRR---LDARLaEARARVEAGLVD-EDDFDEERqgrtaeelLAELEATRPAEEDLVVTH 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446950885 373 NDFSCNHLLLDgNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDI-LRMYG--NIDIEKAKEYQ 441
Cdd:cd05150  168 GDACLPNIILD-PGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERfLDAYGidAPDPERLAYYR 238
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 203-415 3.95e-32

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 120.10  E-value: 3.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 203 DSIEIIGSGYDSVAYLVNN--EYIFKTKFSTNKKkGYAKEKAIYNFLNTNleTNVKIPNIEYSYISDELSILGYKEIKGT 280
Cdd:cd05120    1 ISVKLIKEGGDNKVYLLGDprEYVLKIGPPRLKK-DLEKEAAMLQLLAGK--LSLPVPKVYGFGESDGWEYLLMERIEGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 281 FLTPEIYStMSEEEQNLLKRDIASFLRQMHGLDYTdisectidnkqnvleeyillretiyndltdiekdyiesfmerlna 360
Cdd:cd05120   78 TLSEVWPR-LSEEEKEKIADQLAEILAALHRIDSS--------------------------------------------- 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446950885 361 ttvfegkkCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEE 415
Cdd:cd05120  112 --------VLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 204-440 4.40e-31

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 119.91  E-value: 4.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  204 SIEIIGSGYDSVAYLV---NNEYIFKTKFSTNKKKGYAKEKAIYNFLNTNLETNVkiPNIEYSYISDELSILGYKEIkgT 280
Cdd:pfam01636   1 TLRPISSGASNRTYLVttgDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPV--PRVLAGCTDAELLGLPFLLM--E 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  281 FLTPEIYST-MSEEEQNLLKRDIASFLRQMHGLDYTDISECTIdNKQNVLEEYILLRETIY---NDLTDIEKDYIESFME 356
Cdd:pfam01636  77 YLPGEVLARpLLPEERGALLEALGRALARLHAVDPAALPLAGR-LARLLELLRQLEAALARllaAELLDRLEELEERLLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  357 RLNATTVFEGKKCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDILRMYGNIDIEK 436
Cdd:pfam01636 156 ALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYAR 235


                  ....
gi 446950885  437 AKEY 440
Cdd:pfam01636 236 LREL 239
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-181 1.27e-19

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 85.82  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  10 IRTLIDDDFPLMLKWLTDERVLEFYDGRDkkYTLESLK---KHYTEPWEDE---VFRVIIEYNNVPIGYGQIYKMydely 83
Cdd:COG1670   10 LRPLRPEDAEALAELLNDPEVARYLPGPP--YSLEEARawlERLLADWADGgalPFAIEDKEDGELIGVVGLYDI----- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  84 tDYHYPKTdEIVYGMDqfigePNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHE 163
Cdd:COG1670   83 -DRANRSA-EIGYWLA-----PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155

                        170
                 ....*....|....*...
gi 446950885 164 LHEGKKEDCYLMEYRYDD 181
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 14-164 4.59e-19

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 433280  Cd Length: 145  Bit Score: 83.72  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885   14 IDDDFPLMLKWLTDERVLEFYDGRDkkyTLESLKKHYT----EPWedeVFRVIIEYNNVPIGYGQIYK-MYDELYTDYHY 88
Cdd:pfam13523   2 PEADLELLHRWMNDPRVAFWWMLAG---PLEQVREYLArlaaDPH---SHPYIGLLDGEPFGYFEIYWaKEDRLGEYYDA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446950885   89 PKTDeivYGMDQFIGEPNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIedlPEHEL 164
Cdd:pfam13523  76 RPGD---RGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKV---KEIDL 145
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 191-410 3.43e-12

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 66.68  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 191 YLIEHYFDNFKVDSIEIIGSGYDSVAYLV--NNEYIFKTK-FSTNKKKGYAKEKAIYNFLNTNLEtnVKIPNIeYSYISD 267
Cdd:COG3173   11 LLAAQLPGLAGLPEVEPLSGGWSNLTYRLdtGDRLVLRRPpRGLASAHDVRREARVLRALAPRLG--VPVPRP-LALGED 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 268 ELSI----LGYKEIKGTFLTPEIySTMSEEEQNLLKRDIASFLRQMHGLDYTDISECtiDNKQNVLEEYILLRETIYN-- 341
Cdd:COG3173   88 GEVIgapfYVMEWVEGETLEDAL-PDLSPAERRALARALGEFLAALHAVDPAAAGLA--DGRPEGLERQLARWRAQLRra 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446950885 342 -DLTDIEKDYIESFMERLNATTVFEGKKCLCHNDFSCNHLLLDGNN-RLTGIIDFGDSGIIDEYCDFIYLL 410
Cdd:COG3173  165 lARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDgRLTAVIDWELATLGDPAADLAYLL 235
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 302-441 7.26e-11

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 62.21  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 302 IASFLRQMHGLDYTDiseCTIDNKqnvLEEYI-LLRETIYNDLTDiEKDYIESF--------MERLNATTVFEGKKCLCH 372
Cdd:cd05150   95 LAEALRALHSLPIAD---CPFDRR---LDARLaEARARVEAGLVD-EDDFDEERqgrtaeelLAELEATRPAEEDLVVTH 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446950885 373 NDFSCNHLLLDgNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDI-LRMYG--NIDIEKAKEYQ 441
Cdd:cd05150  168 GDACLPNIILD-PGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERfLDAYGidAPDPERLAYYR 238
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
329-430 4.63e-06

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 46.70  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 329 LEEYILLRETIYNDLtdieKDYIESFMERLNAttvFEGKKCLCHNDFSCNHLLLDGNNRLTgIIDFGDSGIIDEYCDFIY 408
Cdd:COG0510   17 LERYLALGPRDLPEL----LRRLEELERALAA---RPLPLVLCHGDLHPGNFLVTDDGRLY-LIDWEYAGLGDPAFDLAA 88

                         90       100
                 ....*....|....*....|....*
gi 446950885 409 LL---EDSEEEIgtnfgEDILRMYG 430
Cdd:COG0510   89 LLveyGLSPEQA-----EELLEAYG 108
PRK10562 PRK10562
putative acetyltransferase; Provisional
 99-157 2.16e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.51  E-value: 2.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446950885  99 DQFIG----EPNYWSKGIGT---RYIKLIFEFLKkernanaviLDPHKNNPRAIRAYQKSGFRIIE 157
Cdd:PRK10562  68 GRFVGalfvAPKAVRRGIGKalmQHVQQRYPHLS---------LEVYQKNQRAVNFYHAQGFRIVD 124
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 203-415 3.95e-32

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 120.10  E-value: 3.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 203 DSIEIIGSGYDSVAYLVNN--EYIFKTKFSTNKKkGYAKEKAIYNFLNTNleTNVKIPNIEYSYISDELSILGYKEIKGT 280
Cdd:cd05120    1 ISVKLIKEGGDNKVYLLGDprEYVLKIGPPRLKK-DLEKEAAMLQLLAGK--LSLPVPKVYGFGESDGWEYLLMERIEGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 281 FLTPEIYStMSEEEQNLLKRDIASFLRQMHGLDYTdisectidnkqnvleeyillretiyndltdiekdyiesfmerlna 360
Cdd:cd05120   78 TLSEVWPR-LSEEEKEKIADQLAEILAALHRIDSS--------------------------------------------- 111

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446950885 361 ttvfegkkCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEE 415
Cdd:cd05120  112 --------VLTHGDLHPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 204-440 4.40e-31

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 119.91  E-value: 4.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  204 SIEIIGSGYDSVAYLV---NNEYIFKTKFSTNKKKGYAKEKAIYNFLNTNLETNVkiPNIEYSYISDELSILGYKEIkgT 280
Cdd:pfam01636   1 TLRPISSGASNRTYLVttgDGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPV--PRVLAGCTDAELLGLPFLLM--E 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  281 FLTPEIYST-MSEEEQNLLKRDIASFLRQMHGLDYTDISECTIdNKQNVLEEYILLRETIY---NDLTDIEKDYIESFME 356
Cdd:pfam01636  77 YLPGEVLARpLLPEERGALLEALGRALARLHAVDPAALPLAGR-LARLLELLRQLEAALARllaAELLDRLEELEERLLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  357 RLNATTVFEGKKCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDILRMYGNIDIEK 436
Cdd:pfam01636 156 ALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGYAR 235


                  ....
gi 446950885  437 AKEY 440
Cdd:pfam01636 236 LREL 239
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-181 1.27e-19

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 85.82  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  10 IRTLIDDDFPLMLKWLTDERVLEFYDGRDkkYTLESLK---KHYTEPWEDE---VFRVIIEYNNVPIGYGQIYKMydely 83
Cdd:COG1670   10 LRPLRPEDAEALAELLNDPEVARYLPGPP--YSLEEARawlERLLADWADGgalPFAIEDKEDGELIGVVGLYDI----- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  84 tDYHYPKTdEIVYGMDqfigePNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHE 163
Cdd:COG1670   83 -DRANRSA-EIGYWLA-----PAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155

                        170
                 ....*....|....*...
gi 446950885 164 LHEGKKEDCYLMEYRYDD 181
Cdd:COG1670  156 VIDGRYRDHVLYSLLREE 173
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 14-164 4.59e-19

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 433280  Cd Length: 145  Bit Score: 83.72  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885   14 IDDDFPLMLKWLTDERVLEFYDGRDkkyTLESLKKHYT----EPWedeVFRVIIEYNNVPIGYGQIYK-MYDELYTDYHY 88
Cdd:pfam13523   2 PEADLELLHRWMNDPRVAFWWMLAG---PLEQVREYLArlaaDPH---SHPYIGLLDGEPFGYFEIYWaKEDRLGEYYDA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446950885   89 PKTDeivYGMDQFIGEPNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIedlPEHEL 164
Cdd:pfam13523  76 RPGD---RGIHLLIGEPAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKV---KEIDL 145
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 191-410 3.43e-12

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 66.68  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 191 YLIEHYFDNFKVDSIEIIGSGYDSVAYLV--NNEYIFKTK-FSTNKKKGYAKEKAIYNFLNTNLEtnVKIPNIeYSYISD 267
Cdd:COG3173   11 LLAAQLPGLAGLPEVEPLSGGWSNLTYRLdtGDRLVLRRPpRGLASAHDVRREARVLRALAPRLG--VPVPRP-LALGED 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 268 ELSI----LGYKEIKGTFLTPEIySTMSEEEQNLLKRDIASFLRQMHGLDYTDISECtiDNKQNVLEEYILLRETIYN-- 341
Cdd:COG3173   88 GEVIgapfYVMEWVEGETLEDAL-PDLSPAERRALARALGEFLAALHAVDPAAAGLA--DGRPEGLERQLARWRAQLRra 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446950885 342 -DLTDIEKDYIESFMERLNATTVFEGKKCLCHNDFSCNHLLLDGNN-RLTGIIDFGDSGIIDEYCDFIYLL 410
Cdd:COG3173  165 lARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDgRLTAVIDWELATLGDPAADLAYLL 235
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-154 1.08e-11

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 62.36  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885    8 ICIRTLIDDDFPLMLKWLTDERVLEFYDG--RDKKYTLESLKKHYTEPWEDEVFR-VIIEYNNVPIGYGQIYKMYDElyt 84
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPwpLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIGSIGLYDIDGE--- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885   85 dyhyPKTDEIVYGMDqfigePNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFR 154
Cdd:pfam13302  79 ----PERAELGYWLG-----PDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 302-441 7.26e-11

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 62.21  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 302 IASFLRQMHGLDYTDiseCTIDNKqnvLEEYI-LLRETIYNDLTDiEKDYIESF--------MERLNATTVFEGKKCLCH 372
Cdd:cd05150   95 LAEALRALHSLPIAD---CPFDRR---LDARLaEARARVEAGLVD-EDDFDEERqgrtaeelLAELEATRPAEEDLVVTH 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446950885 373 NDFSCNHLLLDgNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDI-LRMYG--NIDIEKAKEYQ 441
Cdd:cd05150  168 GDACLPNIILD-PGRFSGFIDLGRLGVADRYQDLALAVRSLRENLGGEEYAERfLDAYGidAPDPERLAYYR 238
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 41-153 1.41e-10

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 58.68  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885   41 YTLESLKKHYTEPWEDEVFRVIIEYNNVPIGYGQIYKMYDElytdyhypktdEIVYGMDQFIGEPNYWSKGIGTRYIKLI 120
Cdd:pfam00583  16 WPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDE-----------PPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446950885  121 FEFLKkERNANAVILDPHKNNPRAIRAYQKSGF 153
Cdd:pfam00583  85 LEWAR-ERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-178 9.06e-10

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.31  E-value: 9.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  10 IRTLIDDDFPLML---KWLTDERVLEFYDGRDkkyTLESLKKHYTEPWEDEVFRVIIEYNNVPIGYGQiykmYDELYTDY 86
Cdd:COG1247    4 IRPATPEDAPAIAaiyNEAIAEGTATFETEPP---SEEEREAWFAAILAPGRPVLVAEEDGEVVGFAS----LGPFRPRP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  87 HYPKTDEI-VYgmdqfIgEPNYWSKGIGTRYIKLIFEFLKKE--RNANAVILDPhknNPRAIRAYQKSGFRIIEDLPEHE 163
Cdd:COG1247   77 AYRGTAEEsIY-----V-DPDARGRGIGRALLEALIERARARgyRRLVAVVLAD---NEASIALYEKLGFEEVGTLPEVG 147

                        170
                 ....*....|....*
gi 446950885 164 LHEGKKEDCYLMEYR 178
Cdd:COG1247  148 FKFGRWLDLVLMQKR 162
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 51-170 1.36e-09

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  51 TEPWEDEVFR----------VIIEYNNVPIGYGQIyKMYDelytdyhypktDEIVYgMDQFIGEPNYWSKGIGtryiKLI 120
Cdd:COG0454   17 IEALDAELKAmegslagaefIAVDDKGEPIGFAGL-RRLD-----------DKVLE-LKRLYVLPEYRGKGIG----KAL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446950885 121 FEFLK---KERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHEGKKE 170
Cdd:COG0454   80 LEALLewaRERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-178 4.51e-08

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 50.42  E-value: 4.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446950885 105 PNYWSKGIGTRYIKLIFEFLKkERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHElhegkKEDCYLMEYR 178
Cdd:COG0456   23 PEYRGRGIGRALLEAALERAR-ERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY-----GDDALVMEKE 90
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
329-430 4.63e-06

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 46.70  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 329 LEEYILLRETIYNDLtdieKDYIESFMERLNAttvFEGKKCLCHNDFSCNHLLLDGNNRLTgIIDFGDSGIIDEYCDFIY 408
Cdd:COG0510   17 LERYLALGPRDLPEL----LRRLEELERALAA---RPLPLVLCHGDLHPGNFLVTDDGRLY-LIDWEYAGLGDPAFDLAA 88

                         90       100
                 ....*....|....*....|....*
gi 446950885 409 LL---EDSEEEIgtnfgEDILRMYG 430
Cdd:COG0510   89 LLveyGLSPEQA-----EELLEAYG 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
105-166 1.70e-05

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446950885 105 PNYWSKGIGTRYIKLIFEFLKkERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHE 166
Cdd:COG3393   25 PEYRGRGLASALVAALAREAL-ARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFRK 85
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-162 4.81e-05

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.15  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  10 IRTLIDDDFPLMLKWLTDErvlefYDGRDKKYTLESLKKHYtepweDEVFRVIIEYNNVPIGYGQIYKMYDELYTDYHYp 89
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----FGPGREAELVDRLREDP-----AAGLSLVAEDDGEIVGHVALSPVDIDGEGPALL- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446950885  90 ktdeivygmdqfIG----EPNYWSKGIGTRYIKLIFEFLKkERNANAVILDPHknnPRAIRAYQKSGFRIIEDLPEH 162
Cdd:COG3153   70 ------------LGplavDPEYRGQGIGRALMRAALEAAR-ERGARAVVLLGD---PSLLPFYERFGFRPAGELGLT 130
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 293-407 8.18e-04

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 41.07  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 293 EEQNLLKRDIASFLRQMHGLDYTDISECTIDNKQNVLEEYILLRETIYNDLTD-IEKDYIESFMERLNATTVFEGKKCLC 371
Cdd:cd05155   87 ADPAAAAEDLARFLAALHAIDPAGPPNPGRGNPLRGRDLAVRDAEEALAALAGlLDVAAARALWERALAAPAWAGPPVWL 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446950885 372 HNDFSCNHLLLDgNNRLTGIIDFGDSGIIDEYCDFI 407
Cdd:cd05155  167 HGDLHPGNLLVR-DGRLSAVIDFGDLGVGDPACDLA 201
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 61-180 1.91e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 38.43  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885  61 VIIEYNNVPIGYGQIYKMYDE------LYTDyhypktdeivygmdqfigePNYWSKGIGTRYIKLIFEFLKkERNANAVI 134
Cdd:COG1246   31 WVAEEDGEIVGCAALHPLDEDlaelrsLAVH-------------------PDYRGRGIGRRLLEALLAEAR-ELGLKRLF 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446950885 135 LDPhknNPRAIRAYQKSGFRIIEdlpEHELHEGKKEDCYLMEYRYD 180
Cdd:COG1246   91 LLT---TSAAIHFYEKLGFEEID---KEDLPYAKVWQRDSVVMEKD 130
PRK10562 PRK10562
putative acetyltransferase; Provisional
 99-157 2.16e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 38.51  E-value: 2.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446950885  99 DQFIG----EPNYWSKGIGT---RYIKLIFEFLKkernanaviLDPHKNNPRAIRAYQKSGFRIIE 157
Cdd:PRK10562  68 GRFVGalfvAPKAVRRGIGKalmQHVQQRYPHLS---------LEVYQKNQRAVNFYHAQGFRIVD 124
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 280-393 3.45e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 39.14  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446950885 280 TFLTPEIYSTMSEEEQNLLKRDIASFLRQMHGLDYTDISECTIDNKQNVLEEYILLRETIYNDLTDIEKDYIESFMERL- 358
Cdd:cd05154   89 VLPDPLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEGYLERQVDRWRRQLEAAATDPPPALEEALRWLr 168

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446950885 359 -NATTvfEGKKCLCHNDFSCNHLLLDGNNRLTGIID 393
Cdd:cd05154  169 aNLPA--DGRPVLVHGDFRLGNLLFDPDGRVTAVLD 202
 
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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