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Conserved domains on  [gi|1339549014|gb|AUZ17334|]
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neomycin/kanamycin resistance protein, partial [Cloning vector pCA-DEST2300]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aph super family cl43814
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
1-99 1.06e-35

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG3231:

Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 121.56  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIE 78
Cdd:COG3231    58 DRLRWLAGQGLPVPEVLDFGEDDGGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLA 137

                          90       100
                  ....*....|....*....|.
gi 1339549014  79 RARTRMEAGLVDQDDLDEEHQ 99
Cdd:COG3231   138 EARARVAAGLVDPDDFDEERR 158
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
1-99 1.06e-35

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 121.56  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIE 78
Cdd:COG3231    58 DRLRWLAGQGLPVPEVLDFGEDDGGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLA 137

                          90       100
                  ....*....|....*....|.
gi 1339549014  79 RARTRMEAGLVDQDDLDEEHQ 99
Cdd:COG3231   138 EARARVAAGLVDPDDFDEERR 158
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 1-99 1.78e-32

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: 113.06  E-value: 1.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTgVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSH--LAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIE 78
Cdd:cd05150    43 ERLRWLAGK-LPVPEVLDYGSDDGGDWLLTTALPGRDAASLEplLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLA 121

                          90       100
                  ....*....|....*....|.
gi 1339549014  79 RARTRMEAGLVDQDDLDEEHQ 99
Cdd:cd05150   122 EARARVEAGLVDEDDFDEERQ 142
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 1-99 2.11e-05

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: 40.95  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTGV-PCAAVLDVVTEA---GRDWLLLGEVPGQDLLSSHLAPAEKVSI--MADAMRRLHTLDPATCPFDHQAK 74
Cdd:pfam01636  42 ALLRHLAAAGVpPVPRVLAGCTDAellGLPFLLMEYLPGEVLARPLLPEERGALLeaLGRALARLHAVDPAALPLAGRLA 121

                          90       100
                  ....*....|....*....|....*
gi 1339549014  75 HRIERARTRMEAGLVDQDDLDEEHQ 99
Cdd:pfam01636 122 RLLELLRQLEAALARLLAAELLDRL 146
 
Name Accession Description Interval E-value
Aph COG3231
Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];
1-99 1.06e-35

Aminoglycoside phosphotransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442463 [Multi-domain]  Cd Length: 258  Bit Score: 121.56  E-value: 1.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSS--HLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIE 78
Cdd:COG3231    58 DRLRWLAGQGLPVPEVLDFGEDDGGAWLLTTAVPGRPAASVseALDPERAVELLAEALRRLHALPVADCPFDRRLERRLA 137

                          90       100
                  ....*....|....*....|.
gi 1339549014  79 RARTRMEAGLVDQDDLDEEHQ 99
Cdd:COG3231   138 EARARVAAGLVDPDDFDEERR 158
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 1-99 1.78e-32

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: 113.06  E-value: 1.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTgVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSH--LAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIE 78
Cdd:cd05150    43 ERLRWLAGK-LPVPEVLDYGSDDGGDWLLTTALPGRDAASLEplLDPERLVDLLAEALRALHSLPIADCPFDRRLDARLA 121

                          90       100
                  ....*....|....*....|.
gi 1339549014  79 RARTRMEAGLVDQDDLDEEHQ 99
Cdd:cd05150   122 EARARVEAGLVDEDDFDEERQ 142
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 1-99 2.11e-05

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: 40.95  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   1 ARLSWLATTGV-PCAAVLDVVTEA---GRDWLLLGEVPGQDLLSSHLAPAEKVSI--MADAMRRLHTLDPATCPFDHQAK 74
Cdd:pfam01636  42 ALLRHLAAAGVpPVPRVLAGCTDAellGLPFLLMEYLPGEVLARPLLPEERGALLeaLGRALARLHAVDPAALPLAGRLA 121

                          90       100
                  ....*....|....*....|....*
gi 1339549014  75 HRIERARTRMEAGLVDQDDLDEEHQ 99
Cdd:pfam01636 122 RLLELLRQLEAALARLLAAELLDRL 146
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 7-66 8.74e-05

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: 38.82  E-value: 8.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339549014   7 ATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSH--LAPAEKVSIM---ADAMRRLHTLDPAT 66
Cdd:cd05120    48 GKLSLPVPKVYGFGESDGWEYLLMERIEGETLSEVWprLSEEEKEKIAdqlAEILAALHRIDSSV 112
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 3-96 2.92e-03

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 35.09  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   3 LSWLA-TTGVPCAAVLDVVTEA---GRDWLLLGEVPGQDLLS--SHLAPAEKVSI---MADAMRRLHTLDPATCPFD--- 70
Cdd:COG3173    67 LRALApRLGVPVPRPLALGEDGeviGAPFYVMEWVEGETLEDalPDLSPAERRALaraLGEFLAALHAVDPAAAGLAdgr 146

                          90       100
                  ....*....|....*....|....*..
gi 1339549014  71 -HQAKHRIERARTRMEAGLVDQDDLDE 96
Cdd:COG3173   147 pEGLERQLARWRAQLRRALARTDDLPA 173
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 6-97 3.19e-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: 34.90  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339549014   6 LATTGVPCAAVLDVVTEA---GRDWLLL----GEVPGQDLLSSHLAPAEKVSI---MADAMRRLHTLDPATCPFDHQAKH 75
Cdd:cd05154    55 LAGTGVPVPRVLALCEDPsvlGAPFYVMervdGRVLPDPLPRPDLSPEERRALarsLVDALAALHSVDPAALGLADLGRP 134

                          90       100
                  ....*....|....*....|....*...
gi 1339549014  76 R------IERARTRMEAGLVDQDDLDEE 97
Cdd:cd05154   135 EgylerqVDRWRRQLEAAATDPPPALEE 162
 
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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