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Conserved domains on  [gi|15596424|ref|NP_249918|]
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hypothetical protein PA1227 [Pseudomonas aeruginosa PAO1]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 12025366)

aminoglycoside phosphotransferase family protein catalyzes the phosphorylation of small molecule substrates such as aminoglycoside antibiotics and N-acetylhexosamine, similar to Streptomyces vinaceus viomycin phosphotransferase

EC:  2.7.1.-
Gene Ontology:  GO:0005524|GO:0016310

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
11-242 9.67e-18

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: 80.24  E-value: 9.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    11 TFAILASGWHSTAVEVG---GRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPLFSRHEKLPGGYLLG 87
Cdd:pfam01636   1 TLRPISSGASNRTYLVTtgdGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    88 EDYRRLDEP-ARQAVGDALGRFYAELHRLPPARMRAVGALPVRPWESPAAMRRRA---LPLLPAAWRERAERLVREYAKL 163
Cdd:pfam01636  81 EVLARPLLPeERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALArllAAELLDRLEELEERLLAALLAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424   164 PADPLGSIFGFFDGHGWNMAFDsEAGRLNGVYDFADAGIGPLHQEFIYSA-FIDADLTERIVAAYERFSGRRLERRRIAL 242
Cdd:pfam01636 161 LPAELPPVLVHGDLHPGNLLVD-PGGRVSGVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAFGYARLREL 239
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
11-242 9.67e-18

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: 80.24  E-value: 9.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    11 TFAILASGWHSTAVEVG---GRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPLFSRHEKLPGGYLLG 87
Cdd:pfam01636   1 TLRPISSGASNRTYLVTtgdGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    88 EDYRRLDEP-ARQAVGDALGRFYAELHRLPPARMRAVGALPVRPWESPAAMRRRA---LPLLPAAWRERAERLVREYAKL 163
Cdd:pfam01636  81 EVLARPLLPeERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALArllAAELLDRLEELEERLLAALLAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424   164 PADPLGSIFGFFDGHGWNMAFDsEAGRLNGVYDFADAGIGPLHQEFIYSA-FIDADLTERIVAAYERFSGRRLERRRIAL 242
Cdd:pfam01636 161 LPAELPPVLVHGDLHPGNLLVD-PGGRVSGVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAFGYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
15-233 1.92e-14

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 71.68  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  15 LASGWHST--AVEVGGRWVFKF-PRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPL-----FSRHEKLPGGYlL 86
Cdd:COG3173  28 LSGGWSNLtyRLDTGDRLVLRRpPRGLASAHDVRREARVLRALAPRLGVPVPRPLALGEDGEvigapFYVMEWVEGET-L 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  87 GEDYRRLDEPARQAVGDALGRFYAELHRLPPARMRAVGALP------VRPWESPAAMRRRALPLLPaAWRERAERLVREY 160
Cdd:COG3173 107 EDALPDLSPAERRALARALGEFLAALHAVDPAAAGLADGRPeglerqLARWRAQLRRALARTDDLP-ALRERLAAWLAAN 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596424 161 AKLPADPlGSIFGffDGHGWNMAFDSEAGRLNGVYDFADAGIGPLHQEFIYSAFI------DADLTERIVAAYERFSGR 233
Cdd:COG3173 186 LPEWGPP-VLVHG--DLRPGNLLVDPDDGRLTAVIDWELATLGDPAADLAYLLLYwrlpddLLGPRAAFLAAYEEATGD 261
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
27-245 6.71e-08

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 52.63  E-value: 6.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  27 GGRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAgPPLFSrHEKLPGGYLLGEDYRRLD-------EPARQ 99
Cdd:cd05152  35 GRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHT-PELIA-YPLLPGVPAATIDPEIQNyvwnwdpLAPPP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424 100 AVGDALGRFYAELHRLPPARMRAVGALPVRPWESPAAMRRR-----ALPLLPAAWRERAERLVREYAKLPADPlGSIFGf 174
Cdd:cd05152 113 VFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARmdrvkETFGVPPALLARWQAWLADDSLWPFHT-VLVHG- 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596424 175 fDGHGWNMAFDsEAGRLNGVYDFADAGIGPLHQEFI--YSAFiDADLTERIVAAYERFSGR---RLERRRIALLTA 245
Cdd:cd05152 191 -DLHPGHILVD-EDGRVTGLIDWTEAKVGDPADDFAwhYAAF-GEEALERLLDAYEKAGGEvwpRMLEHIIELAAA 263
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
11-242 9.67e-18

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: 80.24  E-value: 9.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    11 TFAILASGWHSTAVEVG---GRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPLFSRHEKLPGGYLLG 87
Cdd:pfam01636   1 TLRPISSGASNRTYLVTtgdGRYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYLPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424    88 EDYRRLDEP-ARQAVGDALGRFYAELHRLPPARMRAVGALPVRPWESPAAMRRRA---LPLLPAAWRERAERLVREYAKL 163
Cdd:pfam01636  81 EVLARPLLPeERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALArllAAELLDRLEELEERLLAALLAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424   164 PADPLGSIFGFFDGHGWNMAFDsEAGRLNGVYDFADAGIGPLHQEFIYSA-FIDADLTERIVAAYERFSGRRLERRRIAL 242
Cdd:pfam01636 161 LPAELPPVLVHGDLHPGNLLVD-PGGRVSGVIDFEDAGLGDPAYDLAILLnSWGRELGAELLAAYLAAYGAFGYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
15-233 1.92e-14

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 71.68  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  15 LASGWHST--AVEVGGRWVFKF-PRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPL-----FSRHEKLPGGYlL 86
Cdd:COG3173  28 LSGGWSNLtyRLDTGDRLVLRRpPRGLASAHDVRREARVLRALAPRLGVPVPRPLALGEDGEvigapFYVMEWVEGET-L 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  87 GEDYRRLDEPARQAVGDALGRFYAELHRLPPARMRAVGALP------VRPWESPAAMRRRALPLLPaAWRERAERLVREY 160
Cdd:COG3173 107 EDALPDLSPAERRALARALGEFLAALHAVDPAAAGLADGRPeglerqLARWRAQLRRALARTDDLP-ALRERLAAWLAAN 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596424 161 AKLPADPlGSIFGffDGHGWNMAFDSEAGRLNGVYDFADAGIGPLHQEFIYSAFI------DADLTERIVAAYERFSGR 233
Cdd:COG3173 186 LPEWGPP-VLVHG--DLRPGNLLVDPDDGRLTAVIDWELATLGDPAADLAYLLLYwrlpddLLGPRAAFLAAYEEATGD 261
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
27-245 6.71e-08

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 52.63  E-value: 6.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  27 GGRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAgPPLFSrHEKLPGGYLLGEDYRRLD-------EPARQ 99
Cdd:cd05152  35 GRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHT-PELIA-YPLLPGVPAATIDPEIQNyvwnwdpLAPPP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424 100 AVGDALGRFYAELHRLPPARMRAVGALPVRPWESPAAMRRR-----ALPLLPAAWRERAERLVREYAKLPADPlGSIFGf 174
Cdd:cd05152 113 VFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARmdrvkETFGVPPALLARWQAWLADDSLWPFHT-VLVHG- 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596424 175 fDGHGWNMAFDsEAGRLNGVYDFADAGIGPLHQEFI--YSAFiDADLTERIVAAYERFSGR---RLERRRIALLTA 245
Cdd:cd05152 191 -DLHPGHILVD-EDGRVTGLIDWTEAKVGDPADDFAwhYAAF-GEEALERLLDAYEKAGGEvwpRMLEHIIELAAA 263
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
84-269 2.51e-06

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 48.02  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  84 YLLGEDYRRLDEPARQAVGDALGRFYAELHRLPPARMRAVGalpvRPWESPAAmrRRALPLLPAAWRERAERLVREYAKL 163
Cdd:cd05153  96 FLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPRG----LAWWKPLA--ERLKARLDLLAADDRALLEDELARL 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424 164 PADPL-----GSIFGffDGHGWNMAFDseAGRLNGVYDFADAGIGPLHQE---------FIYSAFIDADLTERIVAAYEr 229
Cdd:cd05153 170 QALAPsdlprGVIHA--DLFRDNVLFD--GDRLSGIIDFYDACYDPLLYDlaialndwcFDDDGKLDPERAKALLAGYQ- 244
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15596424 230 fSGRRLErrrialltaahrlselaelADEPRHLPDMLAGA 269
Cdd:cd05153 245 -SVRPLT-------------------EEEKAALPLLLRAA 264
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
60-257 4.11e-05

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 44.15  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  60 LPVPAPQV-FAGPPLFSRHEK----LPggYLLGEDYRRLDEPARQAVGDALGRFYAELHRLPPARMRAVGAlpvrpWESP 134
Cdd:COG2334  69 LPVPAPVPtRDGETLLELEGRpaalFP--FLPGRSPEEPSPEQLEELGRLLARLHRALADFPRPNARDLAW-----WDEL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424 135 AAMRRRALpLLPAAWRERAERLVREYAK-----LPADPLGSIFGffDGHGWNMAFDseAGRLNGVYDFADAGIGPLHQEF 209
Cdd:COG2334 142 LERLLGPL-LPDPEDRALLEELLDRLEArlaplLGALPRGVIHG--DLHPDNVLFD--GDGVSGLIDFDDAGYGPRLYDL 216
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15596424 210 ---IYSAFIDADLTER---IVAAYERFsgRRLERRRIALLTAAHRLSELAELAD 257
Cdd:COG2334 217 aiaLNGWADGPLDPARlaaLLEGYRAV--RPLTEAELAALPPLLRLRALRFLAW 268
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
14-203 3.02e-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: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  14 ILASGWHSTAVEVGGRWVFKFPRGAEAEAALLREAAVLRLVRPAVSLPVPAPQVFAGPPLfsrheklpgGY--------- 84
Cdd:cd05155   5 VASSGWDNATFRLGDDLAVRLPRRAWAAELLEKEQRWLPRLAPRLPLPVPVPLALGKPGA---------GYpwpwsvyrw 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596424  85 LLGEDYRRLDEPARQAVGDALGRFYAELHRLPPA------RMRAVGALPVRPWESPAAMRRRALPLLPAAWRERAERLVR 158
Cdd:cd05155  76 LEGETAADAPLADPAAAAEDLARFLAALHAIDPAgppnpgRGNPLRGRDLAVRDAEEALAALAGLLDVAAARALWERALA 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15596424 159 eyAKLPADPLGSIFGffDGHGWNMAFDseAGRLNGVYDFADAGIG 203
Cdd:cd05155 156 --APAWAGPPVWLHG--DLHPGNLLVR--DGRLSAVIDFGDLGVG 194
 
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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