NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490086672|ref|WP_003988626|]
View 

phosphinothricin N-acetyltransferase [Streptomyces viridochromogenes]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
1-170 5.15e-129

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


:

Pssm-ID: 439723  Cd Length: 183  Bit Score: 359.69  E-value: 5.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   1 MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  81 NAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160
                        170
                 ....*....|
gi 490086672 161 VGFWQRDFEL 170
Cdd:NF040502 161 VGFWQRDFVL 170
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
1-170 5.15e-129

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


Pssm-ID: 439723  Cd Length: 183  Bit Score: 359.69  E-value: 5.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   1 MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  81 NAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160
                        170
                 ....*....|
gi 490086672 161 VGFWQRDFEL 170
Cdd:NF040502 161 VGFWQRDFVL 170
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-167 1.12e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 173.26  E-value: 1.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   8 VEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDL-ERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWT 86
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFaAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  87 VESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQR 166
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161

                 .
gi 490086672 167 D 167
Cdd:COG1247  162 R 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-142 1.54e-14

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: 66.39  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   23 DIVNHYIETSTVNFRTEPQTPQEWIDDLERlqdrYPWLVAEVEGVVAGiaYAGPWKARNAYDWTVESTVYVSHRHQRLGL 102
Cdd:pfam00583   3 ALYELLSEEFPEPWPDEPLDLLEDWDEDAS----EGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490086672  103 GSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGY 142
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
59-123 3.06e-05

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 40.34  E-value: 3.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490086672  59 WLVAEVEGVVAGIAYAGPWKARNAYdWTVEStVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVV 123
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDT-AYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
Name Accession Description Interval E-value
PPT_acetyltrans NF040502
phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides ...
1-170 5.15e-129

phosphinothricin N-acetyltransferase; Phosphinothricin N-acetyltransferase (PAT) provides resistance to producers of the natural product phosphinothricin, non-proteinogenic amino acid antibiotic.


Pssm-ID: 439723  Cd Length: 183  Bit Score: 359.69  E-value: 5.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   1 MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKAR 80
Cdd:NF040502   1 MSPERRPEGIRLATAADMPAVCEIVNHYIETSTVNFRTEPQLPQEWEDDLARLRERYPWLVAEVGGEVAGIAYAGPWKAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  81 NAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHD 160
Cdd:NF040502  81 NAYDWTTESTVYVSDRHQRRGLGSTLYTHLLKSLEAQGFKSVVAVIGLPNDPSVRLHEALGYESRGRLRAAGHKHGGWHD 160
                        170
                 ....*....|
gi 490086672 161 VGFWQRDFEL 170
Cdd:NF040502 161 VGFWQRDFVL 170
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-167 1.12e-55

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 173.26  E-value: 1.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   8 VEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDL-ERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWT 86
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFaAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  87 VESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQR 166
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161

                 .
gi 490086672 167 D 167
Cdd:COG1247  162 R 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-142 1.54e-14

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: 66.39  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   23 DIVNHYIETSTVNFRTEPQTPQEWIDDLERlqdrYPWLVAEVEGVVAGiaYAGPWKARNAYDWTVESTVYVSHRHQRLGL 102
Cdd:pfam00583   3 ALYELLSEEFPEPWPDEPLDLLEDWDEDAS----EGFFVAEEDGELVG--FASLSIIDDEPPVGEIEGLAVAPEYRGKGI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490086672  103 GSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGY 142
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-153 1.86e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  10 IRPATAADMAAVCDIVNHYietstvnFRtePQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVES 89
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-------FG--PGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLG 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490086672  90 TVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAViglPNDPSVRLHEALGYTARGTLRAAGY 153
Cdd:COG3153   72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELGLTLG 132
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
8-143 2.70e-11

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: 58.08  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   8 VEIRPATAADMAAVCDIVNHYIetstvnfrtepqtpqewiddLERLQDRYpwLVAEVEGVVAGIAYAGPWKARNAYdwtV 87
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYA--------------------LEEEIGEF--WVAEEDGEIVGCAALHPLDEDLAE---L 55
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490086672  88 EStVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAvigLPNDPSVRLHEALGYT 143
Cdd:COG1246   56 RS-LAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---LTTSAAIHFYEKLGFE 107
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-161 4.47e-10

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: 55.78  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   8 VEIRPATAADMAAVCDIVNHyiETSTVNFRTEPQTPQEWIDDLERLQ------DRYPWLVAEVEG--VVAGIAYAGPwka 79
Cdd:COG1670    8 LRLRPLRPEDAEALAELLND--PEVARYLPGPPYSLEEARAWLERLLadwadgGALPFAIEDKEDgeLIGVVGLYDI--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  80 rNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLK-SMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGW 158
Cdd:COG1670   83 -DRANRSAEIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161

                 ...
gi 490086672 159 HDV 161
Cdd:COG1670  162 RDH 164
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-160 7.07e-10

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 55.07  E-value: 7.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   10 IRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQE---WIDDLERLQdRYPWLVAEVEGVVaGIAYAGPWKARnaYDWT 86
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEfetFLAAYLSPG-EIVFGVAESDRLI-GYATLRQFDYV--KTHK 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490086672   87 VESTVYVSHRHQRlGLGSTLYTHLLK-SMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHD 160
Cdd:pfam13420  77 AELSFYVVKNNDE-GINRELINAIIQyARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
8-144 4.67e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 49.67  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   8 VEIRPATAADMAAVCDIvnhyietstvnfrtepQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKarnayDWTV 87
Cdd:COG0454    1 MSIRKATPEDINFILLI----------------EALDAELKAMEGSLAGAEFIAVDDKGEPIGFAGLRRLD-----DKVL 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490086672  88 E-STVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTA 144
Cdd:COG0454   60 ElKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
90-149 2.21e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 43.88  E-value: 2.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672  90 TVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLR 149
Cdd:COG0456   18 DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
59-123 3.06e-05

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 40.34  E-value: 3.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490086672  59 WLVAEVEGVVAGIAYAGPWKARNAYdWTVEStVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVV 123
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDT-AYIGD-LAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
80-154 3.63e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.66  E-value: 3.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490086672  80 RNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYK 154
Cdd:COG3393   10 AESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
55-143 4.43e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.52  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490086672   55 DRYPWLVAEVEGVVAGIAYAGPwkaRNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAvigLPNDPSV 134
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLP---LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNRAA 74

                  ....*....
gi 490086672  135 RLHEALGYT 143
Cdd:pfam13508  75 AFYEKLGFE 83
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
89-145 8.11e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 39.62  E-value: 8.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490086672   89 STVYVSHRHQRLGLGSTLYTHLLKSMEAQGfKSVVAVIGLPNDPSVRLHEALGYTAR 145
Cdd:pfam08445  25 GALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFRKI 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH