NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|254587982|ref|NP_001157015|]
View 

spermidine/spermine N(1)-acetyltransferase-like protein 1 [Rattus norvegicus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
591-732 1.41e-19

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 86.20  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 591 AFYIRPAEPQDCPDILRLIKE-----LATYEGTQEkvsltELDLFKDGFGEK--PLFYCLVAEapskqaESGvKIIGFAm 663
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAIlaPGRPVLVAE------EDG-EVVGFA- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 664 YYFTYDPRIG-KLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLGA 732
Cdd:COG1247   68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
PTZ00395 super family cl33180
Sec24-related protein; Provisional
 5-123 7.42e-04

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.14  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982    5 GKNQSGMTQSGLSQPVMS-PPGPGPYNMQQPGPSQPYTSQPSMNQPSTNKPGVTRPVSCQLDINQPglgQSNIKQSwTST 83
Cdd:PTZ00395  403 AQSNAGFSNAGYSNPGNSnPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAP---LSNAPPS-SAK 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 254587982   84 NQPGIYKTDLSQQSMresdpRQVGMKQLNSSQPAAMNQTG 123
Cdd:PTZ00395  479 DHHSAYHAAYQHRAA-----NQPAANLPTANQPAANNFHG 513
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
591-732 1.41e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 86.20  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 591 AFYIRPAEPQDCPDILRLIKE-----LATYEGTQEkvsltELDLFKDGFGEK--PLFYCLVAEapskqaESGvKIIGFAm 663
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAIlaPGRPVLVAE------EDG-EVVGFA- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 664 YYFTYDPRIG-KLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLGA 732
Cdd:COG1247   68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 652-731 7.93e-13

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: 65.62  E-value: 7.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  652 AESGVKIIGFAMYYFTYDPriGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLG 731
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 652-712 1.24e-07

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: 49.20  E-value: 1.24e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254587982 652 AESGVKIIGFAMYYFtyDPRIGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGM 712
Cdd:cd04301    4 AEDDGEIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 5-123 7.42e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.14  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982    5 GKNQSGMTQSGLSQPVMS-PPGPGPYNMQQPGPSQPYTSQPSMNQPSTNKPGVTRPVSCQLDINQPglgQSNIKQSwTST 83
Cdd:PTZ00395  403 AQSNAGFSNAGYSNPGNSnPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAP---LSNAPPS-SAK 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 254587982   84 NQPGIYKTDLSQQSMresdpRQVGMKQLNSSQPAAMNQTG 123
Cdd:PTZ00395  479 DHHSAYHAAYQHRAA-----NQPAANLPTANQPAANNFHG 513
PTZ00330 PTZ00330
acetyltransferase; Provisional
 677-731 1.03e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 40.21  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254587982 677 HLEDFYITEDYQGLGIGADMLKKLSQIAINTGCsgmqFLVII-WNQDSVEYYTRLG 731
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGC----YKVILdCTEDMVAFYKKLG 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 630-731 4.74e-03

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 38.08  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  630 FKDGFGEKPLFYCLvaeapskqAESGVKIIGFAMYYFTYDPriGKLLHledFYITEDYQGLGIGADMLKKLSQIAINTGC 709
Cdd:TIGR01575  22 FAEELANYHLCYLL--------ARIGGKVVGYAGVQIVLDE--AHILN---IAVKPEYQGQGIGRALLRELIDEAKGRGV 88

                          90       100
                  ....*....|....*....|..
gi 254587982  710 SGMQFLVIIWNQDSVEYYTRLG 731
Cdd:TIGR01575  89 NEIFLEVRVSNIAAQALYKKLG 110
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
591-732 1.41e-19

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 86.20  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 591 AFYIRPAEPQDCPDILRLIKE-----LATYEGTQEkvsltELDLFKDGFGEK--PLFYCLVAEapskqaESGvKIIGFAm 663
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEPP-----SEEEREAWFAAIlaPGRPVLVAE------EDG-EVVGFA- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 664 YYFTYDPRIG-KLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLGA 732
Cdd:COG1247   68 SLGPFRPRPAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
594-731 2.06e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.19  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 594 IRPAEPQDCPDILRLIKElaTYEGTQEKVSLTELDLFKDgfgekpLFYCLVAEapskqaESGvKIIGFAMYYFTYDPRIG 673
Cdd:COG3153    1 IRPATPEDAEAIAALLRA--AFGPGREAELVDRLREDPA------AGLSLVAE------DDG-EIVGHVALSPVDIDGEG 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254587982 674 KLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGmqfLVIIWNQDSVEYYTRLG 731
Cdd:COG3153   66 PALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARA---VVLLGDPSLLPFYERFG 120
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 652-731 7.93e-13

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: 65.62  E-value: 7.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  652 AESGVKIIGFAMYYFTYDPriGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLG 731
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDE--PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 592-731 3.10e-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: 61.55  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 592 FYIRPAEPQDCPDILRLIKELATYEGTQEkvslteldlfkdgfgekplfyCLVAEapskqaESGvKIIGFAMYYftydPR 671
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE---------------------FWVAE------EDG-EIVGCAALH----PL 48

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 672 IGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLViiwNQDSVEYYTRLG 731
Cdd:COG1246   49 DEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 660-731 5.15e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 59.67  E-value: 5.15e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254587982 660 GFAMYYFTYDPRIGkllHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLG 731
Cdd:COG0456    1 GFALLGLVDGGDEA---EIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 657-731 4.71e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 58.14  E-value: 4.71e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254587982 657 KIIGFAMYYFTYDPRigklLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLVIIWNQDSVEYYTRLG 731
Cdd:COG0454   44 EPIGFAGLRRLDDKV----LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLG 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 652-712 1.24e-07

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: 49.20  E-value: 1.24e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254587982 652 AESGVKIIGFAMYYFtyDPRIGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGM 712
Cdd:cd04301    4 AEDDGEIVGFASLSP--DGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 652-731 1.30e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.68  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  652 AESGVKIIGFAMYYFTYDPRIGKLLHLedfYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLViiwNQDSVEYYTRLG 731
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRL---AVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLG 81
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 5-123 7.42e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.14  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982    5 GKNQSGMTQSGLSQPVMS-PPGPGPYNMQQPGPSQPYTSQPSMNQPSTNKPGVTRPVSCQLDINQPglgQSNIKQSwTST 83
Cdd:PTZ00395  403 AQSNAGFSNAGYSNPGNSnPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAP---LSNAPPS-SAK 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 254587982   84 NQPGIYKTDLSQQSMresdpRQVGMKQLNSSQPAAMNQTG 123
Cdd:PTZ00395  479 DHHSAYHAAYQHRAA-----NQPAANLPTANQPAANNFHG 513
PTZ00330 PTZ00330
acetyltransferase; Provisional
 677-731 1.03e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 40.21  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254587982 677 HLEDFYITEDYQGLGIGADMLKKLSQIAINTGCsgmqFLVII-WNQDSVEYYTRLG 731
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGC----YKVILdCTEDMVAFYKKLG 135
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 652-741 1.87e-03

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 39.18  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  652 AESGVKIIGFAmyyftydpRIGKLLHLEDFYITEDYQGLGIGADMLKKLSQIAINTGCSGMQFLViiwNQD--SVEYYTR 729
Cdd:pfam13673  36 AFEGGQIVGVI--------ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV---NASpyAVPFYEK 104

                          90
                  ....*....|....
gi 254587982  730 LG--ALDLSCEEGW 741
Cdd:pfam13673 105 LGfrATGPEQEFNG 118
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 630-731 4.74e-03

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 38.08  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982  630 FKDGFGEKPLFYCLvaeapskqAESGVKIIGFAMYYFTYDPriGKLLHledFYITEDYQGLGIGADMLKKLSQIAINTGC 709
Cdd:TIGR01575  22 FAEELANYHLCYLL--------ARIGGKVVGYAGVQIVLDE--AHILN---IAVKPEYQGQGIGRALLRELIDEAKGRGV 88

                          90       100
                  ....*....|....*....|..
gi 254587982  710 SGMQFLVIIWNQDSVEYYTRLG 731
Cdd:TIGR01575  89 NEIFLEVRVSNIAAQALYKKLG 110
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 592-731 7.29e-03

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: 38.06  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254587982 592 FYIRPAEPQDCPDILRLI--KELATYEGTQ---EKVSLTELDLFKDGFGEKPLFYCLVAEAPSKQaesgvkIIGFAMYYf 666
Cdd:COG1670    8 LRLRPLRPEDAEALAELLndPEVARYLPGPpysLEEARAWLERLLADWADGGALPFAIEDKEDGE------LIGVVGLY- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254587982 667 tYDPRIGKLLHLeDFYITEDYQGLGIGADMLKKLSQIAINT-GCSGMQFLVIIWNQDSVEYYTRLG 731
Cdd:COG1670   81 -DIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG 144
 
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