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Conserved domains on  [gi|1578637709|emb|VFB61280|]
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ribosomal-protein-alanine acetyltransferase [Clostridioides difficile]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-110 5.70e-22

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: 83.72  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  13 DIDNLKGFLNDTSSFGFIAKENNKIIGFAYCYTLLRPDGKTmfYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMF 92
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG--EIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97

                          90
                  ....*....|....*...
gi 1578637709  93 LITDKGNPRACHVYEKLG 110
Cdd:pfam00583  98 LEVAADNLAAIALYEKLG 115
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-110 5.70e-22

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: 83.72  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  13 DIDNLKGFLNDTSSFGFIAKENNKIIGFAYCYTLLRPDGKTmfYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMF 92
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG--EIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97

                          90
                  ....*....|....*...
gi 1578637709  93 LITDKGNPRACHVYEKLG 110
Cdd:pfam00583  98 LEVAADNLAAIALYEKLG 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
21-110 1.45e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.88  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  21 LNDTSSFGFIAKENNKIIGFAYCYTLLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNP 100
Cdd:COG1247    47 ILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNE 126

                          90
                  ....*....|
gi 1578637709 101 RACHVYEKLG 110
Cdd:COG1247   127 ASIALYEKLG 136
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 29-93 1.78e-13

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: 60.75  E-value: 1.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578637709  29 FIAKENNKIIGFAYCYtlLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFL 93
Cdd:cd04301     2 LVAEDDGEIVGFASLS--PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 33-110 1.42e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 47.23  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578637709  33 ENNKIIGFAYCYTLLrpDGKTMFylhSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:PRK09491   47 VNGQMAAFAITQVVL--DEATLF---NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLG 119
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 31-110 2.97e-07

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: 46.17  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  31 AKENNKIIGFAyCYTLLRPDGKtmfyLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:TIGR01575  36 ARIGGKVVGYA-GVQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLG 110
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 13-110 5.70e-22

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: 83.72  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  13 DIDNLKGFLNDTSSFGFIAKENNKIIGFAYCYTLLRPDGKTmfYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMF 92
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVG--EIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIF 97

                          90
                  ....*....|....*...
gi 1578637709  93 LITDKGNPRACHVYEKLG 110
Cdd:pfam00583  98 LEVAADNLAAIALYEKLG 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
21-110 1.45e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.88  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  21 LNDTSSFGFIAKENNKIIGFAYCYTLLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNP 100
Cdd:COG1247    47 ILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNE 126

                          90
                  ....*....|
gi 1578637709 101 RACHVYEKLG 110
Cdd:COG1247   127 ASIALYEKLG 136
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 39-110 9.71e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.99  E-value: 9.71e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578637709  39 GFAYCYtllRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:COG0456     1 GFALLG---LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 20-110 1.37e-15

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: 67.71  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  20 FLNDTSSFGFIAKENNKIIGFAYcytlLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITdkgN 99
Cdd:COG1246    22 ALEEEIGEFWVAEEDGEIVGCAA----LHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---T 94

                          90
                  ....*....|.
gi 1578637709 100 PRACHVYEKLG 110
Cdd:COG1246    95 SAAIHFYEKLG 105
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 8-110 5.48e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 63.92  E-value: 5.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709   8 DNMVFDIDNLkgflnDTSSFGFIAKENNKIIGFAycytLLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIG 87
Cdd:COG0454    21 DAELKAMEGS-----LAGAEFIAVDDKGEPIGFA----GLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG 91

                          90       100
                  ....*....|....*....|...
gi 1578637709  88 CSEMFLITDKGNPRACHVYEKLG 110
Cdd:COG0454    92 CTALELDTLDGNPAAIRFYERLG 114
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
29-110 1.45e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.80  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  29 FIAKENNKIIGFAYCYTLLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDkgnPRACHVYEK 108
Cdd:COG3153    42 LVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYER 118


                  ..
gi 1578637709 109 LG 110
Cdd:COG3153   119 FG 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 29-93 1.78e-13

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: 60.75  E-value: 1.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578637709  29 FIAKENNKIIGFAYCYtlLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFL 93
Cdd:cd04301     2 LVAEDDGEIVGFASLS--PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 29-110 5.20e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.46  E-value: 5.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  29 FIAKENNKIIGFAycyTLLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITdkgNPRACHVYEK 108
Cdd:pfam13508   6 FVAEDDGKIVGFA---ALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEK 79


                  ..
gi 1578637709 109 LG 110
Cdd:pfam13508  80 LG 81
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
36-110 6.86e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.83  E-value: 6.86e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578637709  36 KIIGFAYcytlLRPDGKTMFYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:COG3393     1 ELVAMAG----VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 27-121 1.52e-09

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: 53.08  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  27 FGFIAKENNKIIGFAYCYTLLRPDGKTMFylhSIGMLPNYQDKGYGSKLLSFIKEYSKEI-GCSEMFLITDKGNPRACHV 105
Cdd:COG1670    63 FAIEDKEDGELIGVVGLYDIDRANRSAEI---GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRV 139

                          90       100
                  ....*....|....*....|....*...
gi 1578637709 106 YEKLG------------GKNDYKDEIVY 121
Cdd:COG1670   140 LEKLGfrlegtlrdalvIDGRYRDHVLY 167
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 33-110 1.42e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 47.23  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578637709  33 ENNKIIGFAYCYTLLrpDGKTMFylhSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:PRK09491   47 VNGQMAAFAITQVVL--DEATLF---NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLG 119
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 31-110 2.97e-07

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: 46.17  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  31 AKENNKIIGFAyCYTLLRPDGKtmfyLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLITDKGNPRACHVYEKLG 110
Cdd:TIGR01575  36 ARIGGKVVGYA-GVQIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLG 110
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 22-95 1.42e-04

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 40.16  E-value: 1.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578637709  22 NDTSSFGFIAKENNkIIGFAYCYTLLRPDGKTMFYLhsiGMLPNYQDKGYGSKLLSFIKEYSKEIGCSEMFLIT 95
Cdd:TIGR01890 319 REISEFSIIEHDGN-IIGCAALYPYAEEDCGEMACL---AVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLT 388
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 64-110 1.74e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 39.39  E-value: 1.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1578637709  64 PNYQDKGYGSKLLSFIKEYSKEI-GCSEMFLITDKGNPRACHVYEKLG 110
Cdd:PRK15130   92 PEYQGKGLATRAAKLAMDYGFTVlNLYKLYLIVDKENEKAIHIYRKLG 139
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 26-120 1.07e-03

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: 35.77  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578637709  26 SFGFIAKENNKIIGFaycytLLRPDGKtmfYLHSIGMLPNYQDKGYGSKLLSFIKEYSKEIGcSEMFLITDKGNPRACHV 105
Cdd:pfam08445   1 VLGIYRGDTGELAAW-----CLRLPGG---ELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRL 71

                          90
                  ....*....|....*
gi 1578637709 106 YEKLGGKNDYKDEIV 120
Cdd:pfam08445  72 YEKLGFRKIDETYWV 86
 
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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