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Conserved domains on  [gi|489287369|ref|WP_003194938|]
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MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
3-149 5.53e-60

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10314:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 153  Bit Score: 182.35  E-value: 5.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   3 VDWVCKHHNDLGKDQLYALLRLRSEVFVVEQKCAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDPESQGGDVVIGRVI 82
Cdd:PRK10314   2 IEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRVI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489287369  83 VSPAARGTGLGHQMMEEALERIEDIWPQTPIFLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:PRK10314  82 VSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAR 148
 
Name Accession Description Interval E-value
PRK10314 PRK10314
GNAT family N-acetyltransferase;
3-149 5.53e-60

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 182.35  E-value: 5.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   3 VDWVCKHHNDLGKDQLYALLRLRSEVFVVEQKCAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDPESQGGDVVIGRVI 82
Cdd:PRK10314   2 IEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRVI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489287369  83 VSPAARGTGLGHQMMEEALERIEDIWPQTPIFLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:PRK10314  82 VSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAR 148
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
16-149 6.26e-56

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 171.52  E-value: 6.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  16 DQLYALLRLRSEVFVVEQK-CAYQDIDGQDLagDTHHLMAWNDNELVAYLRLLDPEsqGGDVVIGRVIVSPAARGTGLGH 94
Cdd:COG2153    2 EELYDALALRREVFVVEQGvPPYLELDGKDE--DARHLLAYDDGELVATARLLPPG--DGEAKIGRVAVLPEYRGQGLGR 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489287369  95 QMMEEALERIEDIwPQTPIFLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:COG2153   78 ALMEAAIEEARER-GARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRK 131
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
35-149 1.41e-17

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: 73.46  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   35 CAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDpesqggDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTP-I 113
Cdd:pfam13673  17 ISPEALRERIDQGEYFFFVAFEGGQIVGVIALRD------RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSeL 90
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489287369  114 FLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:pfam13673  91 TVNASPYAVPFYEKLGFRATGPEQEFNGIRFVPMEK 126
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-103 3.59e-08

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: 47.27  E-value: 3.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489287369  51 HLMAWNDNELVAYLRLLDPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALER 103
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
PRK10314 PRK10314
GNAT family N-acetyltransferase;
3-149 5.53e-60

GNAT family N-acetyltransferase;


Pssm-ID: 182373 [Multi-domain]  Cd Length: 153  Bit Score: 182.35  E-value: 5.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   3 VDWVCKHHNDLGKDQLYALLRLRSEVFVVEQKCAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDPESQGGDVVIGRVI 82
Cdd:PRK10314   2 IEWQDLHHSELSVSQLYALLQLRCAVFVVEQNCPYQDIDGDDLTGDNRHILGWKNDELVAYARILKSDDDLEPVVIGRVI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489287369  83 VSPAARGTGLGHQMMEEALERIEDIWPQTPIFLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:PRK10314  82 VSEALRGEKVGQQLMSKTLESCTRHWPDKPVYLGAQAHLQNFYQSFGFIPVTEVYEEDGIPHIGMAR 148
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
16-149 6.26e-56

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 171.52  E-value: 6.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  16 DQLYALLRLRSEVFVVEQK-CAYQDIDGQDLagDTHHLMAWNDNELVAYLRLLDPEsqGGDVVIGRVIVSPAARGTGLGH 94
Cdd:COG2153    2 EELYDALALRREVFVVEQGvPPYLELDGKDE--DARHLLAYDDGELVATARLLPPG--DGEAKIGRVAVLPEYRGQGLGR 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489287369  95 QMMEEALERIEDIwPQTPIFLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:COG2153   78 ALMEAAIEEARER-GARRIVLSAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRK 131
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
35-149 1.41e-17

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: 73.46  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   35 CAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDpesqggDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTP-I 113
Cdd:pfam13673  17 ISPEALRERIDQGEYFFFVAFEGGQIVGVIALRD------RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSeL 90
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489287369  114 FLSAQAHLQKYYGRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:pfam13673  91 TVNASPYAVPFYEKLGFRATGPEQEFNGIRFVPMEK 126
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
48-149 6.28e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 6.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  48 DTHHLMAWNDNELVAYLRL--LDPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTpIFLSAQAHLQKYY 125
Cdd:COG3153   38 AGLSLVAEDDGEIVGHVALspVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARA-VVLLGDPSLLPFY 116
                         90       100
                 ....*....|....*....|....
gi 489287369 126 GRYGFVVAGEEYLEDDIPHIGMRR 149
Cdd:COG3153  117 ERFGFRPAGELGLTLGPDEVFLAK 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
18-130 5.55e-10

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: 53.68  E-value: 5.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   18 LYALLRLRSEVF-VVEQKCAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDPESQGGDVVIGRVIVSPAARGTGLGHQM 96
Cdd:pfam00583   1 LEALYELLSEEFpEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489287369   97 MEEALERIEDiWPQTPIFL---SAQAHLQKYYGRYGF 130
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLevaADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
48-132 6.97e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 6.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   48 DTHHLMAWNDNELVAYLRLLdPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIwPQTPIFLSAQAHLQKYYGR 127
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALL-PLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEG-GIKLLELETTNRAAAFYEK 79

                  ....*
gi 489287369  128 YGFVV 132
Cdd:pfam13508  80 LGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
66-149 1.98e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.88  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  66 LLDPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTpIFLSAQAH---LQKYYGRYGFVVAGEEYLEDDI 142
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARR-LRLEVREDneaAIALYEKLGFEEVGERPNYYGD 82

                 ....*..
gi 489287369 143 PHIGMRR 149
Cdd:COG0456   83 DALVMEK 89
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-103 3.59e-08

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: 47.27  E-value: 3.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489287369  51 HLMAWNDNELVAYLRLLDPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALER 103
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
54-138 4.28e-08

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: 48.83  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  54 AWNDNELVAYLRLLDPEsqGGDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTpIFLSAQAHLQKYYGRYGFVVA 133
Cdd:COG1246   33 AEEDGEIVGCAALHPLD--EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKR-LFLLTTSAAIHFYEKLGFEEI 109

                 ....*
gi 489287369 134 GEEYL 138
Cdd:COG1246  110 DKEDL 114
Eis COG4552
Predicted acetyltransferase [General function prediction only];
13-137 3.77e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 45.27  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  13 LGKDQLYALLRLRSEVFVVEQKCAYQDIDGQDLAGDTHhLMAWNDNELVAYLRLLDPESQ-GGDVV----IGRVIVSPAA 87
Cdd:COG4552    6 LTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRV-LGVFDDGELVGTLALYPFTLNvGGARVpmagITGVAVAPEH 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489287369  88 RGTGLGHQMMEEALERIED-------IWPqtpiflSAQAhlqkYYGRYGFVVAGEEY 137
Cdd:COG4552   85 RRRGVARALLREALAELRErgqplsaLYP------FEPG----FYRRFGYELAGDRR 131
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
13-130 3.20e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 38.32  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369   13 LGKDQLYALLRLRSEVFVVEQkCAYQDIDGQDLAGDTHHLMAWNDNELVAYLRLLDPE-SQGGDVV----IGRVIVSPAA 87
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDED-SPELREYFRPLLEEGRVLGAFDDGELVSTLALYPFElNVPGKTLpaagITGVATYPEY 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489287369   88 RGTGLGHQMMEEALERIEDiWPQTPIFLSAQAHlqKYYGRYGF 130
Cdd:pfam13527  83 RGRGVMSRLLRRSLEEMRE-RGVPLSFLYPSSY--PIYRRFGY 122
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
52-103 4.44e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.44  E-value: 4.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489287369  52 LMAWNDNELV--AYLRLLDPESQGGDVVIGRVIVSPAARGTGLGHQMMEEALER 103
Cdd:COG1247   55 LVAEEDGEVVgfASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIER 108
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
57-135 5.37e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.73  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489287369  57 DNELVAY--LRLLDPESqggdVVIGRVIVSPAARGTGLG----HQMMEEALER-IEDIWPQTpifLSAQAHLQKYYGRYG 129
Cdd:COG0454   42 KGEPIGFagLRRLDDKV----LELKRLYVLPEYRGKGIGkallEALLEWARERgCTALELDT---LDGNPAAIRFYERLG 114

                 ....*.
gi 489287369 130 FVVAGE 135
Cdd:COG0454  115 FKEIER 120
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
64-98 2.96e-03

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 35.64  E-value: 2.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489287369  64 LRLLDPESQGGDVVIGRVIVSPAARGTGLGH--QMME 98
Cdd:cd00276   86 ITVVDKDSVGRNEVIGQVVLGPDSGGEELEHwnEMLA 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
73-135 4.96e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.11  E-value: 4.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489287369  73 GGDVVIGRVIVSPAARGTGLGHQMMEEALERIEDIWPQTPiFLSAQAH---LQKYYGRYGFVVAGE 135
Cdd:COG3393   13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTP-FLYVDADnpaARRLYERLGFRPVGE 77
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
57-106 9.02e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 33.26  E-value: 9.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489287369   57 DNELVAYLRLldpESQGGDVVIGRVIVSPAARGTGLGHQMMEEALERIED 106
Cdd:pfam14542   8 GGAEVAFLTY---RRGDGVLIITHTEVPPALRGQGIASKLVKAALDDARE 54
 
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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