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Conserved domains on  [gi|1958763045|ref|XP_038961402|]
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cysteine-rich protein 2-binding protein isoform X1 [Rattus norvegicus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11688059)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 472-547 1.23e-12

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 472 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 547
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 390-552 3.30e-03

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 PRK09831:

Pssm-ID: 473072  Cd Length: 147  Bit Score: 38.40  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 390 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 467
Cdd:PRK09831    4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 468 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 539
Cdd:PRK09831   56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                         170
                  ....*....|....
gi 1958763045 540 -EEYVLDFYDKYYP 552
Cdd:PRK09831  132 rGEWFINFYMRYKP 145
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 472-547 1.23e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 472 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 547
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 458-537 6.29e-12

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: 62.54  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 458 PDFSVVVLYKKVIVAF-GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLY 532
Cdd:pfam00583  32 SEGFFVAEEDGELVGFaSLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGcerIFLEVAADNlAAIALY 111


                  ....*
gi 1958763045 533 QKFGF 537
Cdd:pfam00583 112 EKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 461-513 9.83e-06

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: 43.42  E-value: 9.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958763045 461 SVVVLYKKVIVAFGFMVP-DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTC 513
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
PRK09831 PRK09831
GNAT family N-acetyltransferase;
390-552 3.30e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 38.40  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 390 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 467
Cdd:PRK09831    4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 468 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 539
Cdd:PRK09831   56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                         170
                  ....*....|....
gi 1958763045 540 -EEYVLDFYDKYYP 552
Cdd:PRK09831  132 rGEWFINFYMRYKP 145
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 474-552 4.77e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 474 GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASN-PAMLLYQKFGFKTeeyvLDFYDK 549
Cdd:PRK09491   53 AFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVAtlwLEVRASNaAAIALYESLGFNE----VTIRRN 128


                  ...
gi 1958763045 550 YYP 552
Cdd:PRK09491  129 YYP 131
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 472-547 1.23e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 472 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 547
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 458-537 6.29e-12

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: 62.54  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 458 PDFSVVVLYKKVIVAF-GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLY 532
Cdd:pfam00583  32 SEGFFVAEEDGELVGFaSLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGcerIFLEVAADNlAAIALY 111


                  ....*
gi 1958763045 533 QKFGF 537
Cdd:pfam00583 112 EKLGF 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
470-538 1.46e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.91  E-value: 1.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958763045 470 IVAFGFMVPDVkYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCM---GKDVTLHVSASNPAML-LYQKFGFK 538
Cdd:COG3393     2 LVAMAGVRAES-PGVAEISGVYTHPEYRGRGLASALVAALAREALargARTPFLYVDADNPAARrLYERLGFR 73
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 455-550 1.58e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 455 LQYPDFSVVVLYKKVIVAFG--FMVPDvkyNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASNP-A 528
Cdd:COG0454    30 SLAGAEFIAVDDKGEPIGFAglRRLDD---KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTaleLDTLDGNPaA 106

                          90       100
                  ....*....|....*....|...
gi 1958763045 529 MLLYQKFGFK-TEEYVLDFYDKY 550
Cdd:COG0454   107 IRFYERLGFKeIERYVAYVGGEF 129
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 462-538 1.65e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 54.77  E-value: 1.65e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958763045 462 VVVLYKKVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTL-HVSASNPAMLLYQKFGFK 538
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLlELETTNRAAAFYEKLGFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 462-567 2.82e-09

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: 55.38  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 462 VVVLYKKVIVAFGFMVPDVKyNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDV-TLHVSASNPAMLLYQKFGFKte 540
Cdd:COG1246    31 WVAEEDGEIVGCAALHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLkRLFLLTTSAAIHFYEKLGFE-- 107

                          90       100
                  ....*....|....*....|....*..
gi 1958763045 541 eyVLDFYDKYYPLESTECKHAFFLRLR 567
Cdd:COG1246   108 --EIDKEDLPYAKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
430-548 2.39e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.17  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 430 RPNHIPTINSMCQEFFWPG--IDLSECLQ---YPDFSVVVLYKKVIVAFGFMVP---DVKYNEAYISFLLVHPEWRRAGI 501
Cdd:COG3153     5 TPEDAEAIAALLRAAFGPGreAELVDRLRedpAAGLSLVAEDDGEIVGHVALSPvdiDGEGPALLLGPLAVDPEYRGQGI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958763045 502 ATFMIYHLIQTCMGKDVT-LHVSASNPAMLLYQKFGFK-TEEYVLDFYD 548
Cdd:COG3153    85 GRALMRAALEAARERGARaVVLLGDPSLLPFYERFGFRpAGELGLTLGP 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 460-539 2.64e-06

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: 46.88  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 460 FSVVVLYKKVIVAFGFMvpdvkYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTLH---VSASNPAMLLYQKFG 536
Cdd:pfam13673  32 FFFVAFEGGQIVGVIAL-----RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSeltVNASPYAVPFYEKLG 106


                  ...
gi 1958763045 537 FKT 539
Cdd:pfam13673 107 FRA 109
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
462-549 5.77e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.53  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 462 VVVLYKKVIVAFGFMVP---DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASNPAML-LYQK 534
Cdd:COG1247    55 LVAEEDGEVVGFASLGPfrpRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRrlvAVVLADNEASIaLYEK 134

                          90
                  ....*....|....*
gi 1958763045 535 FGFKTEEYVLDFYDK 549
Cdd:COG1247   135 LGFEEVGTLPEVGFK 149
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 461-513 9.83e-06

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: 43.42  E-value: 9.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958763045 461 SVVVLYKKVIVAFGFMVP-DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTC 513
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 473-568 5.46e-05

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: 43.83  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 473 FGFMVPDVKYNEAYISFLLvHPEWRRAGIATFMIYHLIQTC---MG-KDVTLHVSASNPAML-LYQKFGFKTEEYVldfy 547
Cdd:COG1670    77 VGLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAfeeLGlHRVEAEVDPDNTASIrVLEKLGFRLEGTL---- 151

                          90       100
                  ....*....|....*....|.
gi 1958763045 548 DKYYPLESTECKHAFFLRLRR 568
Cdd:COG1670   152 RDALVIDGRYRDHVLYSLLRE 172
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
483-545 5.80e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.25  E-value: 5.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958763045 483 NEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT-LHVSASNPAMLLYQKFGFKT--EEYVLD 545
Cdd:COG2153    57 GEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARrIVLSAQAHAVGFYEKLGFVPvgEEFLEA 122
PRK09831 PRK09831
GNAT family N-acetyltransferase;
390-552 3.30e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 38.40  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 390 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 467
Cdd:PRK09831    4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 468 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 539
Cdd:PRK09831   56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                         170
                  ....*....|....
gi 1958763045 540 -EEYVLDFYDKYYP 552
Cdd:PRK09831  132 rGEWFINFYMRYKP 145
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 477-539 4.20e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.55  E-value: 4.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958763045 477 VPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTLHV-SASNPAMllYQKFGFKT 539
Cdd:pfam13527  63 VPGKTLPAAGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFlYPSSYPI--YRRFGYEI 124
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 474-552 4.77e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763045 474 GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASN-PAMLLYQKFGFKTeeyvLDFYDK 549
Cdd:PRK09491   53 AFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVAtlwLEVRASNaAAIALYESLGFNE----VTIRRN 128


                  ...
gi 1958763045 550 YYP 552
Cdd:PRK09491  129 YYP 131
 
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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