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Conserved domains on  [gi|644351516|ref|WP_025301961|]
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MULTISPECIES: GNAT family N-acetyltransferase [Serratia]

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

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-171 2.10e-64

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 195.21  E-value: 2.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  12 DATPDDMAAVLQIYTHHVLYGAASFEEQPPTLAEMQLRLGKVREAGLPWLVAKSEGRVMGYCYATPYRPRPAYRFTVEDS 91
Cdd:COG1247    6 PATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEES 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  92 VYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSaaNHGSLALHQSLGFTSAGTLKAVGFKLGEWRDTQIMQRAL 171
Cdd:COG1247   86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-171 2.10e-64

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 195.21  E-value: 2.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  12 DATPDDMAAVLQIYTHHVLYGAASFEEQPPTLAEMQLRLGKVREAGLPWLVAKSEGRVMGYCYATPYRPRPAYRFTVEDS 91
Cdd:COG1247    6 PATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEES 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  92 VYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSaaNHGSLALHQSLGFTSAGTLKAVGFKLGEWRDTQIMQRAL 171
Cdd:COG1247   86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-145 6.00e-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: 59.45  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   44 AEMQLRLGKVREAGLPWLVAKSEGRVMGYCYATPYRPRPayRFTVEDSVYIAEGQQGKGVGKALLSALIARC-EQGPWRQ 122
Cdd:pfam00583  19 EPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWArERGCERI 96

                          90       100
                  ....*....|....*....|...
gi 644351516  123 MLAIVgdsAANHGSLALHQSLGF 145
Cdd:pfam00583  97 FLEVA---ADNLAAIALYEKLGF 116
PRK10140 PRK10140
N-acetyltransferase;
13-169 1.44e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  13 ATPDDMAAVLQIYTHHVLYgAASFEEQPPTLAEMQLRLGKvrEAGLPWLVAKSEGRVMGY-CYATPYRPRpayRFTVED- 90
Cdd:PRK10140   9 AETRDYEAIRQIHAQPEVY-HNTLQVPHPSDHMWQERLAD--RPGIKQLVACIDGDVVGHlTIDVQQRPR---RSHVADf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  91 SVYIAEGQQGKGVGKALLSALIARCEQgpW----RQMLAIVGDsaaNHGSLALHQSLGFTSAGTLKAVGFKLGEWRDTQI 166
Cdd:PRK10140  83 GICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYY 157


                 ...
gi 644351516 167 MQR 169
Cdd:PRK10140 158 MAR 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-117 1.15e-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: 41.49  E-value: 1.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 644351516  60 WLVAKSEGRVMGYCYATPYRPRPaYRFTVEDsVYIAEGQQGKGVGKALLSALIARCEQ 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG-DTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-171 2.10e-64

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 195.21  E-value: 2.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  12 DATPDDMAAVLQIYTHHVLYGAASFEEQPPTLAEMQLRLGKVREAGLPWLVAKSEGRVMGYCYATPYRPRPAYRFTVEDS 91
Cdd:COG1247    6 PATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEES 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  92 VYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSaaNHGSLALHQSLGFTSAGTLKAVGFKLGEWRDTQIMQRAL 171
Cdd:COG1247   86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLAD--NEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-173 2.59e-15

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: 69.64  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   1 MTLSAPVLSLLDATPDDMAAVLQIYTHHVLygAASFEEQPPTLAEMQLRLGKVREA-----GLPWLVA-KSEGRVMGYCy 74
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEV--ARYLPGPPYSLEEARAWLERLLADwadggALPFAIEdKEDGELIGVV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  75 aTPYRPRPAYRfTVEDSVYIAEGQQGKGVGKALLSALIARC-EQGPWRQMLAIVgdSAANHGSLALHQSLGFTSAGTLKA 153
Cdd:COG1670   78 -GLYDIDRANR-SAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEV--DPDNTASIRVLEKLGFRLEGTLRD 153

                        170       180
                 ....*....|....*....|
gi 644351516 154 VGFKLGEWRDTQIMQRALGD 173
Cdd:COG1670  154 ALVIDGRYRDHVLYSLLREE 173
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 44-145 6.00e-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: 59.45  E-value: 6.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   44 AEMQLRLGKVREAGLPWLVAKSEGRVMGYCYATPYRPRPayRFTVEDSVYIAEGQQGKGVGKALLSALIARC-EQGPWRQ 122
Cdd:pfam00583  19 EPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIEGLAVAPEYRGKGIGTALLQALLEWArERGCERI 96

                          90       100
                  ....*....|....*....|...
gi 644351516  123 MLAIVgdsAANHGSLALHQSLGF 145
Cdd:pfam00583  97 FLEVA---ADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-151 3.20e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 52.78  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  13 ATPDDMAAVLQIYthhvlygAASFEeqPPTLAEMQLRLGKVREAGLPWlVAKSEGRVMGYCYATPYRPRPAYRFTVEDSV 92
Cdd:COG3153    4 ATPEDAEAIAALL-------RAAFG--PGREAELVDRLREDPAAGLSL-VAEDDGEIVGHVALSPVDIDGEGPALLLGPL 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 644351516  93 YIAEGQQGKGVGKALLSALIARCEQGPWRQMLaIVGDSaanhGSLALHQSLGFTSAGTL 151
Cdd:COG3153   74 AVDPEYRGQGIGRALMRAALEAARERGARAVV-LLGDP----SLLPFYERFGFRPAGEL 127
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
13-163 5.99e-09

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 52.37  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   13 ATPDDMAAVLQIYTHHVLYGAASFEEQPPTLAEMQLRL-GKVREAGLPWLVAKSEgRVMGYCYATPYRPRpaYRFTVEDS 91
Cdd:pfam13420   4 LTQNDLKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLaAYLSPGEIVFGVAESD-RLIGYATLRQFDYV--KTHKAELS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644351516   92 VYIAEGQQgKGVGKALLSALI--ARCEQGPWRQMLAIVgdsAANHGSLALHQSLGFTSAGTLKAVGFKLGEWRD 163
Cdd:pfam13420  81 FYVVKNND-EGINRELINAIIqyARKNQNIENLEACIA---SNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 12-171 4.74e-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: 49.22  E-value: 4.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  12 DATPDDMAAVLQIYTHHVLYgaasfeeqpptlaemqlrlgkvrEAGLPWLVAKSEGRVMGYCYATPYRPRpayrfTVE-D 90
Cdd:COG1246    5 PATPDDVPAILELIRPYALE-----------------------EEIGEFWVAEEDGEIVGCAALHPLDED-----LAElR 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  91 SVYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSAAnhgslALHQSLGFTSAGTlKAVGFKLGEWRDTQIMQRA 170
Cdd:COG1246   57 SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAI-----HFYEKLGFEEIDK-EDLPYAKVWQRDSVVMEKD 130


                 .
gi 644351516 171 L 171
Cdd:COG1246  131 L 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 61-146 5.19e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.22  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   61 LVAKSEGRVMGYCYATPYrprPAYRFTVEDSVYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSAAnhgslALH 140
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPL---DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAA-----AFY 77


                  ....*.
gi 644351516  141 QSLGFT 146
Cdd:pfam13508  78 EKLGFE 83
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 71-171 1.22e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.34  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  71 GYCYATPYRPRPAYRFtveDSVYIAEGQQGKGVGKALLSALIARCEQGPWRQMLAIVGDSaaNHGSLALHQSLGFTSAGT 150
Cdd:COG0456    1 GFALLGLVDGGDEAEI---EDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVRED--NEAAIALYEKLGFEEVGE 75

                         90       100
                 ....*....|....*....|.
gi 644351516 151 LKAVGfklgeWRDTQIMQRAL 171
Cdd:COG0456   76 RPNYY-----GDDALVMEKEL 91
PRK10140 PRK10140
N-acetyltransferase;
13-169 1.44e-07

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  13 ATPDDMAAVLQIYTHHVLYgAASFEEQPPTLAEMQLRLGKvrEAGLPWLVAKSEGRVMGY-CYATPYRPRpayRFTVED- 90
Cdd:PRK10140   9 AETRDYEAIRQIHAQPEVY-HNTLQVPHPSDHMWQERLAD--RPGIKQLVACIDGDVVGHlTIDVQQRPR---RSHVADf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516  91 SVYIAEGQQGKGVGKALLSALIARCEQgpW----RQMLAIVGDsaaNHGSLALHQSLGFTSAGTLKAVGFKLGEWRDTQI 166
Cdd:PRK10140  83 GICVDSRWKNRGVASALMREMIEMCDN--WlrvdRIELTVFVD---NAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYY 157


                 ...
gi 644351516 167 MQR 169
Cdd:PRK10140 158 MAR 160
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 8-153 3.43e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 44.27  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   8 LSLLDATPDDMAAVLQIythhvlygaasfEEQPPTLAEMqlrLGKVREAGlpWLVAKSEGRVMGYCYATPYRPRPAYrft 87
Cdd:COG0454    1 MSIRKATPEDINFILLI------------EALDAELKAM---EGSLAGAE--FIAVDDKGEPIGFAGLRRLDDKVLE--- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644351516  88 VEDsVYIAEGQQGKGVGKALLSALI--ARcEQGPWRQMLAIVgdsAANHGSLALHQSLGFTSAGTLKA 153
Cdd:COG0454   61 LKR-LYVLPEYRGKGIGKALLEALLewAR-ERGCTALELDTL---DGNPAAIRFYERLGFKEIERYVA 123
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-117 1.15e-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: 41.49  E-value: 1.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 644351516  60 WLVAKSEGRVMGYCYATPYRPRPaYRFTVEDsVYIAEGQQGKGVGKALLSALIARCEQ 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGG-DTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARE 56
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 99-145 2.03e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.53  E-value: 2.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 644351516  99 QGKGVGKALLSALIARCEQgpwRQMLAI---VGDSaaNHGSLALHQSLGF 145
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEK---RGVATLwleVRAS--NAAAIALYESLGF 120
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 14-146 6.80e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   14 TPDDMAAVLQIYTH-HVLYGAASFeeqPPTLAEMQLRLGKV-----REAGLPWLVAKSEGRVMGYCyatPYRPRPAYRFT 87
Cdd:pfam13302   8 TEEDAEALFELLSDpEVMRYGVPW---PLTLEEAREWLARIwaadeAERGYGWAIELKDTGFIGSI---GLYDIDGEPER 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516   88 VEDSVYIAEGQQGKGVGKALLSALIARC-EQGPWRQMLAIVgdSAANHGSLALHQSLGFT 146
Cdd:pfam13302  82 AELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARI--DPENTASRRVLEKLGFK 139
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 100-155 1.47e-03

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 37.84  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 644351516 100 GKG-VGKALLSALIARC--EQGpwRQMLAIVGDSAANhgslaLHQSLGFT-SAGTLKAVG 155
Cdd:COG3640    7 GKGgVGKTTLSALLARYlaEKG--KPVLAVDADPNAN-----LAEALGLEvEADLIKPLG 59
 
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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