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Conserved domains on  [gi|2263699705|ref|WP_253104196|]
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MULTISPECIES: DapH/DapD/GlmU-related protein [unclassified Pseudoalteromonas]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
31-177 4.24e-35

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.36  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  31 SLFGIERISLGDNVRIDDFCILSAGseGITLGSYIHIGAYSSLIGDSAIILEDYAGLSARVTIYSSSDDYSgewmtnptv 110
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYGG--NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID--------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2263699705 111 DEAFTNVTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRSR 177
Cdd:COG0110    71 DPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
31-177 4.24e-35

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.36  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  31 SLFGIERISLGDNVRIDDFCILSAGseGITLGSYIHIGAYSSLIGDSAIILEDYAGLSARVTIYSSSDDYSgewmtnptv 110
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYGG--NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID--------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2263699705 111 DEAFTNVTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRSR 177
Cdd:COG0110    71 DPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 37-172 4.13e-28

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 101.38  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  37 RISLGDNVRIDDFCILSAGsEGITLGSYIHIGAYssligdsaiiledyaglsarVTIYSSSDDYsgewmtNPTVDEAFTN 116
Cdd:cd04647     1 NISIGDNVYIGPGCVISAG-GGITIGDNVLIGPN--------------------VTIYDHNHDI------DDPERPIEQG 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2263699705 117 VTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFV 172
Cdd:cd04647    54 VTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 33-175 3.19e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 70.29  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  33 FGIERISLGDNVRIDDfcilsagsegitlgsYIHIGAYSSL-IGDSAIILEdyaglSARVTIYSSSDDYSGEWMTNPTVD 111
Cdd:PRK09677   61 FGRGKLFFGDNVQVND---------------YVHIACIESItIGRDTLIAS-----KVFITDHNHGSFKHSDDFSSPNLP 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2263699705 112 EAFTNVTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSR 175
Cdd:PRK09677  121 PDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 25-169 4.16e-12

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 62.13  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  25 LVSRKASLFgiERISLGDNVRIDDFCILSAGSegiTLGSYIHIGAYSSLIGDSAIilEDYAGLSARVTIysssddySGEw 104
Cdd:TIGR03570  89 LIHPSAIVS--PSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAIVEHDCVI--GDFVHIAPGVTL-------SGG- 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705 105 mtnptvdeaftnvtskpVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPA 169
Cdd:TIGR03570 154 -----------------VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
31-177 4.24e-35

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.36  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  31 SLFGIERISLGDNVRIDDFCILSAGseGITLGSYIHIGAYSSLIGDSAIILEDYAGLSARVTIYSSSDDYSgewmtnptv 110
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYGG--NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID--------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2263699705 111 DEAFTNVTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRSR 177
Cdd:COG0110    71 DPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 37-172 4.13e-28

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 101.38  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  37 RISLGDNVRIDDFCILSAGsEGITLGSYIHIGAYssligdsaiiledyaglsarVTIYSSSDDYsgewmtNPTVDEAFTN 116
Cdd:cd04647     1 NISIGDNVYIGPGCVISAG-GGITIGDNVLIGPN--------------------VTIYDHNHDI------DDPERPIEQG 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2263699705 117 VTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFV 172
Cdd:cd04647    54 VTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 20-173 1.18e-16

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 72.15  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  20 VGDNCLVSRKASlfgIER-ISLGDNVRIDDFCILSAGSegiTLGSYIHIGAYSSLIGDsaiiledyaglsarvtIYSSSD 98
Cdd:cd03358     1 IGDNCIIGTNVF---IENdVKIGDNVKIQSNVSIYEGV---TIEDDVFIGPNVVFTND----------------LYPRSK 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705  99 DYSGEWMtnptvdeaftnvtsKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVK 173
Cdd:cd03358    59 IYRKWEL--------------KGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 118-170 2.10e-16

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 72.84  E-value: 2.10e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2263699705 118 TSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPAR 170
Cdd:cd03357   115 YAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPAR 167
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 65-172 6.65e-16

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 69.94  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  65 IHIGAYSSlIGDSAII-------LEDYAGLSARVTIYSSSDDYSgewmtnptvDEAFTNVTsKPVYLGKHCIIGAGAIVL 137
Cdd:cd05825     4 LTIGDNSW-IGEGVWIynlapvtIGSDACISQGAYLCTGSHDYR---------SPAFPLIT-APIVIGDGAWVAAEAFVG 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2263699705 138 PGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFV 172
Cdd:cd05825    73 PGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 33-175 3.19e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 70.29  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  33 FGIERISLGDNVRIDDfcilsagsegitlgsYIHIGAYSSL-IGDSAIILEdyaglSARVTIYSSSDDYSGEWMTNPTVD 111
Cdd:PRK09677   61 FGRGKLFFGDNVQVND---------------YVHIACIESItIGRDTLIAS-----KVFITDHNHGSFKHSDDFSSPNLP 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2263699705 112 EAFTNVTSKPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSR 175
Cdd:PRK09677  121 PDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 62-175 3.50e-15

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 69.11  E-value: 3.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  62 GSYIHIGAYSSlIGDSAIILEDyaGLSARVTIYSSSDDYSGEWMTNPTVDEAFTnvTSKPVYLGKHCIIGAGAIVLPGVT 141
Cdd:cd03349    19 GDKLSIGKFCS-IAPGVKIGLG--GNHPTDWVSTYPFYIFGGEWEDDAKFDDWP--SKGDVIIGNDVWIGHGATILPGVT 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2263699705 142 LKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSR 175
Cdd:cd03349    94 IGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
PRK10502 PRK10502
putative acyl transferase; Provisional
 64-176 4.75e-14

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 66.90  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  64 YIHIGAYSsLIGDSA-------IILEDYAGLSARVTIYSSSDDYSgewmtnptvDEAFTNVTsKPVYLGKHCIIGAGAIV 136
Cdd:PRK10502   71 KLTIGDYA-WIGDDVwlynlgeITIGAHCVISQKSYLCTGSHDYS---------DPHFDLNT-APIVIGEGCWLAADVFV 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2263699705 137 LPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRS 176
Cdd:PRK10502  140 APGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRV 179
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 25-169 4.16e-12

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 62.13  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  25 LVSRKASLFgiERISLGDNVRIDDFCILSAGSegiTLGSYIHIGAYSSLIGDSAIilEDYAGLSARVTIysssddySGEw 104
Cdd:TIGR03570  89 LIHPSAIVS--PSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAIVEHDCVI--GDFVHIAPGVTL-------SGG- 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705 105 mtnptvdeaftnvtskpVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPA 169
Cdd:TIGR03570 154 -----------------VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 40-168 1.84e-10

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 57.49  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  40 LGDNVRIDDFCILSAGSegiTLGSYIHIGAYS-----SLIG-DSaiILEDYAGLSARVTIysssddySGEwmtnptvdea 113
Cdd:cd03360    93 VSPSAVIGEGCVIMAGA---VINPDARIGDNViintgAVIGhDC--VIGDFVHIAPGVVL-------SGG---------- 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705 114 ftnvtskpVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSP 168
Cdd:cd03360   151 --------VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 124-178 6.01e-10

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 55.47  E-value: 6.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRSRA 178
Cdd:COG1045   120 IGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK 174
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 123-187 3.17e-09

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.49  E-value: 3.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2263699705 123 YLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVT--RSVDEFKIVAGSPARFVksrsRALLEKEKAFK 187
Cdd:COG0663    90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVV----RELTEEEIAFL 152
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 20-186 4.01e-09

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 52.80  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  20 VGDNCLVSRKASLFGieRISLGDNVRIDDFCILSAGSEgitlgsYIHIGAYSSlIGDSAIILEDYaglSARVTIysssdd 99
Cdd:cd04645     2 IDPSAFIAPNATVIG--DVTLGEGSSVWFGAVLRGDVN------PIRIGERTN-IQDGSVLHVDP---GYPTII------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705 100 ysGEWMT---NPTVdEAFTnvtskpvyLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVT--RSVDEFKIVAGSPARFVks 174
Cdd:cd04645    64 --GDNVTvghGAVL-HGCT--------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVV-- 130

                         170
                  ....*....|..
gi 2263699705 175 rsRALLEKEKAF 186
Cdd:cd04645   131 --RELTDEEIAE 140
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 120-173 6.18e-09

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 52.89  E-value: 6.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2263699705 120 KPVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVK 173
Cdd:PRK10092  128 KPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 124-168 2.37e-07

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 47.05  E-value: 2.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSP 168
Cdd:cd03354    57 IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 124-170 4.08e-07

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.86  E-value: 4.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPAR 170
Cdd:COG1044   261 IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 124-170 2.67e-06

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.86  E-value: 2.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPAR 170
Cdd:cd03352   153 IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 60-186 5.88e-06

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 44.99  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  60 TLGSYIHIGA--YS----SLIGDSAIILEDYAGLSARVTIYSSSDDYSGEWMTNptvDEAFtnvtSKPVYLGKHCIIGAG 133
Cdd:PRK09527   71 SYGSNIHIGRnfYAnfnlTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKN---GEMY----SFPITIGNNVWIGSH 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2263699705 134 AIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVksrsRALLEKEKAF 186
Cdd:PRK09527  144 VVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI----REINDRDKQY 192
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 124-170 6.83e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 6.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEF-KIVAGSPAR 170
Cdd:PRK00892  264 IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQ 311
PLN02296 PLN02296
carbonate dehydratase
 109-186 4.33e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 42.80  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705 109 TV-DEAFtnvtskpvylgkhciIGAGAIVLPGVTLKEGVAVGAQSLVTRS--VDEFKIVAGSPARFVksrsRALLEKEKA 185
Cdd:PLN02296  138 TVeDEAF---------------VGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFL----RKLTEEEIA 198


                  .
gi 2263699705 186 F 186
Cdd:PLN02296  199 F 199
PLN02694 PLN02694
serine O-acetyltransferase
 124-183 5.07e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 42.71  E-value: 5.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFVKSRSRALLEKE 183
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKPAKHEE 274
cysE PRK11132
serine acetyltransferase; Provisional
 129-172 7.00e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 41.99  E-value: 7.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2263699705 129 IIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFV 172
Cdd:PRK11132  201 MIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 59-189 7.72e-05

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.20  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  59 ITLGSYIHIGAYSSLIGD-SAIILEDYAGLSARVTIYSSSDDysgewmtnPTVDEAFTNVTSKPV----YLGKHCIIGAG 133
Cdd:cd04745    19 VIIGKNCYIGPHASLRGDfGRIVIRDGANVQDNCVIHGFPGQ--------DTVLEENGHIGHGAIlhgcTIGRNALVGMN 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2263699705 134 AIVLPGVTLKEGVAVGAQSLVTRS--VDEFKIVAGSPARFVksrsRALLEKEKAFKGQ 189
Cdd:cd04745    91 AVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVI----RELSDEEVAWKTR 144
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 26-174 8.93e-05

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 41.05  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  26 VSRKASLFGIERISLGDNVRIDDFCILSAGSEGITLGSYihigaysSLIGDSAIILEDYaglsarvTIYSSSDDYS---- 101
Cdd:cd03359    10 VSRKSVICGSQNIVLNGKTIIQSDVIIRGDLATVSIGRY-------CILSEGCVIRPPF-------KKFSKGVAFFplhi 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2263699705 102 GE--WMTNPTVDEAfTNVTSKpVYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTrsvdEFKIVAGSPARFVKS 174
Cdd:cd03359    76 GDyvFIGENCVVNA-AQIGSY-VHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIP----PYSVVSGRPARFIGE 144
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 124-173 2.51e-04

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 2.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVT--RSVDEFKIVAGSPARFVK 173
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVR 132
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 59-166 1.15e-03

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 37.75  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  59 ITLGSYIHIGAYsslIGDSAIIlEDYAGLSARVTIysssddysGEWMT---NPTVDEAFTNVTSKPVYLGKHCIIGAGAI 135
Cdd:cd03350    22 LMMPSYVNIGAY---VDEGTMV-DSWATVGSCAQI--------GKNVHlsaGAVIGGVLEPLQATPVIIEDDVFIGANCE 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2263699705 136 VLPGVTLKEGVAVGAQSLVTRSVDEFKIVAG 166
Cdd:cd03350    90 VVEGVIVGKGAVLAAGVVLTQSTPIYDRETG 120
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 122-169 1.60e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 38.58  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2263699705 122 VYLGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTR--SVDEFKIVAGSPA 169
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
PLN02357 PLN02357
serine acetyltransferase
 124-172 2.54e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 37.55  E-value: 2.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2263699705 124 LGKHCIIGAGAIVLPGVTLKEGVAVGAQSLVTRSVDEFKIVAGSPARFV 172
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 39-136 7.48e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.15  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263699705  39 SLGDNVRIDDFCILSAGSE---GITLGSYIHIGAYSSlIGDSAIIledyaglSARVTIYSSsddysgewmtnptvdeaft 115
Cdd:COG1044   110 KIGEGVSIGPFAVIGAGVVigdGVVIGPGVVIGDGVV-IGDDCVL-------HPNVTIYER------------------- 162

                          90       100
                  ....*....|....*....|.
gi 2263699705 116 nvtskpVYLGKHCIIGAGAIV 136
Cdd:COG1044   163 ------CVIGDRVIIHSGAVI 177
 
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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