|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
206-441 |
1.06e-135 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 389.43 E-value: 1.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 206 TLYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGG 285
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 286 GIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALrniaRDVPGITGVIVGRALYDGRISLGDA 441
Cdd:PRK00748 162 AIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKAL----KGLGAVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
206-446 |
1.98e-128 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 370.91 E-value: 1.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 206 TLYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGG 285
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 286 GIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDALNVL 445
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL-----GVEGAIVGKALYEGKIDLEEALALA 235
|
.
gi 2035452869 446 G 446
Cdd:COG0106 236 R 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
207-442 |
5.07e-115 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 336.76 E-value: 5.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:cd04732 2 IIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPG-RIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:cd04732 82 IRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDAL 442
Cdd:cd04732 162 AIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL-----GVAGVIVGKALYEGKITLEEAL 233
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
207-437 |
4.59e-102 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 303.63 E-value: 4.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:pfam00977 2 IIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPG-RIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:pfam00977 82 IRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGAG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNiardvPGITGVIVGRALYDGRIS 437
Cdd:pfam00977 162 EILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFT-----EGVDGVIAGSALYEGEIT 228
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
207-440 |
2.11e-98 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 294.11 E-value: 2.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAY-PGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGD 440
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL-----GVYGVIVGKALYEGKITLEE 230
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
14-171 |
1.37e-18 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 82.73 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 14 PDDLENLIEATTAGILDGGGFGWVQPPGNQALARYFEGLLLvPERSLYVVRDEGVICGAgQVVRPPASYEAHAATANITg 93
Cdd:COG1247 9 PEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILA-PGRPVLVAEEDGEVVGF-ASLGPFRPRPAYRGTAEES- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452869 94 FFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHPYYARIGGQTVRGLFLSKLL 171
Cdd:COG1247 86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
39-145 |
6.66e-13 |
|
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: 64.85 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 39 PPGNQALARYFEGLLLVPERSLYVVRDEGVICGAGqVVRPPASYEAHAAtanITGFFVAPYARGRGLGRALVKAMLQGAR 118
Cdd:pfam00583 14 EPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA-SLSIIDDEPPVGE---IEGLAVAPEYRGKGIGTALLQALLEWAR 89
|
90 100
....*....|....*....|....*..
gi 2035452869 119 SLGCKVVNCDVRETHATAIGLFRSLGF 145
Cdd:pfam00583 90 ERGCERIFLEVAADNLAAIALYEKLGF 116
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
88-154 |
5.82e-09 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 54.26 E-value: 5.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452869 88 TANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHP-YY 154
Cdd:TIGR01575 54 EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRnYY 121
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
60-125 |
1.28e-07 |
|
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: 48.43 E-value: 1.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 60 LYVVRDEGVICGAGQVVRPPASYEahaaTANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVV 125
Cdd:cd04301 1 FLVAEDDGEIVGFASLSPDGSGGD----TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
|
|
| PRK07757 |
PRK07757 |
N-acetyltransferase; |
43-146 |
2.20e-06 |
|
N-acetyltransferase;
Pssm-ID: 236088 [Multi-domain] Cd Length: 152 Bit Score: 47.11 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 43 QALARYF--EGLLLvpERSL----------YVVRDEGVICGAGQVvrppasyeaHAAT---ANITGFFVAPYARGRGLGR 107
Cdd:PRK07757 16 HALINVYakKGLML--PRSLdelyenirdfYVAEEEGEIVGCCAL---------HILWedlAEIRSLAVSEDYRGQGIGR 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 2035452869 108 ALVKAMLQGARSLGCKVVNCDVREThataiGLFRSLGFE 146
Cdd:PRK07757 85 MLVEACLEEARELGVKRVFALTYQP-----EFFEKLGFR 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
206-441 |
1.06e-135 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 389.43 E-value: 1.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 206 TLYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGG 285
Cdd:PRK00748 2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 286 GIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:PRK00748 82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALrniaRDVPGITGVIVGRALYDGRISLGDA 441
Cdd:PRK00748 162 AIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKAL----KGLGAVEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
206-446 |
1.98e-128 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 370.91 E-value: 1.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 206 TLYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGG 285
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 286 GIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDALNVL 445
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL-----GVEGAIVGKALYEGKIDLEEALALA 235
|
.
gi 2035452869 446 G 446
Cdd:COG0106 236 R 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
207-442 |
5.07e-115 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 336.76 E-value: 5.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:cd04732 2 IIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPG-RIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:cd04732 82 IRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGVK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDAL 442
Cdd:cd04732 162 AIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL-----GVAGVIVGKALYEGKITLEEAL 233
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
207-437 |
4.59e-102 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 303.63 E-value: 4.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:pfam00977 2 IIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPG-RIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:pfam00977 82 IRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSqCIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGAG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNiardvPGITGVIVGRALYDGRIS 437
Cdd:pfam00977 162 EILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFT-----EGVDGVIAGSALYEGEIT 228
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
207-440 |
2.11e-98 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 294.11 E-value: 2.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAY-PGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGD 440
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL-----GVYGVIVGKALYEGKITLEE 230
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
208-447 |
7.46e-76 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 237.11 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 208 YPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGGI 287
Cdd:PRK13585 6 IPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 288 RDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQ-AARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVAA 366
Cdd:PRK13585 86 RSAEDAASLLDLGVDRVILGTAAVENPEIVRElSEEFGSERVMVSLDAKDGEVVIKGWTEKTGYTPVEAAKRFEELGAGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 367 VIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDALNVLG 446
Cdd:PRK13585 166 ILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEA-----GAAGVVVGSALYKGKFTLEEAIEAVK 240
|
.
gi 2035452869 447 S 447
Cdd:PRK13585 241 G 241
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
205-446 |
1.05e-49 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 168.98 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 205 LTLYPAIDLKDGACVRLRRGEMEDATHYSDdPAAQARMFEEAGCRHLHVVDLNGAFaGRSTNIPAIEAIVAATNLPVQLG 284
Cdd:PRK14024 4 LTLLPAVDVVDGQAVRLVQGEAGSETSYGS-PLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 285 GGIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEvselEATDL---ALRMED 361
Cdd:PRK14024 82 GGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTR----DGGDLwevLERLDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 362 AGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIARDvpGITGVIVGRALYDGRISLGDA 441
Cdd:PRK14024 158 AGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPL--GVEGAIVGKALYAGAFTLPEA 235
|
....*
gi 2035452869 442 LNVLG 446
Cdd:PRK14024 236 LAVVR 240
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
207-445 |
3.17e-43 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 151.85 E-value: 3.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDdPAAQARMFEEAgCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGG 286
Cdd:PRK04128 4 IYPAIDLMNGKAVRLYKGRKEEVKVYGD-PVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 287 IRDMAAIDRWLEAGVSRVILGSVAVkDPDLVRQAARAYPGrIVAGIDARMGRVATEGWAEVSELEATDlALRMEDAGVAA 366
Cdd:PRK04128 82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG-ITVSLDVKGGRIAVKGWLEESSIKVED-AYEMLKNYVNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 367 VIFTEITRDGMLAGLdldqtaDLARRL--SIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGDALNV 444
Cdd:PRK04128 159 FIYTSIERDGTLTGI------EEIERFwgDEEFIYAGGVSSAEDVKKLAEI-----GFSGVIIGKALYEGRISLEELLEV 227
|
.
gi 2035452869 445 L 445
Cdd:PRK04128 228 Q 228
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
207-442 |
2.33e-40 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 144.34 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATH------YSDDPAAQARMFEEAGCRHLHVVDLNgAFAGRSTNIPAIEAIVAATNLP 280
Cdd:cd04723 2 IIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLD-AIMGRGDNDEAIRELAAAWPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 281 VQLGGGIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRME 360
Cdd:cd04723 81 LWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLAALGEQRLVLSLDFRGGQLLKPTDFIGPEELLRRLAKWPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 361 DagvaaVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRISLGD 440
Cdd:cd04723 161 E-----LIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL-----GASGALVASALHDGGLTLED 230
|
..
gi 2035452869 441 AL 442
Cdd:cd04723 231 VV 232
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
207-430 |
7.62e-40 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 143.05 E-value: 7.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 207 LYPAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGC-RHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGG 285
Cdd:PRK13587 4 LWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQFECvNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 286 GIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVA 365
Cdd:PRK13587 84 GIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIPLG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452869 366 AVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRA 430
Cdd:PRK13587 164 GIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL-----NVHAAIIGKA 223
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
209-412 |
2.99e-36 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240082 Cd Length: 243 Bit Score: 133.36 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGACVRLRR-GEMEDAthysDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGGI 287
Cdd:cd04731 5 PCLDVKDGRVVKGVNfKNLRDA----GDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 288 RDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYpGR--IVAGIDAR-----MGRVATEGWAEVSELEATDLALRME 360
Cdd:cd04731 81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRF-GSqcVVVSIDAKrrgdgGYEVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2035452869 361 DAGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQAL 412
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEA 211
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
209-438 |
1.01e-35 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 132.06 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGACVRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNlPVQLGGGIR 288
Cdd:PRK14114 5 PAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 289 DMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAaRAYPGRIVAGIDARMGRVATEGWAEVSELEATDLALRMEDAGVAAVI 368
Cdd:PRK14114 84 SLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFL-KEIDVEPVFSLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEYGLEEIV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035452869 369 FTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIARDVPG-ITGVIVGRALYDGRISL 438
Cdd:PRK14114 163 HTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQRVHRETNGlLKGVIVGRAFLEGILTV 233
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
209-409 |
3.10e-35 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 130.91 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGACV------RLRrgemedathYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQ 282
Cdd:COG0107 7 PCLDVKDGRVVkgvnfvNLR---------DAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 283 LGGGIRDMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYpGR--IVAGIDARmgRVATEGWaEV--------SELEA 352
Cdd:COG0107 78 VGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERF-GSqcIVVAIDAK--RVPDGGW-EVythggrkpTGLDA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452869 353 TDLALRMEDAGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHL 409
Cdd:COG0107 154 VEWAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHF 210
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
209-408 |
4.36e-30 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 117.08 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGacvRLRRGEMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGGIR 288
Cdd:TIGR00735 8 PCLDVRDG---RVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGGIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 289 DMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPGR-IVAGIDARMGRVATEGWAEVS--------ELEATDLALRM 359
Cdd:TIGR00735 85 SIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQcIVVAIDAKRVYVNSYCWYEVYiyggrestGLDAVEWAKEV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2035452869 360 EDAGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSH 408
Cdd:TIGR00735 165 EKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEH 213
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
209-436 |
1.39e-23 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 98.66 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGACVRLRRGeMEDATHYSDDPAAQARMFEEAGCRHLHVVDLNGAfAGRSTNIPAIEAIVAATNLPVQLGGGIR 288
Cdd:PRK13586 6 PSIDISLGKAVKRIRG-VKGTGLILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 289 DMAAIDRWLEAGVSRVILGSVAVKDPDLVRQAARAYPG-RIVAGID-ARMGRVATEGWAEVSeLEATDLALRMEDAGVAA 366
Cdd:PRK13586 84 DIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSnRVLVSIDyDNTKRVLIRGWKEKS-MEVIDGIKKVNELELLG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 367 VIFTEITRDGMLAGLDlDQTADLARRLSIPVIASGGVGELSHLQALRNIardvpGITGVIVGRALYDGRI 436
Cdd:PRK13586 163 IIFTYISNEGTTKGID-YNVKDYARLIRGLKEYAGGVSSDADLEYLKNV-----GFDYIIVGMAFYLGKL 226
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
14-171 |
1.37e-18 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 82.73 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 14 PDDLENLIEATTAGILDGGGFGWVQPPGNQALARYFEGLLLvPERSLYVVRDEGVICGAgQVVRPPASYEAHAATANITg 93
Cdd:COG1247 9 PEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILA-PGRPVLVAEEDGEVVGF-ASLGPFRPRPAYRGTAEES- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452869 94 FFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHPYYARIGGQTVRGLFLSKLL 171
Cdd:COG1247 86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
80-154 |
9.52e-14 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 66.60 E-value: 9.52e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452869 80 ASYEAHAATANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHPYY 154
Cdd:COG0456 5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
52-163 |
6.59e-13 |
|
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: 65.40 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 52 LLLVPERSLYVVRDEGVICGAGQVVRPPASyeahaaTANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCdvrE 131
Cdd:COG1246 22 ALEEEIGEFWVAEEDGEIVGCAALHPLDED------LAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL---L 92
|
90 100 110
....*....|....*....|....*....|....
gi 2035452869 132 THATAIGLFRSLGFEH--WGTHPYYARIGGQTVR 163
Cdd:COG1246 93 TTSAAIHFYEKLGFEEidKEDLPYAKVWQRDSVV 126
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
39-145 |
6.66e-13 |
|
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: 64.85 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 39 PPGNQALARYFEGLLLVPERSLYVVRDEGVICGAGqVVRPPASYEAHAAtanITGFFVAPYARGRGLGRALVKAMLQGAR 118
Cdd:pfam00583 14 EPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFA-SLSIIDDEPPVGE---IEGLAVAPEYRGKGIGTALLQALLEWAR 89
|
90 100
....*....|....*....|....*..
gi 2035452869 119 SLGCKVVNCDVRETHATAIGLFRSLGF 145
Cdd:pfam00583 90 ERGCERIFLEVAADNLAAIALYEKLGF 116
|
|
| PLN02446 |
PLN02446 |
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
209-431 |
2.48e-10 |
|
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Pssm-ID: 215245 Cd Length: 262 Bit Score: 60.87 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 209 PAIDLKDGACVRLRRGEMEDATHY------------SDDPAAQ-ARMFEEAGCRHLHVVDLNgafAGRSTNIPAIEAIVA 275
Cdd:PLN02446 5 PCIDIHKGKVKQIVGSTLKDSKDGsedgselvtnfeSDKSAAEfAEMYKRDGLTGGHVIMLG---ADDASLAAALEALRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 276 ATNlPVQLGGGIRDMAAIdRWLEAGVSRVILGSVAVKD--------PDLVRQAARAypgRIVAGIDARM--GR--VATEG 343
Cdd:PLN02446 82 YPG-GLQVGGGVNSENAM-SYLDAGASHVIVTSYVFRDgqidlerlKDLVRLVGKQ---RLVLDLSCRKkdGRyyVVTDR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 344 WAEVSELEATDLALRMEDAGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSHLQALRNIARdvpGIT 423
Cdd:PLN02446 157 WQKFSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLERVKVAGG---GRV 233
|
....*...
gi 2035452869 424 GVIVGRAL 431
Cdd:PLN02446 234 DVTVGSAL 241
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
56-146 |
3.75e-10 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 56.31 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 56 PERSLYVVRDEGVICGAGQVVRppasYEAHAATANItGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCdvrETHAT 135
Cdd:pfam13508 1 PGGRFFVAEDDGKIVGFAALLP----LDDEGALAEL-RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEL---ETTNR 72
|
90
....*....|.
gi 2035452869 136 AIGLFRSLGFE 146
Cdd:pfam13508 73 AAAFYEKLGFE 83
|
|
| COG3393 |
COG3393 |
Predicted acetyltransferase, GNAT family [General function prediction only]; |
91-154 |
7.51e-10 |
|
Predicted acetyltransferase, GNAT family [General function prediction only];
Pssm-ID: 442620 [Multi-domain] Cd Length: 86 Bit Score: 55.30 E-value: 7.51e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035452869 91 ITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHPYY 154
Cdd:COG3393 18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
61-153 |
2.11e-09 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 55.86 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 61 YVVRDEGVICGAGQVVRPPASYEAHAATanITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVncdVRETHATAIGLF 140
Cdd:COG3153 42 LVAEDDGEIVGHVALSPVDIDGEGPALL--LGPLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFY 116
|
90
....*....|...
gi 2035452869 141 RSLGFEHWGTHPY 153
Cdd:COG3153 117 ERFGFRPAGELGL 129
|
|
| RimL |
COG1670 |
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ... |
9-170 |
5.68e-09 |
|
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441276 [Multi-domain] Cd Length: 173 Bit Score: 55.39 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 9 TSHFSPDDLENLIEATTAGILDGGGFGWVqppgnqalaryfeglllVperslyVVRDEGVICGAGQVVRPPAsyeaHAAT 88
Cdd:COG1670 36 GPPYSLEEARAWLERLLADWADGGALPFA-----------------I------EDKEDGELIGVVGLYDIDR----ANRS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 89 ANItGFFVAPYARGRGLGRALVKAMLQ-GARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHPYYARIGGQTVRGLFL 167
Cdd:COG1670 89 AEI-GYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167
|
...
gi 2035452869 168 SKL 170
Cdd:COG1670 168 SLL 170
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
88-154 |
5.82e-09 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 54.26 E-value: 5.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452869 88 TANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEHWGTHP-YY 154
Cdd:TIGR01575 54 EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRnYY 121
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
307-432 |
6.13e-09 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 56.35 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 307 GSVAVKDPDLVRQAARAypgrIVAGIDA------RMGrvategWAEvsELEATDLALRMEDAGVAAVIfteI---TRDGM 377
Cdd:cd02801 101 GAALLKDPELVAEIVRA----VREAVPIpvtvkiRLG------WDD--EEETLELAKALEDAGASALT---VhgrTREQR 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 378 LAG-LDLDQTADLARRLSIPVIASGGVGELSHLQALRNIArdvpGITGVIVGRALY 432
Cdd:cd02801 166 YSGpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQT----GVDGVMIGRGAL 217
|
|
| ElaA |
COG2153 |
Predicted N-acyltransferase, GNAT family [General function prediction only]; |
61-146 |
6.45e-09 |
|
Predicted N-acyltransferase, GNAT family [General function prediction only];
Pssm-ID: 441756 [Multi-domain] Cd Length: 134 Bit Score: 54.03 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 61 YVVRDEGVICGAGqVVRPPASYEAHaatanITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRethATAIGLF 140
Cdd:COG2153 37 LLAYDDGELVATA-RLLPPGDGEAK-----IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQ---AHAVGFY 107
|
....*.
gi 2035452869 141 RSLGFE 146
Cdd:COG2153 108 EKLGFV 113
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
46-158 |
3.27e-08 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 51.98 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 46 ARYFEGLLLVPERSLYVVRDEGVICGAGQVvrppaSYEAHAaTANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVV 125
Cdd:COG0454 22 AELKAMEGSLAGAEFIAVDDKGEPIGFAGL-----RRLDDK-VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTAL 95
|
90 100 110
....*....|....*....|....*....|...
gi 2035452869 126 NCDVRETHATAIGLFRSLGFEHWGTHPYYARIG 158
Cdd:COG0454 96 ELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
307-432 |
5.90e-08 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 53.94 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 307 GSVAVKDPDLVRQAARAypgrIVAGIDA------RMGrvategWAEvSELEATDLALRMEDAGVAAVIfteI---TRDGM 377
Cdd:COG0042 108 GAALLRDPELVAEIVKA----VVEAVDVpvtvkiRLG------WDD-DDENALEFARIAEDAGAAALT---VhgrTREQR 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 378 LAG-LDLDQTADLARRLSIPVIASGGVGELShlQALRniARDVPGITGVIVGRALY 432
Cdd:COG0042 174 YKGpADWDAIARVKEAVSIPVIGNGDIFSPE--DAKR--MLEETGCDGVMIGRGAL 225
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
60-125 |
1.28e-07 |
|
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: 48.43 E-value: 1.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 60 LYVVRDEGVICGAGQVVRPPASYEahaaTANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVV 125
Cdd:cd04301 1 FLVAEDDGEIVGFASLSPDGSGGD----TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
|
|
| PRK07757 |
PRK07757 |
N-acetyltransferase; |
43-146 |
2.20e-06 |
|
N-acetyltransferase;
Pssm-ID: 236088 [Multi-domain] Cd Length: 152 Bit Score: 47.11 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 43 QALARYF--EGLLLvpERSL----------YVVRDEGVICGAGQVvrppasyeaHAAT---ANITGFFVAPYARGRGLGR 107
Cdd:PRK07757 16 HALINVYakKGLML--PRSLdelyenirdfYVAEEEGEIVGCCAL---------HILWedlAEIRSLAVSEDYRGQGIGR 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 2035452869 108 ALVKAMLQGARSLGCKVVNCDVREThataiGLFRSLGFE 146
Cdd:PRK07757 85 MLVEACLEEARELGVKRVFALTYQP-----EFFEKLGFR 118
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
307-432 |
5.29e-06 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 48.09 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 307 GSVAVKDPDL----VRQAARAYPgrIVAGIDARMGrvategWAEvSELEATDLALRMEDAGVAAVIFTEITRDGMLAG-L 381
Cdd:pfam01207 100 GAALLRNPDLvaqiVKAVVKAVG--IPVTVKIRIG------WDD-SHENAVEIAKIVEDAGAQALTVHGRTRAQNYEGtA 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2035452869 382 DLDQTADLARRLSIPVIASGGVGELSHLQAlrniARDVPGITGVIVGRALY 432
Cdd:pfam01207 171 DWDAIKQVKQAVSIPVIANGDITDPEDAQR----CLAYTGADGVMIGRGAL 217
|
|
| PRK03624 |
PRK03624 |
putative acetyltransferase; Provisional |
96-147 |
5.37e-06 |
|
putative acetyltransferase; Provisional
Pssm-ID: 235142 [Multi-domain] Cd Length: 140 Bit Score: 45.69 E-value: 5.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2035452869 96 VAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGFEH 147
Cdd:PRK03624 76 VHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEE 127
|
|
| Acetyltransf_10 |
pfam13673 |
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ... |
60-146 |
8.94e-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: 44.95 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 60 LYVVRDEGVICGAGQVVRppasyEAHaatanITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVREtHATAIGL 139
Cdd:pfam13673 33 FFVAFEGGQIVGVIALRD-----RGH-----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNA-SPYAVPF 101
|
....*..
gi 2035452869 140 FRSLGFE 146
Cdd:pfam13673 102 YEKLGFR 108
|
|
| YidJ |
COG2388 |
Predicted acetyltransferase, GNAT superfamily [General function prediction only]; |
56-125 |
2.16e-05 |
|
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
Pssm-ID: 441953 [Multi-domain] Cd Length: 88 Bit Score: 42.83 E-value: 2.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 56 PERSLYVVRDEGVICGAgqvvrppASYEAHAATANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVV 125
Cdd:COG2388 7 EEKGRFELEVDGELAGE-------LTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVV 69
|
|
| PRK10514 |
PRK10514 |
putative acetyltransferase; Provisional |
95-152 |
1.07e-04 |
|
putative acetyltransferase; Provisional
Pssm-ID: 182510 [Multi-domain] Cd Length: 145 Bit Score: 42.30 E-value: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2035452869 95 FVAPYARGRGLGRALVKAMLQGARSLgckvvNCDVRETHATAIGLFRSLGFEHWGTHP 152
Cdd:PRK10514 76 FVDPDVRGCGVGRMLVEHALSLHPEL-----TTDVNEQNEQAVGFYKKMGFKVTGRSE 128
|
|
| PRK10415 |
PRK10415 |
tRNA-dihydrouridine synthase B; Provisional |
268-430 |
1.10e-04 |
|
tRNA-dihydrouridine synthase B; Provisional
Pssm-ID: 182440 Cd Length: 321 Bit Score: 44.19 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 268 PAIEAIVAATNLPVQLGGGIRDMAA-----IDrwLEAG-----VSRVILGSVAVKDPDLVRQAARAypgrIVAGIDARMG 337
Cdd:PRK10415 64 PGIRTVQIAGSDPKEMADAARINVEsgaqiID--INMGcpakkVNRKLAGSALLQYPDLVKSILTE----VVNAVDVPVT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 338 RVATEGWAEvSELEATDLALRMEDAGVAAVIFTEITRDGMLAG-LDLDQTADLARRLSIPVIASGGVGELSHLQALrnia 416
Cdd:PRK10415 138 LKIRTGWAP-EHRNCVEIAQLAEDCGIQALTIHGRTRACLFNGeAEYDSIRAVKQKVSIPVIANGDITDPLKARAV---- 212
|
170
....*....|....
gi 2035452869 417 RDVPGITGVIVGRA 430
Cdd:PRK10415 213 LDYTGADALMIGRA 226
|
|
| Acetyltransf_CG |
pfam14542 |
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ... |
80-125 |
2.15e-04 |
|
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: 39.81 E-value: 2.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2035452869 80 ASYEAHAATANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVV 125
Cdd:pfam14542 15 LTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIV 60
|
|
| rimI |
PRK09491 |
ribosomal-protein-alanine N-acetyltransferase; Provisional |
90-145 |
2.24e-04 |
|
ribosomal-protein-alanine N-acetyltransferase; Provisional
Pssm-ID: 181904 [Multi-domain] Cd Length: 146 Bit Score: 41.45 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2035452869 90 NITgffVAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVRETHATAIGLFRSLGF 145
Cdd:PRK09491 68 NIA---VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
352-408 |
5.90e-04 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 42.01 E-value: 5.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2035452869 352 ATDLALRMEDAGVAAVIFTEITRDGMLAGLDLDQTADLARRLSIPVIASGGVGELSH 408
Cdd:PLN02617 440 AYELAKAVEELGAGEILLNCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEH 496
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
234-328 |
7.32e-04 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 41.69 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 234 DDPAAQARMFEEAGCRHLHVV-------DLNGAFAGRSTNIPAIEAIVAATNLPVQLGGGIRDMAAIDRWLEAGVSRVI- 305
Cdd:COG1902 236 EESVELAKALEEAGVDYLHVSsggyepdAMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVa 315
|
90 100
....*....|....*....|...
gi 2035452869 306 LGSVAVKDPDLVRQAARAYPGRI 328
Cdd:COG1902 316 LGRPLLADPDLPNKAAAGRGDEI 338
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
234-322 |
9.22e-04 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 41.02 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 234 DDPAAQARMFEEAGCRHLHV---------VDLNGAFAGRSTNIPAIEAIVAATNLPVQLGGGIRDMAAIDRWLEAGVSRV 304
Cdd:cd02803 228 EEAIEIAKALEEAGVDALHVsggsyesppPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADL 307
|
90
....*....|....*....
gi 2035452869 305 I-LGSVAVKDPDLVRQAAR 322
Cdd:cd02803 308 VaLGRALLADPDLPNKARE 326
|
|
| Eis |
COG4552 |
Predicted acetyltransferase [General function prediction only]; |
13-147 |
1.48e-03 |
|
Predicted acetyltransferase [General function prediction only];
Pssm-ID: 443616 [Multi-domain] Cd Length: 393 Bit Score: 40.65 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 13 SPDDLENLIEattagiLDGGGFGWvqPPGNQALARYFEglLLVPERSLYVVRDEGVICGA----------GQVVRppasy 82
Cdd:COG4552 7 TEDDLDAFAR------LLAYAFGP--EPDDEELEAYRP--LLEPGRVLGVFDDGELVGTLalypftlnvgGARVP----- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035452869 83 eahaaTANITGFFVAPYARGRGLGRALVKAMLQGARSLGCKVVNcdvreTHATAIGLFRSLGFEH 147
Cdd:COG4552 72 -----MAGITGVAVAPEHRRRGVARALLREALAELRERGQPLSA-----LYPFEPGFYRRFGYEL 126
|
|
| FR47 |
pfam08445 |
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ... |
63-146 |
1.75e-03 |
|
FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.
Pssm-ID: 117022 [Multi-domain] Cd Length: 86 Bit Score: 37.31 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035452869 63 VRDEGVICGAGQVVRPPASYeahaatanITGFFVAPYARGRGLGRALVKAMLQGARSLGcKVVNCDVRETHATAIGLFRS 142
Cdd:pfam08445 4 IYRGDTGELAAWCLRLPGGE--------LGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEK 74
|
....
gi 2035452869 143 LGFE 146
Cdd:pfam08445 75 LGFR 78
|
|
| PRK07922 |
PRK07922 |
amino-acid N-acetyltransferase; |
96-146 |
2.90e-03 |
|
amino-acid N-acetyltransferase;
Pssm-ID: 236132 [Multi-domain] Cd Length: 169 Bit Score: 38.36 E-value: 2.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2035452869 96 VAPYARGRGLGRALVKAMLQGARSLGCKVVNCDVREThataiGLFRSLGFE 146
Cdd:PRK07922 78 VDPAARGRGVGHAIVERLLDVARELGLSRVFVLTFEV-----EFFARHGFV 123
|
|
| |
