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Conserved domains on  [gi|42568351|ref|NP_568663|]
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16S rRNA processing protein RimM family [Arabidopsis thaliana]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11478123)

glycosyltransferase family 2 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rimM PRK00122
16S rRNA-processing protein RimM; Provisional
 79-264 5.02e-55

16S rRNA-processing protein RimM; Provisional


:

Pssm-ID: 234650 [Multi-domain]  Cd Length: 172  Bit Score: 184.96  E-value: 5.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   79 DLVEVGFLSGVHGLQGEICIKPNTDFPDLRFsKPGRRWLKQQLLGQdkidEVELVEGRPHPaqKSWILKFRGLDDVDQVR 158
Cdd:PRK00122   6 DLLVVGKIVSAHGIKGEVKVKSFTDFPERIF-DYGPWLLGKGGEWQ----EVEIESGRFHK--GFLIVKFEGVDDRNAAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLHVLLDSSMEvcngnaktnqlVWIP 238
Cdd:PRK00122  79 ALKGCELFVPRSQLPELEEDEYYWHDLIGLEVVD-EDGEELGKVTDILETGANDVLVVLKDKKEE-----------RLIP 146

                        170       180
                 ....*....|....*....|....*.
gi 42568351  239 FVDAIVPDVDLERKEMYITPPKGLLE 264
Cdd:PRK00122 147 FVEEVVKEVDLEAKRITVDWPEGLLD 172
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 437-574 4.62e-18

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd04193:

Pssm-ID: 472172  Cd Length: 323  Bit Score: 85.74  E-value: 4.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 437 KEEDRACVPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcsspeePKKHKILMKSPWEILESPVGSGGV 516
Cdd:cd04193  66 ASGKKVPIPWYIMTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCV------DFDGKILLEEKGKIAMAPNGNGGL 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568351 517 LSILASHGTTDSLSTLGINYLQVHSIET---KPqpsqhyINPMLVGFVSARGAEIGIQVTE 574
Cdd:cd04193 140 YKALQTAGILEDMKKRGIKYIHVYSVDNilvKV------ADPVFIGFCISKGADVGAKVVR 194
 
Name Accession Description Interval E-value
rimM PRK00122
16S rRNA-processing protein RimM; Provisional
 79-264 5.02e-55

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 234650 [Multi-domain]  Cd Length: 172  Bit Score: 184.96  E-value: 5.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   79 DLVEVGFLSGVHGLQGEICIKPNTDFPDLRFsKPGRRWLKQQLLGQdkidEVELVEGRPHPaqKSWILKFRGLDDVDQVR 158
Cdd:PRK00122   6 DLLVVGKIVSAHGIKGEVKVKSFTDFPERIF-DYGPWLLGKGGEWQ----EVEIESGRFHK--GFLIVKFEGVDDRNAAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLHVLLDSSMEvcngnaktnqlVWIP 238
Cdd:PRK00122  79 ALKGCELFVPRSQLPELEEDEYYWHDLIGLEVVD-EDGEELGKVTDILETGANDVLVVLKDKKEE-----------RLIP 146

                        170       180
                 ....*....|....*....|....*.
gi 42568351  239 FVDAIVPDVDLERKEMYITPPKGLLE 264
Cdd:PRK00122 147 FVEEVVKEVDLEAKRITVDWPEGLLD 172
RimM COG0806
Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing [Translation, ...
 79-265 6.61e-52

Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440569 [Multi-domain]  Cd Length: 173  Bit Score: 176.84  E-value: 6.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  79 DLVEVGFLSGVHGLQGEICIKPNTDFPDlRFSKPGRRWLKQqllGQDKIDEVELVEGRPHpaQKSWILKFRGLDDVDQVR 158
Cdd:COG0806   5 DLVVVGRIVKAHGVKGEVKVKSFTDDPE-RFFDYGPVFLED---PDGELRPLTVESVRPH--KGGLLVKFEGVDDREAAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLhvlldssmEVCNGNAKTnqlVWIP 238
Cdd:COG0806  79 ALRGAELYVPRDDLPELEEDEFYWHDLIGLEVVD-EDGEELGKVTDVLETGANDVL--------VVKGPGGKE---VLIP 146

                       170       180
                ....*....|....*....|....*..
gi 42568351 239 FVDAIVPDVDLERKEMYITPPKGLLEV 265
Cdd:COG0806 147 FVDEFVPEVDLEAGRIVVDPPEGLLDL 173
16S_RimM TIGR02273
16S rRNA processing protein RimM; This family consists of the bacterial protein RimM (YfjA, ...
 80-261 1.08e-38

16S rRNA processing protein RimM; This family consists of the bacterial protein RimM (YfjA, 21K), a 30S ribosomal subunit-binding protein implicated in 16S ribsomal RNA processing. It has been partially characterized in Escherichia coli, is found with other translation-associated genes such as trmD. It is broadly distributed among bacteria, including some minimal genomes such the aphid endosymbiont Buchnera aphidicola. The protein contains a PRC-barrel domain that it shares with other protein families (pfam05239) and a unique domain (pfam01782). This model describes the full-length protein. A member from Arabidopsis (plant) has additional N-terminal sequence likely to represent a chloroplast transit peptide. [Transcription, RNA processing]


Pssm-ID: 274061 [Multi-domain]  Cd Length: 165  Bit Score: 140.42  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351    80 LVEVGFLSGVHGLQGEICIKPNTDFPDLRFSKPGRRWLKqqllgqDKIDEVELVEGRPHPAQKSWILKFRGLDDVDQVRQ 159
Cdd:TIGR02273   1 LLVVGKIGGPHGIKGEVKVKSFTDFPESLFDYGPWLILK------GSKQWQTVKVARVRKQNNKLIVKFEGIDDREAAEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   160 LVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLKEtGQLVGTVANIFDNGGNDLLHVlldssmEVCNGNAKtnqlVWIPF 239
Cdd:TIGR02273  75 LKGLELFVPREALPELEEDEYYWTDLIGLEVVTEE-GEELGKVVEILETGANDVLVV------RSKKGKKE----VLIPF 143

                         170       180
                  ....*....|....*....|..
gi 42568351   240 VDAIVPDVDLERKEMYITPPKG 261
Cdd:TIGR02273 144 VEEIVKEIDLEKKIITVDWPEG 165
RimM pfam01782
RimM N-terminal domain; The RimM protein is essential for efficient processing of 16S rRNA. ...
 82-171 5.44e-21

RimM N-terminal domain; The RimM protein is essential for efficient processing of 16S rRNA. The RimM protein was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes. This N-terminal domain is found associated with a PRC-barrel domain.


Pssm-ID: 460327  Cd Length: 84  Bit Score: 87.61  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351    82 EVGFLSGVHGLQGEICIKPNTDFPDLRFSKPGRRWLKQqllgQDKIDEVELVEGRPHpaQKSWILKFRGLDDVDQVRQLV 161
Cdd:pfam01782   1 VVGKIVGTHGLKGEVKVKSFTDFPEDRFDYGPVFLLKK----KGKWQTLTVESVRVH--KKGLILKFEGIDDRDAAEALK 74

                          90
                  ....*....|
gi 42568351   162 GATLLAEDDD 171
Cdd:pfam01782  75 GAELYVPRSD 84
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 437-574 4.62e-18

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


Pssm-ID: 133036  Cd Length: 323  Bit Score: 85.74  E-value: 4.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 437 KEEDRACVPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcsspeePKKHKILMKSPWEILESPVGSGGV 516
Cdd:cd04193  66 ASGKKVPIPWYIMTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCV------DFDGKILLEEKGKIAMAPNGNGGL 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568351 517 LSILASHGTTDSLSTLGINYLQVHSIET---KPqpsqhyINPMLVGFVSARGAEIGIQVTE 574
Cdd:cd04193 140 YKALQTAGILEDMKKRGIKYIHVYSVDNilvKV------ADPVFIGFCISKGADVGAKVVR 194
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
444-574 2.65e-09

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 59.51  E-value: 2.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 444 VPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcSSPEEPkkhkILMKSPWEILESPVGSGGVLSILASH 523
Cdd:COG4284 147 LPLYIMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPAL-DADLGP----VLLPADPELELCPPGHGGIYTALLAS 221

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42568351 524 GTTDSLSTLGINYLQVHSIETkpqPSQHYINPMLVGFVSARGAEIGIQVTE 574
Cdd:COG4284 222 GLLDKLLERGIRYLFVSNVDN---PLGAVPDPAFAGWHAASGAPFTAKVVR 269
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 444-543 1.07e-08

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 57.96  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  444 VPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVCsspeepKKHKILMKSPWEILESPVGSGGVLSILASH 523
Cdd:PLN02435 178 IHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVS------KDGKFIMETPFKVAKAPDGNGGVYAALKSS 251

                         90       100
                 ....*....|....*....|
gi 42568351  524 GTTDSLSTLGINYLQVHSIE 543
Cdd:PLN02435 252 RLLEDMASRGIKYVDCYGVD 271
 
Name Accession Description Interval E-value
rimM PRK00122
16S rRNA-processing protein RimM; Provisional
 79-264 5.02e-55

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 234650 [Multi-domain]  Cd Length: 172  Bit Score: 184.96  E-value: 5.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   79 DLVEVGFLSGVHGLQGEICIKPNTDFPDLRFsKPGRRWLKQQLLGQdkidEVELVEGRPHPaqKSWILKFRGLDDVDQVR 158
Cdd:PRK00122   6 DLLVVGKIVSAHGIKGEVKVKSFTDFPERIF-DYGPWLLGKGGEWQ----EVEIESGRFHK--GFLIVKFEGVDDRNAAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLHVLLDSSMEvcngnaktnqlVWIP 238
Cdd:PRK00122  79 ALKGCELFVPRSQLPELEEDEYYWHDLIGLEVVD-EDGEELGKVTDILETGANDVLVVLKDKKEE-----------RLIP 146

                        170       180
                 ....*....|....*....|....*.
gi 42568351  239 FVDAIVPDVDLERKEMYITPPKGLLE 264
Cdd:PRK00122 147 FVEEVVKEVDLEAKRITVDWPEGLLD 172
RimM COG0806
Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing [Translation, ...
 79-265 6.61e-52

Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing [Translation, ribosomal structure and biogenesis]; Ribosomal 30S subunit maturation factor RimM, required for 16S rRNA processing is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440569 [Multi-domain]  Cd Length: 173  Bit Score: 176.84  E-value: 6.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  79 DLVEVGFLSGVHGLQGEICIKPNTDFPDlRFSKPGRRWLKQqllGQDKIDEVELVEGRPHpaQKSWILKFRGLDDVDQVR 158
Cdd:COG0806   5 DLVVVGRIVKAHGVKGEVKVKSFTDDPE-RFFDYGPVFLED---PDGELRPLTVESVRPH--KGGLLVKFEGVDDREAAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLhvlldssmEVCNGNAKTnqlVWIP 238
Cdd:COG0806  79 ALRGAELYVPRDDLPELEEDEFYWHDLIGLEVVD-EDGEELGKVTDVLETGANDVL--------VVKGPGGKE---VLIP 146

                       170       180
                ....*....|....*....|....*..
gi 42568351 239 FVDAIVPDVDLERKEMYITPPKGLLEV 265
Cdd:COG0806 147 FVDEFVPEVDLEAGRIVVDPPEGLLDL 173
16S_RimM TIGR02273
16S rRNA processing protein RimM; This family consists of the bacterial protein RimM (YfjA, ...
 80-261 1.08e-38

16S rRNA processing protein RimM; This family consists of the bacterial protein RimM (YfjA, 21K), a 30S ribosomal subunit-binding protein implicated in 16S ribsomal RNA processing. It has been partially characterized in Escherichia coli, is found with other translation-associated genes such as trmD. It is broadly distributed among bacteria, including some minimal genomes such the aphid endosymbiont Buchnera aphidicola. The protein contains a PRC-barrel domain that it shares with other protein families (pfam05239) and a unique domain (pfam01782). This model describes the full-length protein. A member from Arabidopsis (plant) has additional N-terminal sequence likely to represent a chloroplast transit peptide. [Transcription, RNA processing]


Pssm-ID: 274061 [Multi-domain]  Cd Length: 165  Bit Score: 140.42  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351    80 LVEVGFLSGVHGLQGEICIKPNTDFPDLRFSKPGRRWLKqqllgqDKIDEVELVEGRPHPAQKSWILKFRGLDDVDQVRQ 159
Cdd:TIGR02273   1 LLVVGKIGGPHGIKGEVKVKSFTDFPESLFDYGPWLILK------GSKQWQTVKVARVRKQNNKLIVKFEGIDDREAAEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   160 LVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLKEtGQLVGTVANIFDNGGNDLLHVlldssmEVCNGNAKtnqlVWIPF 239
Cdd:TIGR02273  75 LKGLELFVPREALPELEEDEYYWTDLIGLEVVTEE-GEELGKVVEILETGANDVLVV------RSKKGKKE----VLIPF 143

                         170       180
                  ....*....|....*....|..
gi 42568351   240 VDAIVPDVDLERKEMYITPPKG 261
Cdd:TIGR02273 144 VEEIVKEIDLEKKIITVDWPEG 165
RimM pfam01782
RimM N-terminal domain; The RimM protein is essential for efficient processing of 16S rRNA. ...
 82-171 5.44e-21

RimM N-terminal domain; The RimM protein is essential for efficient processing of 16S rRNA. The RimM protein was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes. This N-terminal domain is found associated with a PRC-barrel domain.


Pssm-ID: 460327  Cd Length: 84  Bit Score: 87.61  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351    82 EVGFLSGVHGLQGEICIKPNTDFPDLRFSKPGRRWLKQqllgQDKIDEVELVEGRPHpaQKSWILKFRGLDDVDQVRQLV 161
Cdd:pfam01782   1 VVGKIVGTHGLKGEVKVKSFTDFPEDRFDYGPVFLLKK----KGKWQTLTVESVRVH--KKGLILKFEGIDDRDAAEALK 74

                          90
                  ....*....|
gi 42568351   162 GATLLAEDDD 171
Cdd:pfam01782  75 GAELYVPRSD 84
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 437-574 4.62e-18

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


Pssm-ID: 133036  Cd Length: 323  Bit Score: 85.74  E-value: 4.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 437 KEEDRACVPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcsspeePKKHKILMKSPWEILESPVGSGGV 516
Cdd:cd04193  66 ASGKKVPIPWYIMTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCV------DFDGKILLEEKGKIAMAPNGNGGL 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568351 517 LSILASHGTTDSLSTLGINYLQVHSIET---KPqpsqhyINPMLVGFVSARGAEIGIQVTE 574
Cdd:cd04193 140 YKALQTAGILEDMKKRGIKYIHVYSVDNilvKV------ADPVFIGFCISKGADVGAKVVR 194
rimM PRK13828
16S rRNA-processing protein RimM; Provisional
 94-264 1.27e-14

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 184351 [Multi-domain]  Cd Length: 161  Bit Score: 71.90  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   94 GEICIKPNTDFP-DLRFSKPgrrwlkqqLLGQDKIDEVELVEGRPhpAQKSWILKFRGLDDVDQVRQLVGATLLAEDDDR 172
Cdd:PRK13828   3 GEVRLKSFTEDPlAIADYGP--------LTTEDGARSFTVALARP--AKDGLVARLKGVATREAAEALRGLELYVPRDRL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  173 PELDEGEFYSRDLVGMRVlLKETGQLVGTVANIFDNGGNDLLHVlldssmevcnGNAKTNQLVWIPFVDAIVPDVDLERK 252
Cdd:PRK13828  73 PELDDDEFYHADLIGLAA-VDTGGALLGRVKAVHNFGAGDILEI----------APPGGGPTLLLPFTRAVVPTVDLAAG 141

                        170
                 ....*....|..
gi 42568351  253 EMYITPPKGLLE 264
Cdd:PRK13828 142 RVVADPPAEIEG 153
rimM PRK14592
16S rRNA-processing protein RimM; Provisional
 79-260 6.18e-14

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 173056 [Multi-domain]  Cd Length: 165  Bit Score: 70.14  E-value: 6.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   79 DLVEVGFLSGVHGLQGEICIKPNTDFPDlRFSKPGrrwlkqQLLGQDKIDEVELVEgrpHPAQKSWILKFRGLDDVDQVR 158
Cdd:PRK14592   1 DLICLGVITSPHGIKGHVKIKTFTEDPE-NISAYG------KLTDGSNTYKISVVS---VIGANLVIAKISGINSRTEAE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  159 QLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLLkETGQLVGTVANIFDNGGNDLLHVLLDSSMEVcngnaktnqlVWIP 238
Cdd:PRK14592  71 LLRNKKLYVERSKLPNLNEDEFYQSDLIGMEVKL-EDNTIYGYIKKIYNFGSCDIIEISLTSTKKS----------TMLP 139

                        170       180
                 ....*....|....*....|..
gi 42568351  239 FVDAIVPDVDLERKEMYITPPK 260
Cdd:PRK14592 140 FTKEIFPHINVKERYIILVPPE 161
rimM PRK13829
16S rRNA-processing protein RimM; Provisional
 78-263 4.36e-13

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 184352 [Multi-domain]  Cd Length: 162  Bit Score: 67.46  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   78 LDLVEVGFLSGVHGLQGEICIKPNTDFPDL-RFSKPGRRWLKqqllgqdkIDEVELVEGrphpaqkSWILKFRGLDDVDQ 156
Cdd:PRK13829   1 MRRTEIGRFGGPYGVQGGLKFRGEPVVLDLpRVYVEGLGWRA--------IERAERVGP-------ELVLHLAGVTSREG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  157 VRQLVGATLLAEDDDRPELDEGEFYSRDLVGMRVllKETGQLVGTVANIFDNGGNDLLhvlldssmeVCNGNAKTNQLVW 236
Cdd:PRK13829  66 AEALVGLRVYADDADLPPLEEGSYYYHELRGLPV--YVDGEPLGEVVDVEDAGAQDLL---------VIRHVGGSLRARA 134

                        170       180
                 ....*....|....*....|....*..
gi 42568351  237 IPFVDAIVPDVDLERKEMYITPPKGLL 263
Cdd:PRK13829 135 TYFVPLQAPYVRVELDGITADAIPGLL 161
rimM PRK14590
16S rRNA-processing protein RimM; Provisional
 124-265 1.18e-10

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 173054 [Multi-domain]  Cd Length: 171  Bit Score: 60.64  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  124 QDKIDEVELVEGRPHPAQksWILKFRGLDDVDQVRQLVGATLLAEDDDRPELD-EGEFYSRDLVGMRVlLKETGQ-LVGT 201
Cdd:PRK14590  42 QFPESEIALLEIRPHGGK--FLVRFEGYDTPEEAVKWRGGSLFLPQELLPKIEtKGEFYSEDLIGLQA-IDETGKpLNWK 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568351  202 VANIFDNGGNDLLhvlldssmEVCNGNAKTnqlVWIPFVDAIVPDVDLERKEMYITPPKGLLEV 265
Cdd:PRK14590 119 LTDVQDNPAHPIL--------VFIKGEGEE---ILIPFLNVFVGDLDLEKQTIVLIQPEQWNEL 171
PRC pfam05239
PRC-barrel domain; The PRC-barrel is an all beta barrel domain found in photosystem reaction ...
 177-263 3.42e-10

PRC-barrel domain; The PRC-barrel is an all beta barrel domain found in photosystem reaction centre subunit H of the purple bacteria and RNA metabolism proteins of the RimM group. PRC-barrels are approximately 80 residues long, and found widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain.


Pssm-ID: 398765  Cd Length: 78  Bit Score: 56.53  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   177 EGEFYSRDLVGMRVLLkETGQLVGTVANI-FDNGGNDLLHVLLDSSMEVCNGNaktnqlVWIPFVDaivPDVDLERKEMY 255
Cdd:pfam05239   1 EDEFYASDLIGLEVYT-EDGEKLGKVKDVvIDEGEGRVRYLVVSVGGFLGGKE------VLIPFDK---LNVKLGKDRII 70


                  ....*...
gi 42568351   256 ITPPKGLL 263
Cdd:pfam05239  71 VDPPKELL 78
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
444-574 2.65e-09

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 59.51  E-value: 2.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 444 VPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcSSPEEPkkhkILMKSPWEILESPVGSGGVLSILASH 523
Cdd:COG4284 147 LPLYIMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPAL-DADLGP----VLLPADPELELCPPGHGGIYTALLAS 221

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42568351 524 GTTDSLSTLGINYLQVHSIETkpqPSQHYINPMLVGFVSARGAEIGIQVTE 574
Cdd:COG4284 222 GLLDKLLERGIRYLFVSNVDN---PLGAVPDPAFAGWHAASGAPFTAKVVR 269
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 444-543 1.07e-08

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 57.96  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  444 VPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVCsspeepKKHKILMKSPWEILESPVGSGGVLSILASH 523
Cdd:PLN02435 178 IHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVS------KDGKFIMETPFKVAKAPDGNGGVYAALKSS 251

                         90       100
                 ....*....|....*....|
gi 42568351  524 GTTDSLSTLGINYLQVHSIE 543
Cdd:PLN02435 252 RLLEDMASRGIKYVDCYGVD 271
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 440-567 1.06e-07

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 54.75  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  440 DRACVPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVCSSpeepkKHKILMKSPWEILESPVGSGGVLSI 519
Cdd:PTZ00339 162 DDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDEN-----TGRFIMSSQGSLCTAPGGNGDVFKA 236

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42568351  520 LASHGTTDSLSTLGINYLQVHSIE---TKPqpsqhyINPMLVGFVSARGAE 567
Cdd:PTZ00339 237 LAKCSELMDIVRKGIKYVQVISIDnilAKV------LDPEFIGLASSFPAH 281
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
 444-537 2.83e-07

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 53.54  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  444 VPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVcsspeEPKKHKILMKS--PWEILESPVGSGGVLSILA 521
Cdd:PLN02830 187 IPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACL-----MDNDARLALDPndPYKIQTKPHGHGDVHALLY 261

                         90
                 ....*....|....*.
gi 42568351  522 SHGTTDSLSTLGINYL 537
Cdd:PLN02830 262 SSGLLDKWLSAGKKWV 277
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
 433-537 3.23e-07

UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose Pyrophosphorylase catalyzes the reversible production of UDP-Glucose/UDP-Galactose and pyrophosphate (PPi) from Glucose-1-phosphate/Galactose-1-phosphate and UTP. Its dual substrate specificity distinguishes it from the single substrate enzyme UDP-glucose pyrophosphorylase. It may play a key role in the galactose metabolism in raffinose oligosaccharide (RFO) metabolizing plants. RFO raffinose is a major photoassimilate and is a galactosylderivative of sucrose (Suc) containing a galactose (Gal) moiety. Upon arriving at the sink tissue, the Gal moieties of the RFOs are initially removed by alpha-galactosidase and then are phosphorylated to Gal-1-P. Gal-1-P is converted to UDP-Gal. The UDP-Gal is further metabolized to UDP-Glc via an epimerase reaction. The UDP-Glc can be directly utilized in cell wall metabolism or in Suc synthesis. However, for the Suc synthesis UDP-Glc must be further metabolized to Glc-1-P. This can be carried out either by the UGPase in the reverse direction or by the dual substrate PPase itself operating in the reverse direction. According to the latter possibility, the three-step pathway of Gal-1-P to Glc-1-P could be carried out by a single PPase, functioning sequentially in reverse directions separated by the epimerase reaction.


Pssm-ID: 133046  Cd Length: 315  Bit Score: 52.46  E-value: 3.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 433 QRFIKEEDRACVPLVIVSPEHTIEALQKLFQDNDHFGFESEKIWILKEETLPVVCSS-----PEEPKKHKILMKspweil 507
Cdd:cd06424  45 QEASKKGEKMEIPFVIMTSDDTHSKTLKLLEENNYFGLEKDQVHILKQEKVFCLIDNdahlaLDPDNTYSILTK------ 118

                        90       100       110
                ....*....|....*....|....*....|
gi 42568351 508 esPVGSGGVLSILASHGTTDSLSTLGINYL 537
Cdd:cd06424 119 --PHGHGDVHTLLYNSGLLKKWIEAGYKWL 146
rimM PRK14594
16S rRNA-processing protein RimM; Provisional
 142-252 3.29e-05

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 173058 [Multi-domain]  Cd Length: 166  Bit Score: 44.77  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  142 KSWILKFRGLDDVDQVRQLVGATLLAEDDDRPELDEGEFYSRDLVGMRVLlkETGQLVGTVANIFDNGGNDLLHVLLDSs 221
Cdd:PRK14594  59 NSLLLKFEEFNAPEPIKPLIGFELWVDDELASKLEEGEYYFGKLIGYAIV--NDGKELGEVVSFFECLNSVLLEVKVGI- 135

                         90       100       110
                 ....*....|....*....|....*....|.
gi 42568351  222 mevcngnaktnQLVWIPFVDAIVPDVDLERK 252
Cdd:PRK14594 136 -----------KLFFVPFLSIYLGDINRELK 155
rimM PRK14591
16S rRNA-processing protein RimM; Provisional
 79-256 1.97e-04

16S rRNA-processing protein RimM; Provisional


Pssm-ID: 173055 [Multi-domain]  Cd Length: 169  Bit Score: 42.33  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351   79 DLVEVGFLSGVHGLQGEICIKPNTD-------FPDLRFSKPGRR-WlkQQLLGQDKIDEvelvegrphpAQKSWIlKFRG 150
Cdd:PRK14591   4 DFVEIAKIGATYKLNGELNLYPLANsietllsYGDWYIQLPATNvW--QQLKGESVLKR----------ADKVYI-KLAN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351  151 LDDVDQVRQLVGATLLAEDDDRPELDEGEFYSRDLVGMRVlLKETGQLVGTVANIFDNGGNDLLhvlldssmeVCNgnaK 230
Cdd:PRK14591  71 INNADTAKKYVNALIGVPKRALPQLAEDEVYFKDLIGCSV-KNINNDSFGVVVDIIETGANEVL---------VCK---E 137

                        170       180
                 ....*....|....*....|....*.
gi 42568351  231 TNQLVWIPFVDAIVPDVDLERKEMYI 256
Cdd:PRK14591 138 DNSEYLIPYVKQYIVSEDLNSKKIVV 163
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
 444-613 1.31e-03

Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family includes UDP-Glucose Pyrophosphorylase (UDPase) and UDPGlcNAc pyrophosphorylase enzymes. The two enzymes share significant sequence and structure similarity. UDP-Glucose Pyrophosphorylase catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans . UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1P from PPi and UDPGlcNAc, which is a key precursor of N- and O-linked glycosylations and is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker anchoring a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis.


Pssm-ID: 133023  Cd Length: 266  Bit Score: 41.00  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 444 VPLVIVSPEHTIEALQKLFQDNDHfgfESEKIWILKEETLPVV----CSSPEEpkKHKILMKspweilesPVGSGGVLSI 519
Cdd:cd04180  54 IPEQLMNSKYTHEKTQCYFEKINQ---KNSYVITFMQGKLPLKndddARDPHN--KTKCHLF--------PCGHGDVVLA 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568351 520 LASHGTTDSLSTLGINYL---QVHSIETKPqpsqhyINPMLVGFVSARGAEIGIQVTEeselknlemtfsmkflKRLKGK 596
Cdd:cd04180 121 LIHSGHLNKLLEKGYRYIhfiGVDNLLVKV------ADPLFIGIAIQNRKAINQKVVP----------------KTRNEE 178

                       170
                ....*....|....*..
gi 42568351 597 IEFEAVMKMNSHVQNVE 613
Cdd:cd04180 179 SGGYRIANINGRVQLLE 195
 
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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