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Conserved domains on  [gi|1231969915|gb|OYT32898|]
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galactose-1-phosphate uridylyltransferase [Candidatus Woesearchaeota archaeon ex4484_78]

Protein Classification

HIT family protein( domain architecture ID 694)

HIT (Histidine triad) family protein, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), is part of a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-309 1.27e-104

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 309.07  E-value: 1.27e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   1 MGELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTD---YFAPGNEHLTPPEKgrieKNRKWQIRWFENKFPALTPE 77
Cdd:COG1085     5 MPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDPPEYDedcPLCPGNERATPPEI----PPPGWDVRVFPNKFPALSPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  78 GnPNIQTHNKFFTFSSNYGYHEIIVETP-TKKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSII 156
Cdd:COG1085    81 A-PDAREGDGLYDAMPGRGRHEVICFSPdHDLSLAELSVERIRDVLEAWRDRTAELGADPRIRYVQIFENRGAEAGASLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 157 HAHSQVTALNIIPPNIKEKLIAIKKFVN----CPYCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKHITR 231
Cdd:COG1085   160 HPHGQIIAYPFVPPRIARELRGARAYYEehgrCLLCDILAQElAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 232 LE---DANHKELAKILKRVLEKIKEL--KVSYNIIIHYSPKG----EDLHLCIEILPR------IATWAGFEFSSGIVIN 296
Cdd:COG1085   240 FEeltDEERDDLARILKRVLRRLDNLlgDFPYNMGLHQAPVDgeerDHYHWHLEIYPRlrsatvLKFLAGFELGAGAFIN 319
                         330
                  ....*....|...
gi 1231969915 297 SVSPERAAAYYRG 309
Cdd:COG1085   320 DVTPEQAAERLRE 332
 
Name Accession Description Interval E-value
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-309 1.27e-104

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 309.07  E-value: 1.27e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   1 MGELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTD---YFAPGNEHLTPPEKgrieKNRKWQIRWFENKFPALTPE 77
Cdd:COG1085     5 MPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDPPEYDedcPLCPGNERATPPEI----PPPGWDVRVFPNKFPALSPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  78 GnPNIQTHNKFFTFSSNYGYHEIIVETP-TKKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSII 156
Cdd:COG1085    81 A-PDAREGDGLYDAMPGRGRHEVICFSPdHDLSLAELSVERIRDVLEAWRDRTAELGADPRIRYVQIFENRGAEAGASLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 157 HAHSQVTALNIIPPNIKEKLIAIKKFVN----CPYCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKHITR 231
Cdd:COG1085   160 HPHGQIIAYPFVPPRIARELRGARAYYEehgrCLLCDILAQElAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 232 LE---DANHKELAKILKRVLEKIKEL--KVSYNIIIHYSPKG----EDLHLCIEILPR------IATWAGFEFSSGIVIN 296
Cdd:COG1085   240 FEeltDEERDDLARILKRVLRRLDNLlgDFPYNMGLHQAPVDgeerDHYHWHLEIYPRlrsatvLKFLAGFELGAGAFIN 319
                         330
                  ....*....|...
gi 1231969915 297 SVSPERAAAYYRG 309
Cdd:COG1085   320 DVTPEQAAERLRE 332
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
3-308 1.05e-83

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 255.31  E-value: 1.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   3 ELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTD---YFAPGNEHLTPPEKgriekNRKWQIRWFENKFPALTPEGN 79
Cdd:cd00608     1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAPKKLPEYDpdcPLCPGNERADTGEQ-----NPDYDVRVFENDFPALKPDAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  80 PNIQTHNKFFTFSSNYGYHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSIIHA 158
Cdd:cd00608    76 APEDSDDGLFRTAPARGRCEVICFSPDhNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQIFENKGAEMGASLPHP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 159 HSQVTALNIIPPNIKEKLIAIKKFV----NCPYCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKH---IT 230
Cdd:cd00608   156 HGQIWALPFLPPEVARELRNQKAYYekhgRCLLCDYLKLElESKERIVVENEHFVAVVPFWARWPFEVHILPKRHvsrFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 231 RLEDANHKELAKILKRVLEKIKEL---KVSYNIIIHYSPKG------EDLHLCIEILPRIATW-----AGFEFSSGIVIN 296
Cdd:cd00608   236 DLTDEEREDLAEILKRLLARYDNLfncSFPYSMGWHQAPTGgkelenWYYHWHFEIPPRRSATvlkfmAGFELGAGEFIN 315
                         330
                  ....*....|..
gi 1231969915 297 SVSPERAAAYYR 308
Cdd:cd00608   316 DVTPEQAAARLR 327
PLN02643 PLN02643
ADP-glucose phosphorylase
1-312 2.26e-71

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 224.25  E-value: 2.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   1 MGELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTDY----FAPGNEHLTPPEKGRI---EKNRKWQIRWFENKFPA 73
Cdd:PLN02643    1 MAELRKDPVTNRWVIFSPARGKRPTDFKSKSPQNPNGNHSsgcpFCIGHEHECAPEIFRVpddASAPDWKVRVIENLYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  74 LTPEGNPNiQTHNKFFTFSS----NYGYHEIIVETPTKK-QLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEG 148
Cdd:PLN02643   81 LSRDLEPP-CTEGQGEDYGGrrlpGFGFHDVVIETPVHSvQLSDLPARHIGEVLKAYKKRINQLQSDSRFKYVQVFKNHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 149 PKGGTSIIHAHSQVTALNIIPPNIKEKLIAIKKFVN----CPYCEIVKEEAKGTrkcfENKEFLAFCPYASRFNFETWIM 224
Cdd:PLN02643  160 ASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEktgkCSLCEVVKKDLLID----ESSHFVSIAPFAATFPFEIWII 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 225 PKKHITRLEDANHKE---LAKILKRVLEKI-KELK-VSYNIIIHYSPKGED------LHLCIEILPRIATWAGFEFSSGI 293
Cdd:PLN02643  236 PRDHSSNFHEIDDDKavdLGGLLKLMLQKIsKQLNdPPYNYMIQTSPLGVEesnlpyTHWFLQIVPQLSGVGGFELGTGC 315
                         330
                  ....*....|....*....
gi 1231969915 294 VINSVSPERAAAYYRgELN 312
Cdd:PLN02643  316 YINPVFPEDAAKVLR-EVN 333
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
5-271 7.06e-30

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 116.21  E-value: 7.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   5 RKDYILDRWVIIAETRKKRPKEFKEQPAKTEKK-----TDYFAPGNEHLTPpekgriEKNRKWQIRW-FENKFPALTPEG 78
Cdd:TIGR00209  13 RYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLpaydpDCYLCPGNKRVTG------DLNPDYTGTYvFTNDFAALMSDT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  79 NPNIQTHNKFFTFSSNYGYHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKKphIKYAAVFKNEGPKGGTSIIH 157
Cdd:TIGR00209  87 PDAPESHDPLMRCQSARGTSRVICFSPDhSKTLPELSVAALTEIVKTWQEQTAELGKT--YPWVQIFENKGAAMGCSNPH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 158 AHSQVTALNIIPPNIKEKLIAIKKFV---NCP-YCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKH---I 229
Cdd:TIGR00209 165 PHGQIWANSFLPNEVEREDRLQKEYFaehKSPmLVDYVKRElADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHvlrI 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1231969915 230 TRLEDANHKELAKILKRVLEKIKEL---KVSYNIIIHYSP-KGEDL 271
Cdd:TIGR00209 245 TDLTDAQRSDLALILKKLTSKYDNLfetSFPYSMGWHGAPfNGEEN 290
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
10-169 4.44e-16

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 74.63  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  10 LDRWVIIAETRKKRP----KEFKEQPAKTEKK-TDYFAPGNEhltppekgRI--EKNRKWQ-IRWFENKFPALTPEgNPN 81
Cdd:pfam01087  19 TGEWVLVSPHRLKRPwagqQEKISKDTLPEYDpMCYLCPGPS--------RAngDFNPDYKsPFVFTNDFYALSKD-NPY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  82 IQT----HNKFFTFSSNYGYHEIIVETP-TKKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSII 156
Cdd:pfam01087  90 IKTdaiaKNILFKAETVYGDCEVTCFLSkPELTLPLMSPKDPKAIAAAWQEKYAELGASSYPKCVLCFENEGYAMGCSNP 169
                         170
                  ....*....|...
gi 1231969915 157 HAHSQVTALNIIP 169
Cdd:pfam01087 170 HPHGQIWASSHLP 182
 
Name Accession Description Interval E-value
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-309 1.27e-104

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 309.07  E-value: 1.27e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   1 MGELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTD---YFAPGNEHLTPPEKgrieKNRKWQIRWFENKFPALTPE 77
Cdd:COG1085     5 MPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDPPEYDedcPLCPGNERATPPEI----PPPGWDVRVFPNKFPALSPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  78 GnPNIQTHNKFFTFSSNYGYHEIIVETP-TKKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSII 156
Cdd:COG1085    81 A-PDAREGDGLYDAMPGRGRHEVICFSPdHDLSLAELSVERIRDVLEAWRDRTAELGADPRIRYVQIFENRGAEAGASLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 157 HAHSQVTALNIIPPNIKEKLIAIKKFVN----CPYCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKHITR 231
Cdd:COG1085   160 HPHGQIIAYPFVPPRIARELRGARAYYEehgrCLLCDILAQElAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 232 LE---DANHKELAKILKRVLEKIKEL--KVSYNIIIHYSPKG----EDLHLCIEILPR------IATWAGFEFSSGIVIN 296
Cdd:COG1085   240 FEeltDEERDDLARILKRVLRRLDNLlgDFPYNMGLHQAPVDgeerDHYHWHLEIYPRlrsatvLKFLAGFELGAGAFIN 319
                         330
                  ....*....|...
gi 1231969915 297 SVSPERAAAYYRG 309
Cdd:COG1085   320 DVTPEQAAERLRE 332
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
3-308 1.05e-83

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 255.31  E-value: 1.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   3 ELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTD---YFAPGNEHLTPPEKgriekNRKWQIRWFENKFPALTPEGN 79
Cdd:cd00608     1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAPKKLPEYDpdcPLCPGNERADTGEQ-----NPDYDVRVFENDFPALKPDAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  80 PNIQTHNKFFTFSSNYGYHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSIIHA 158
Cdd:cd00608    76 APEDSDDGLFRTAPARGRCEVICFSPDhNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQIFENKGAEMGASLPHP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 159 HSQVTALNIIPPNIKEKLIAIKKFV----NCPYCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKH---IT 230
Cdd:cd00608   156 HGQIWALPFLPPEVARELRNQKAYYekhgRCLLCDYLKLElESKERIVVENEHFVAVVPFWARWPFEVHILPKRHvsrFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 231 RLEDANHKELAKILKRVLEKIKEL---KVSYNIIIHYSPKG------EDLHLCIEILPRIATW-----AGFEFSSGIVIN 296
Cdd:cd00608   236 DLTDEEREDLAEILKRLLARYDNLfncSFPYSMGWHQAPTGgkelenWYYHWHFEIPPRRSATvlkfmAGFELGAGEFIN 315
                         330
                  ....*....|..
gi 1231969915 297 SVSPERAAAYYR 308
Cdd:cd00608   316 DVTPEQAAARLR 327
PLN02643 PLN02643
ADP-glucose phosphorylase
1-312 2.26e-71

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 224.25  E-value: 2.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   1 MGELRKDYILDRWVIIAETRKKRPKEFKEQPAKTEKKTDY----FAPGNEHLTPPEKGRI---EKNRKWQIRWFENKFPA 73
Cdd:PLN02643    1 MAELRKDPVTNRWVIFSPARGKRPTDFKSKSPQNPNGNHSsgcpFCIGHEHECAPEIFRVpddASAPDWKVRVIENLYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  74 LTPEGNPNiQTHNKFFTFSS----NYGYHEIIVETPTKK-QLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEG 148
Cdd:PLN02643   81 LSRDLEPP-CTEGQGEDYGGrrlpGFGFHDVVIETPVHSvQLSDLPARHIGEVLKAYKKRINQLQSDSRFKYVQVFKNHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 149 PKGGTSIIHAHSQVTALNIIPPNIKEKLIAIKKFVN----CPYCEIVKEEAKGTrkcfENKEFLAFCPYASRFNFETWIM 224
Cdd:PLN02643  160 ASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEktgkCSLCEVVKKDLLID----ESSHFVSIAPFAATFPFEIWII 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 225 PKKHITRLEDANHKE---LAKILKRVLEKI-KELK-VSYNIIIHYSPKGED------LHLCIEILPRIATWAGFEFSSGI 293
Cdd:PLN02643  236 PRDHSSNFHEIDDDKavdLGGLLKLMLQKIsKQLNdPPYNYMIQTSPLGVEesnlpyTHWFLQIVPQLSGVGGFELGTGC 315
                         330
                  ....*....|....*....
gi 1231969915 294 VINSVSPERAAAYYRgELN 312
Cdd:PLN02643  316 YINPVFPEDAAKVLR-EVN 333
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
5-271 7.06e-30

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 116.21  E-value: 7.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   5 RKDYILDRWVIIAETRKKRPKEFKEQPAKTEKK-----TDYFAPGNEHLTPpekgriEKNRKWQIRW-FENKFPALTPEG 78
Cdd:TIGR00209  13 RYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLpaydpDCYLCPGNKRVTG------DLNPDYTGTYvFTNDFAALMSDT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  79 NPNIQTHNKFFTFSSNYGYHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKKphIKYAAVFKNEGPKGGTSIIH 157
Cdd:TIGR00209  87 PDAPESHDPLMRCQSARGTSRVICFSPDhSKTLPELSVAALTEIVKTWQEQTAELGKT--YPWVQIFENKGAAMGCSNPH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 158 AHSQVTALNIIPPNIKEKLIAIKKFV---NCP-YCEIVKEE-AKGTRKCFENKEFLAFCPYASRFNFETWIMPKKH---I 229
Cdd:TIGR00209 165 PHGQIWANSFLPNEVEREDRLQKEYFaehKSPmLVDYVKRElADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHvlrI 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1231969915 230 TRLEDANHKELAKILKRVLEKIKEL---KVSYNIIIHYSP-KGEDL 271
Cdd:TIGR00209 245 TDLTDAQRSDLALILKKLTSKYDNLfetSFPYSMGWHGAPfNGEEN 290
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
5-272 2.79e-24

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 100.75  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915   5 RKDYILDRWVIIAETRKKRPKEFK-EQPAKTEK----KTDYFAPGNEhltppekgRI--EKNRKWQIRW-FENKFPALTP 76
Cdd:PRK11720   13 RYNPLTGQWVLVSPHRAKRPWQGQqETPAKETLpaydPDCFLCPGNT--------RVtgDVNPDYTGTYvFTNDFAALMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  77 EGNPNIQTHNKFFTFSSNYGYHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKkpHIKYAAVFKNEGPKGGTSI 155
Cdd:PRK11720   85 DTPDAPESDDPLFRCQSARGTSRVICFSPDhSKTLPELSVAALREVVDTWQEQTAELGK--TYPWVQVFENKGAAMGCSN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 156 IHAHSQVTALNIIPPNIKEKLIAIKKFVN-------CPYCEivKEEAKGTRKCFENKEFLAFCPYASRFNFETWIMPKKH 228
Cdd:PRK11720  163 PHPHGQIWANSFLPNEAEREDRLQRAYFAehgspllVDYVQ--RELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAH 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1231969915 229 ITRLED---ANHKELAKILKRVLEKIKEL-KVS--YNIIIHYSP-KGED-----LH 272
Cdd:PRK11720  241 VLRLTDltdAQRDDLALALKKLTSRYDNLfQCSfpYSMGWHGAPfNGEEndhwqLH 296
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
10-169 4.44e-16

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 74.63  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  10 LDRWVIIAETRKKRP----KEFKEQPAKTEKK-TDYFAPGNEhltppekgRI--EKNRKWQ-IRWFENKFPALTPEgNPN 81
Cdd:pfam01087  19 TGEWVLVSPHRLKRPwagqQEKISKDTLPEYDpMCYLCPGPS--------RAngDFNPDYKsPFVFTNDFYALSKD-NPY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  82 IQT----HNKFFTFSSNYGYHEIIVETP-TKKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSII 156
Cdd:pfam01087  90 IKTdaiaKNILFKAETVYGDCEVTCFLSkPELTLPLMSPKDPKAIAAAWQEKYAELGASSYPKCVLCFENEGYAMGCSNP 169
                         170
                  ....*....|...
gi 1231969915 157 HAHSQVTALNIIP 169
Cdd:pfam01087 170 HPHGQIWASSHLP 182
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
184-308 7.37e-08

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 50.33  E-value: 7.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 184 NCPYCEIVKEEAKGtRKCFENKEFLAFC---PYAsrfnfETWIM--PKKHITRLEDANHKELAKI---LKRVLEKIKE-L 254
Cdd:COG0537     2 DCIFCKIIAGEIPA-LIVYEDEHVLAFLdinPYA-----PGHTLviPKRHVASLFDLTPEELAELmrlAQKVAKALRKaL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1231969915 255 KVS-YNIIIHYSPKG--EDLHLCIEILPRiatWAGFEFSSGIVINSVSPERAAAYYR 308
Cdd:COG0537    76 GPDgFNLGINNGEAAgqTVPHLHVHVIPR---YEGDDNFMPVIGTKVDPEELEETAR 129
DUF4931 pfam16285
Domain of unknown function (DUF4931); This family consists of uncharacterized proteins around ...
86-166 8.58e-05

Domain of unknown function (DUF4931); This family consists of uncharacterized proteins around 270 residues in length and is mainly found in various Bacillus cereus species. Some members of this family are annotated as Galactose-1-phosphate uridylyltransferases, but the specific function of this family is unknown.


Pssm-ID: 406647  Cd Length: 245  Bit Score: 43.20  E-value: 8.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915  86 NKFFTFSSNYgyHEIIVETPT-KKQLPELSAEEIEELLKVYANRIIELEKKPHIKYAAVFKNEGPKGGTSIIHAHSQVTA 164
Cdd:pfam16285  43 NKFPVLEDTF--QTVLIETDEcEGDISTYSEEHMRSLLRFGVKHWLEMQKSGEFKSVLFFKNHGPLSGGSIRHPHMQIVG 120

                  ..
gi 1231969915 165 LN 166
Cdd:pfam16285 121 LK 122
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
193-270 4.20e-03

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 37.46  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231969915 193 EEAKGTRKCFENKEFLAFCPYASRFNFETWIMPKKHITRLEDANHKE---LAKILKRVLEK---IKELKVSYNIIIHYSP 266
Cdd:pfam02744  24 ELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEredLAAILKPLTRRydnLFETSFPYSMGIHQAP 103

                  ....
gi 1231969915 267 KGED 270
Cdd:pfam02744 104 LNAE 107
 
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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