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Conserved domains on  [gi|385251404|ref|NP_001245261|]
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galactose-1-phosphate uridylyltransferase isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11720 super family cl29677
UDP-glucose--hexose-1-phosphate uridylyltransferase;
12-257 5.49e-169

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


The actual alignment was detected with superfamily member PRK11720:

Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 470.93  E-value: 5.49e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  12 SEPTESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQ 91
Cdd:PRK11720 101 SARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  92 REERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMK 171
Cdd:PRK11720 181 REDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 172 KLLTKYDNLFETSFPYSMGWHGAPTGSEAGAnwnHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA 251
Cdd:PRK11720 261 KLTSRYDNLFQCSFPYSMGWHGAPFNGEEND---HWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRA 337


                 ....*.
gi 385251404 252 LPEVHY 257
Cdd:PRK11720 338 VSDIHY 343
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
12-257 5.49e-169

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 470.93  E-value: 5.49e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  12 SEPTESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQ 91
Cdd:PRK11720 101 SARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  92 REERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMK 171
Cdd:PRK11720 181 REDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 172 KLLTKYDNLFETSFPYSMGWHGAPTGSEAGAnwnHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA 251
Cdd:PRK11720 261 KLTSRYDNLFQCSFPYSMGWHGAPFNGEEND---HWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRA 337


                 ....*.
gi 385251404 252 LPEVHY 257
Cdd:PRK11720 338 VSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 17-252 1.20e-129

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: 370.48  E-value: 1.20e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  17 SKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREE 94
Cdd:cd00608   94 CEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHGQIWALPFLPPEVAREL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  95 RSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLL 174
Cdd:cd00608  174 RNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLL 253

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385251404 175 TKYDNLFETSFPYSMGWHGAPTGseaGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQRDLTPEQAAERLRAL 252
Cdd:cd00608  254 ARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDVTPEQAAARLREV 329
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 16-257 1.75e-124

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: 358.12  E-value: 1.75e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   16 ESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREER 95
Cdd:TIGR00209 105 TSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVEREDR 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   96 SQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLT 175
Cdd:TIGR00209 185 LQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLRITDLTDAQRSDLALILKKLTS 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  176 KYDNLFETSFPYSMGWHGAPTGseaGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEV 255
Cdd:TIGR00209 265 KYDNLFETSFPYSMGWHGAPFN---GEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGETQRDLTAEQAAERLRALSDI 341


                  ..
gi 385251404  256 HY 257
Cdd:TIGR00209 342 HY 343
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
17-255 2.21e-113

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 329.49  E-value: 2.21e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  17 SKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREE 94
Cdd:COG1085  100 HEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLPHPHGQIIAYPFVPPRIAREL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  95 RSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLL 174
Cdd:COG1085  180 RGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 175 TKYDNLFETsFPYSMGWHGAPTGSEAGanwNHWQLHAHYYPPlLRSATVRKFMVGYEMLAQA-QRDLTPEQAAERLRALP 253
Cdd:COG1085  260 RRLDNLLGD-FPYNMGLHQAPVDGEER---DHYHWHLEIYPR-LRSATVLKFLAGFELGAGAfINDVTPEQAAERLREVS 334


                 ..
gi 385251404 254 EV 255
Cdd:COG1085  335 EV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
 93-261 1.01e-91

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: 268.19  E-value: 1.01e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   93 EERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKK 172
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  173 LLTKYDNLFETSFPYSMGWHGAPTGSEagaNWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 252
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLNAE---ELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157


                  ....*....
gi 385251404  253 PEVHYHLGQ 261
Cdd:pfam02744 158 SEVHYRWAL 166
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
12-257 5.49e-169

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 470.93  E-value: 5.49e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  12 SEPTESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQ 91
Cdd:PRK11720 101 SARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  92 REERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMK 171
Cdd:PRK11720 181 REDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 172 KLLTKYDNLFETSFPYSMGWHGAPTGSEAGAnwnHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA 251
Cdd:PRK11720 261 KLTSRYDNLFQCSFPYSMGWHGAPFNGEEND---HWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRA 337


                 ....*.
gi 385251404 252 LPEVHY 257
Cdd:PRK11720 338 VSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 17-252 1.20e-129

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: 370.48  E-value: 1.20e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  17 SKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREE 94
Cdd:cd00608   94 CEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHGQIWALPFLPPEVAREL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  95 RSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLL 174
Cdd:cd00608  174 RNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLL 253

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385251404 175 TKYDNLFETSFPYSMGWHGAPTGseaGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQRDLTPEQAAERLRAL 252
Cdd:cd00608  254 ARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDVTPEQAAARLREV 329
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 16-257 1.75e-124

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: 358.12  E-value: 1.75e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   16 ESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREER 95
Cdd:TIGR00209 105 TSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVEREDR 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   96 SQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLT 175
Cdd:TIGR00209 185 LQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLRITDLTDAQRSDLALILKKLTS 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  176 KYDNLFETSFPYSMGWHGAPTGseaGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEV 255
Cdd:TIGR00209 265 KYDNLFETSFPYSMGWHGAPFN---GEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGETQRDLTAEQAAERLRALSDI 341


                  ..
gi 385251404  256 HY 257
Cdd:TIGR00209 342 HY 343
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
17-255 2.21e-113

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 329.49  E-value: 2.21e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  17 SKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREE 94
Cdd:COG1085  100 HEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLPHPHGQIIAYPFVPPRIAREL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  95 RSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLL 174
Cdd:COG1085  180 RGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 175 TKYDNLFETsFPYSMGWHGAPTGSEAGanwNHWQLHAHYYPPlLRSATVRKFMVGYEMLAQA-QRDLTPEQAAERLRALP 253
Cdd:COG1085  260 RRLDNLLGD-FPYNMGLHQAPVDGEER---DHYHWHLEIYPR-LRSATVLKFLAGFELGAGAfINDVTPEQAAERLREVS 334


                 ..
gi 385251404 254 EV 255
Cdd:COG1085  335 EV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
 93-261 1.01e-91

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: 268.19  E-value: 1.01e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404   93 EERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKK 172
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  173 LLTKYDNLFETSFPYSMGWHGAPTGSEagaNWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 252
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLNAE---ELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157


                  ....*....
gi 385251404  253 PEVHYHLGQ 261
Cdd:pfam02744 158 SEVHYRWAL 166
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
 16-87 3.28e-38

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: 132.41  E-value: 3.28e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385251404   16 ESKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLP 87
Cdd:pfam01087 109 DCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGAssYPKCVLCFENEGYAMGCSNPHPHGQIWASSHLP 182
PLN02643 PLN02643
ADP-glucose phosphorylase
 24-209 1.48e-20

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 89.43  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404  24 PWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYK 101
Cdd:PLN02643 115 PVHSVQLSDLPARHIGEVLKAYKKRINQLQSdsRFKYVQVFKNHGASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYF 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 102 SQHGEPLLMEYSRQELLRKErlvltSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLF 181
Cdd:PLN02643 195 EKTGKCSLCEVVKKDLLIDE-----SSHFVSIAPFAATFPFEIWIIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQL 269

                        170       180
                 ....*....|....*....|....*....
gi 385251404 182 ETSfPYSMGWHGAPTG-SEAGANWNHWQL 209
Cdd:PLN02643 270 NDP-PYNYMIQTSPLGvEESNLPYTHWFL 297
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 29-82 5.78e-08

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


Pssm-ID: 238263 [Multi-domain]  Cd Length: 86  Bit Score: 49.39  E-value: 5.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385251404  29 TLPLMSVPEIRAVVDAWASVTEEL--GAQYPWVQIFENKGAMMGCSNPHPHCQVWA 82
Cdd:cd00468   31 TLPDLDEALLADLVITAQRVAAELekHGNVPSLTVFVNDGAAAGQSVPHVHLHVLP 86
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 122-251 6.54e-04

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: 38.78  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385251404 122 RLVLTSEHWLVlvpFWATWPYQ---TLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFEtsfP--YSMGWHgapT 196
Cdd:COG0537   16 LIVYEDEHVLA---FLDINPYApghTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALG---PdgFNLGIN---N 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 385251404 197 GSEAGANWNHwqLHAHYYPpllRSATVRKFMVGYEMLAQAQRdltPEQAAERLRA 251
Cdd:COG0537   87 GEAAGQTVPH--LHVHVIP---RYEGDDNFMPVIGTKVDPEE---LEETARKLRA 133
PRK14109 PRK14109
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ...
 188-252 8.48e-03

bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;


Pssm-ID: 237613 [Multi-domain]  Cd Length: 1007  Bit Score: 37.52  E-value: 8.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385251404  188 SMGWHGAPTGSEAGANWNHWQLHAH---------YYPPLLrSATVRkfmvgyemLAQAQRDLTPEQAAERLRAL 252
Cdd:PRK14109  464 AAGLRPDGRRDAAEELRAEWRRTRRrvrrlheklFYRPLL-EAVAR--------LSAEEARLSPEAARRRLAAL 528
 
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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