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Conserved domains on  [gi|1595488041|ref|NP_001356069|]
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galactose-1-phosphate uridylyltransferase isoform 4 [Mus musculus]

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;
2-238 7.12e-166

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: 462.07  E-value: 7.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   2 CFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQTY 81
Cdd:PRK11720  110 CFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQRAY 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  82 HSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNL 161
Cdd:PRK11720  190 FAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALKKLTSRYDNL 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488041 162 FETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHY 238
Cdd:PRK11720  270 FQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
2-238 7.12e-166

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 462.07  E-value: 7.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   2 CFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQTY 81
Cdd:PRK11720  110 CFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQRAY 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  82 HSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNL 161
Cdd:PRK11720  190 FAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALKKLTSRYDNL 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488041 162 FETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHY 238
Cdd:PRK11720  270 FQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
1-233 5.46e-126

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: 360.46  E-value: 5.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   1 MCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQ 78
Cdd:cd00608    97 ICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHGQIWALPFLPPEVARELRNQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  79 QTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKY 158
Cdd:cd00608   177 KAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLLARY 256
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488041 159 DNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQRDLTPEQAAERLRAL 233
Cdd:cd00608   257 DNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDVTPEQAAARLREV 329
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
1-238 9.77e-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: 355.42  E-value: 9.77e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   1 MCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQT 80
Cdd:TIGR00209 109 ICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVEREDRLQKE 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  81 YHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDN 160
Cdd:TIGR00209 189 YFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLRITDLTDAQRSDLALILKKLTSKYDN 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488041 161 LFETSFPYSMGWHGAPTglkTGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHY 238
Cdd:TIGR00209 269 LFETSFPYSMGWHGAPF---NGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGETQRDLTAEQAAERLRALSDIHY 343
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
2-236 1.95e-113

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 328.72  E-value: 1.95e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   2 CFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQ 79
Cdd:COG1085   104 CFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLPHPHGQIIAYPFVPPRIARELRGAR 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  80 TYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYD 159
Cdd:COG1085   184 AYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVLRRLD 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488041 160 NLFETsFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPlLRSATVRKFMVGYEMLAQA-QRDLTPEQAAERLRALPEV 236
Cdd:COG1085   264 NLLGD-FPYNMGLHQAPVD---GEERDHYHWHLEIYPR-LRSATVLKFLAGFELGAGAfINDVTPEQAAERLREVSEV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
74-242 1.54e-87

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: 257.02  E-value: 1.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  74 EERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKK 153
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041 154 LLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 233
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLN---AEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157

                  ....*....
gi 1595488041 234 PEVHYCLAQ 242
Cdd:pfam02744 158 SEVHYRWAL 166
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
2-238 7.12e-166

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 462.07  E-value: 7.12e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   2 CFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQTY 81
Cdd:PRK11720  110 CFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCSNPHPHGQIWANSFLPNEAEREDRLQRAY 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  82 HSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNL 161
Cdd:PRK11720  190 FAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHVLRLTDLTDAQRDDLALALKKLTSRYDNL 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488041 162 FETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHY 238
Cdd:PRK11720  270 FQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
1-233 5.46e-126

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: 360.46  E-value: 5.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   1 MCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQ 78
Cdd:cd00608    97 ICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHGQIWALPFLPPEVARELRNQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  79 QTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKY 158
Cdd:cd00608   177 KAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLLARY 256
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488041 159 DNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQRDLTPEQAAERLRAL 233
Cdd:cd00608   257 DNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDVTPEQAAARLREV 329
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
1-238 9.77e-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: 355.42  E-value: 9.77e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   1 MCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQT 80
Cdd:TIGR00209 109 ICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVEREDRLQKE 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  81 YHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDN 160
Cdd:TIGR00209 189 YFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLRITDLTDAQRSDLALILKKLTSKYDN 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488041 161 LFETSFPYSMGWHGAPTglkTGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHY 238
Cdd:TIGR00209 269 LFETSFPYSMGWHGAPF---NGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGETQRDLTAEQAAERLRALSDIHY 343
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
2-236 1.95e-113

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 328.72  E-value: 1.95e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   2 CFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQ 79
Cdd:COG1085   104 CFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLPHPHGQIIAYPFVPPRIARELRGAR 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  80 TYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYD 159
Cdd:COG1085   184 AYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVLRRLD 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488041 160 NLFETsFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPlLRSATVRKFMVGYEMLAQA-QRDLTPEQAAERLRALPEV 236
Cdd:COG1085   264 NLLGD-FPYNMGLHQAPVD---GEERDHYHWHLEIYPR-LRSATVLKFLAGFELGAGAfINDVTPEQAAERLREVSEV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
74-242 1.54e-87

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: 257.02  E-value: 1.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  74 EERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKK 153
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041 154 LLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 233
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLN---AEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157

                  ....*....
gi 1595488041 234 PEVHYCLAQ 242
Cdd:pfam02744 158 SEVHYRWAL 166
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
1-68 5.94e-37

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: 128.56  E-value: 5.94e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   1 MCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLP 68
Cdd:pfam01087 113 TCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGAssYPKCVLCFENEGYAMGCSNPHPHGQIWASSHLP 182
PLN02643 PLN02643
ADP-glucose phosphorylase
5-190 2.32e-22

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 93.67  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041   5 PWSDVTLPLMSVPEIRAVIDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQTYH 82
Cdd:PLN02643  115 PVHSVQLSDLPARHIGEVLKAYKKRINQLQSdsRFKYVQVFKNHGASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYF 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041  83 SQHGKPLLLEYGHQELLRKErlvltSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNLF 162
Cdd:PLN02643  195 EKTGKCSLCEVVKKDLLIDE-----SSHFVSIAPFAATFPFEIWIIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQL 269
                         170       180
                  ....*....|....*....|....*....
gi 1595488041 163 ETSfPYSMGWHGAPTGLKTGATC-DHWQL 190
Cdd:PLN02643  270 NDP-PYNYMIQTSPLGVEESNLPyTHWFL 297
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
10-63 2.45e-07

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: 47.46  E-value: 2.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595488041  10 TLPLMSVPEIRAVIDAWASVTEEL--GAQYPWVQIFENKGAMMGCSNPHPHCQVWA 63
Cdd:cd00468    31 TLPDLDEALLADLVITAQRVAAELekHGNVPSLTVFVNDGAAAGQSVPHVHLHVLP 86
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
125-232 3.08e-03

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: 36.85  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488041 125 TLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSfPYSMGWHgapTGLKTGATCDHwqLHAHYYPpllRSATV 204
Cdd:COG0537    38 TLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPD-GFNLGIN---NGEAAGQTVPH--LHVHVIP---RYEGD 108
                          90       100
                  ....*....|....*....|....*...
gi 1595488041 205 RKFMVGYEMLAQAQRdltPEQAAERLRA 232
Cdd:COG0537   109 DNFMPVIGTKVDPEE---LEETARKLRA 133
 
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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