NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|386769761|ref|NP_001246063|]
View 

glucosidase 2 beta subunit, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRKCSH-like super family cl28164
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
26-193 6.02e-40

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


The actual alignment was detected with superfamily member pfam12999:

Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 143.01  E-value: 6.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   26 ASEVPRPLGVPLAKASLYQPRAgENSWTCLDGSR-TIPFSHINDDYCDCADGSDEPGTAACPQGQFHCVNKGHQPVNIPS 104
Cdd:pfam12999  13 AIALGKLRGVSPDNLHLYQPDE-NGNWKCLNHSEiKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  105 SQVQDGICD---CCDGSDESETVgCPNTCLELGAAAAVQRRNAAELHKRGAERRQEMItrgkqmrAEREARRLELDQRRK 181
Cdd:pfam12999  92 FKVDDGVCDydiCCDGSDEALGK-CPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLL-------LAAQKKRDELKKRLK 163
                         170
                  ....*....|...
gi 386769761  182 EQE-LLRAEKEQL 193
Cdd:pfam12999 164 ELEdSLPAKQQRL 176
PRKCSH super family cl06793
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
398-547 2.06e-19

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


The actual alignment was detected with superfamily member pfam13015:

Pssm-ID: 414904  Cd Length: 154  Bit Score: 85.27  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  398 LEEVERSLREIQQEVNEIDDQNNKGYGLTEEWAVHDGQCYNFEDREYVYTLCPFDRASQKSRSggpettLGRWDKWSGep 477
Cdd:pfam13015   5 IDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDDIS------IGNFKKQEG-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761  478 kqySQQKYTNGAACWNGPNRSAIINISCALEPKITAVSEPNRCEYYFEFETPAACDSEAFQ---SESENLHDE 547
Cdd:pfam13015  77 ---NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAACSNVYLVkslAEEESLAPF 146
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
154-428 1.12e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   154 RRQEMITRGkqmRAEREARRLEldqRRKEQELLRAEKEQLKQTAEALEAEAIEIfKEQQREVDADTAQAEREPQQMRQEA 233
Cdd:TIGR02168  656 RPGGVITGG---SAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQI 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   234 TLTFVRY-----------DTNKDGFVEVTELMVDMNLDRDRngvVTVEEAKYFLDERERVDLDAFVTLAWPRIKSL---- 298
Cdd:TIGR02168  729 SALRKDLarleaeveqleERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKALreal 805
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   299 ----------------------QMLAEGLFQPPQPEEVAQQPEVTTESIQptppKLSEEQAEL-AGDDDIEADEEGEEDQ 355
Cdd:TIGR02168  806 delraeltllneeaanlrerleSLERRIAATERRLEDLEEQIEELSEDIE----SLAAEIEELeELIEELESELEALLNE 881
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761   356 YDDEEPDVGVGEASPDAEEATPPNYDPETQRLIQQANEARNALEEVERSLREIQQEVNEIDDQNNKGYGLTEE 428
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
 
Name Accession Description Interval E-value
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
26-193 6.02e-40

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 143.01  E-value: 6.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   26 ASEVPRPLGVPLAKASLYQPRAgENSWTCLDGSR-TIPFSHINDDYCDCADGSDEPGTAACPQGQFHCVNKGHQPVNIPS 104
Cdd:pfam12999  13 AIALGKLRGVSPDNLHLYQPDE-NGNWKCLNHSEiKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  105 SQVQDGICD---CCDGSDESETVgCPNTCLELGAAAAVQRRNAAELHKRGAERRQEMItrgkqmrAEREARRLELDQRRK 181
Cdd:pfam12999  92 FKVDDGVCDydiCCDGSDEALGK-CPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLL-------LAAQKKRDELKKRLK 163
                         170
                  ....*....|...
gi 386769761  182 EQE-LLRAEKEQL 193
Cdd:pfam12999 164 ELEdSLPAKQQRL 176
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
398-547 2.06e-19

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. The beta-subunit confers substrate specificity for di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit.


Pssm-ID: 404038  Cd Length: 154  Bit Score: 85.27  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  398 LEEVERSLREIQQEVNEIDDQNNKGYGLTEEWAVHDGQCYNFEDREYVYTLCPFDRASQKSRSggpettLGRWDKWSGep 477
Cdd:pfam13015   5 IDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDDIS------IGNFKKQEG-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761  478 kqySQQKYTNGAACWNGPNRSAIINISCALEPKITAVSEPNRCEYYFEFETPAACDSEAFQ---SESENLHDE 547
Cdd:pfam13015  77 ---NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAACSNVYLVkslAEEESLAPF 146
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
85-120 1.02e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.28  E-value: 1.02e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 386769761  85 CPQGQFHCVNKghqpVNIPSSQVQDGICDCCDGSDE 120
Cdd:cd00112    1 CPPNEFRCANG----RCIPSSWVCDGEDDCGDGSDE 32
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
85-120 1.97e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.46  E-value: 1.97e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 386769761    85 CPQGQFHCVNkGHQpvnIPSSQVQDGICDCCDGSDE 120
Cdd:smart00192   2 CPPGEFQCDN-GRC---IPSSWVCDGVDDCGDGSDE 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
154-428 1.12e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   154 RRQEMITRGkqmRAEREARRLEldqRRKEQELLRAEKEQLKQTAEALEAEAIEIfKEQQREVDADTAQAEREPQQMRQEA 233
Cdd:TIGR02168  656 RPGGVITGG---SAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQI 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   234 TLTFVRY-----------DTNKDGFVEVTELMVDMNLDRDRngvVTVEEAKYFLDERERVDLDAFVTLAWPRIKSL---- 298
Cdd:TIGR02168  729 SALRKDLarleaeveqleERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKALreal 805
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   299 ----------------------QMLAEGLFQPPQPEEVAQQPEVTTESIQptppKLSEEQAEL-AGDDDIEADEEGEEDQ 355
Cdd:TIGR02168  806 delraeltllneeaanlrerleSLERRIAATERRLEDLEEQIEELSEDIE----SLAAEIEELeELIEELESELEALLNE 881
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761   356 YDDEEPDVGVGEASPDAEEATPPNYDPETQRLIQQANEARNALEEVERSLREIQQEVNEIDDQNNKGYGLTEE 428
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
219-271 6.19e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 6.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769761 219 TAQAEREPQQMRQEATLTFVRYDTNKDGFVEVTELMVDMN---------------LDRDRNGVVTVEE 271
Cdd:COG5126   57 AGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTalgvseeeadelfarLDTDGDGKISFEE 124
 
Name Accession Description Interval E-value
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
26-193 6.02e-40

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 143.01  E-value: 6.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   26 ASEVPRPLGVPLAKASLYQPRAgENSWTCLDGSR-TIPFSHINDDYCDCADGSDEPGTAACPQGQFHCVNKGHQPVNIPS 104
Cdd:pfam12999  13 AIALGKLRGVSPDNLHLYQPDE-NGNWKCLNHSEiKLSFDQVNDDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  105 SQVQDGICD---CCDGSDESETVgCPNTCLELGAAAAVQRRNAAELHKRGAERRQEMItrgkqmrAEREARRLELDQRRK 181
Cdd:pfam12999  92 FKVDDGVCDydiCCDGSDEALGK-CPNKCGEIARQFEEYLTEHNNSVKNGLKIKEGLL-------LAAQKKRDELKKRLK 163
                         170
                  ....*....|...
gi 386769761  182 EQE-LLRAEKEQL 193
Cdd:pfam12999 164 ELEdSLPAKQQRL 176
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
398-547 2.06e-19

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. The beta-subunit confers substrate specificity for di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit.


Pssm-ID: 404038  Cd Length: 154  Bit Score: 85.27  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761  398 LEEVERSLREIQQEVNEIDDQNNKGYGLTEEWAVHDGQCYNFEDREYVYTLCPFDRASQKSRSggpettLGRWDKWSGep 477
Cdd:pfam13015   5 IDEHEKDIKKIESDITILEENLNSRYGPDDILRAYEGRETKEKIGGYTYKVCFLGSIFQDDIS------IGNFKKQEG-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761  478 kqySQQKYTNGAACWNGPNRSAIINISCALEPKITAVSEPNRCEYYFEFETPAACDSEAFQ---SESENLHDE 547
Cdd:pfam13015  77 ---NKLYYENGAKCWNGPHRSAIVEVECGDVNELVSVSEPEKCEYLFVVKSPAACSNVYLVkslAEEESLAPF 146
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
434-491 2.03e-12

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


Pssm-ID: 400321  Cd Length: 72  Bit Score: 62.56  E-value: 2.03e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769761  434 GQCYNFEDREYVYTLCPFDRASQKSRS---GGPETTLGRWDK-----------WSGEPKQYSQQKYTNGAAC 491
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGqekGGSSFSLGRFSEsswaestyddeWTKGSNRYISMIYGNGTKC 72
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
85-120 1.02e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.28  E-value: 1.02e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 386769761  85 CPQGQFHCVNKghqpVNIPSSQVQDGICDCCDGSDE 120
Cdd:cd00112    1 CPPNEFRCANG----RCIPSSWVCDGEDDCGDGSDE 32
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
85-120 1.97e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.46  E-value: 1.97e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 386769761    85 CPQGQFHCVNkGHQpvnIPSSQVQDGICDCCDGSDE 120
Cdd:smart00192   2 CPPGEFQCDN-GRC---IPSSWVCDGVDDCGDGSDE 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
154-428 1.12e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   154 RRQEMITRGkqmRAEREARRLEldqRRKEQELLRAEKEQLKQTAEALEAEAIEIfKEQQREVDADTAQAEREPQQMRQEA 233
Cdd:TIGR02168  656 RPGGVITGG---SAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQI 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   234 TLTFVRY-----------DTNKDGFVEVTELMVDMNLDRDRngvVTVEEAKYFLDERERVDLDAFVTLAWPRIKSL---- 298
Cdd:TIGR02168  729 SALRKDLarleaeveqleERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKALreal 805
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769761   299 ----------------------QMLAEGLFQPPQPEEVAQQPEVTTESIQptppKLSEEQAEL-AGDDDIEADEEGEEDQ 355
Cdd:TIGR02168  806 delraeltllneeaanlrerleSLERRIAATERRLEDLEEQIEELSEDIE----SLAAEIEELeELIEELESELEALLNE 881
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769761   356 YDDEEPDVGVGEASPDAEEATPPNYDPETQRLIQQANEARNALEEVERSLREIQQEVNEIDDQNNKGYGLTEE 428
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
219-271 6.19e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 6.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769761 219 TAQAEREPQQMRQEATLTFVRYDTNKDGFVEVTELMVDMN---------------LDRDRNGVVTVEE 271
Cdd:COG5126   57 AGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTalgvseeeadelfarLDTDGDGKISFEE 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH