NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|223532189|gb|EEF33994|]
View 

conserved hypothetical protein [Ricinus communis]

Protein Classification

SMC_prok_B and ATG11 domain-containing protein( domain architecture ID 11897327)

protein containing domains ATG17_like, SMC_prok_B, and ATG11

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
988-1133 1.09e-25

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


:

Pssm-ID: 463063  Cd Length: 130  Bit Score: 103.45  E-value: 1.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   988 KELEEKKELVTTLYKKHQLEK-----------QANKERISFGRLEIHEIAAFVINTAGH------YEAINRSSSNYYLSA 1050
Cdd:pfam10377    2 SAVIKRFKDVETLAKKLTKENkskrekleklqSEAHEKITLKNFKVGDLALFLPTRRHNdlstppWAAFNVGAPHYFLKA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  1051 ESValftdHLPSRPRYIVGQIVHIERQTAKPlparpehgrgnpvdhltsdtgtdlltlknLGSSSNPYNLPIGCEYFVVT 1130
Cdd:pfam10377   82 DSL-----LALKSREWFVGRITSIEERVVDL-----------------------------SDKDSNPFKLSKGTVWYLVT 127

                   ...
gi 223532189  1131 VAM 1133
Cdd:pfam10377  128 AEE 130
ATG17_like super family cl27196
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
153-484 3.60e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


The actual alignment was detected with superfamily member pfam04108:

Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 81.67  E-value: 3.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   153 THAKYAH--CERFLREQKVQGRAIDVARGNLDQYYRMISQNYSEFMKRYTQQHRMHSELLVNYRRDLEKLRSIKLHPALQ 230
Cdd:pfam04108   17 TDARSLLeeLVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALP 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   231 ATT--RTCLVDFVKEENLRKAVENCSNSHRQFEKKVSEFKQM-------FGEVKRKVEDLFACRASFPLKNLELtiKEHQ 301
Cdd:pfam04108   97 PGEekQKTLLDFIDEDSVEILRDALKELIDELQAAQESLDSDlkrfdddLRDLQKELESLSSPSESISLIPTLL--KELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   302 KFINEQKSIMQSLSKDvntvkklVDDCLSCQLSSSlrphdavSALGPMYDVHDK------NHLPKMEACGRSITKLLE-- 373
Cdd:pfam04108  175 SLEEEMASLLESLTNH-------YDQCVTAVKLTE-------GGRAEMLEVLENdareldDVVPELQDRLDEMENNYErl 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   374 -FCKDKKNEMNIFVHNYMQKITYVSYIIKDAKLQFPVFREA-MVRQDDLFTDLKLVR-------GIGPAYRACLAEVVRR 444
Cdd:pfam04108  241 qKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERwEEEKETIEDYLSELEdlrefyeGFPSAYGSLLLEVERR 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 223532189   445 KASMKLYMGMAGQLAERLATKREVEVRRREEFLKAHSSYI 484
Cdd:pfam04108  321 REWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
812-1005 1.39e-05

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: 49.67  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   812 AKTSDVVLELQRALDEKSDQLGEIENKLkaamedvTVLTRELEMSRKLLDESQMNCAHLENCLHEAREEAQThlcaadrR 891
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEELESRLEELEEQLET-------L 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   892 ASEYNALRASAVKMRSLFERLKScvcapvgvagfadSLRALAQSLGNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREE 971
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEA-------------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
                          170       180       190
                   ....*....|....*....|....*....|....
gi 223532189   972 LLDKYPKLEAANEQLRKELEEKKELVTTLYKKHQ 1005
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA 485
 
Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
988-1133 1.09e-25

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 103.45  E-value: 1.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   988 KELEEKKELVTTLYKKHQLEK-----------QANKERISFGRLEIHEIAAFVINTAGH------YEAINRSSSNYYLSA 1050
Cdd:pfam10377    2 SAVIKRFKDVETLAKKLTKENkskrekleklqSEAHEKITLKNFKVGDLALFLPTRRHNdlstppWAAFNVGAPHYFLKA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  1051 ESValftdHLPSRPRYIVGQIVHIERQTAKPlparpehgrgnpvdhltsdtgtdlltlknLGSSSNPYNLPIGCEYFVVT 1130
Cdd:pfam10377   82 DSL-----LALKSREWFVGRITSIEERVVDL-----------------------------SDKDSNPFKLSKGTVWYLVT 127

                   ...
gi 223532189  1131 VAM 1133
Cdd:pfam10377  128 AEE 130
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
153-484 3.60e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 81.67  E-value: 3.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   153 THAKYAH--CERFLREQKVQGRAIDVARGNLDQYYRMISQNYSEFMKRYTQQHRMHSELLVNYRRDLEKLRSIKLHPALQ 230
Cdd:pfam04108   17 TDARSLLeeLVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALP 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   231 ATT--RTCLVDFVKEENLRKAVENCSNSHRQFEKKVSEFKQM-------FGEVKRKVEDLFACRASFPLKNLELtiKEHQ 301
Cdd:pfam04108   97 PGEekQKTLLDFIDEDSVEILRDALKELIDELQAAQESLDSDlkrfdddLRDLQKELESLSSPSESISLIPTLL--KELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   302 KFINEQKSIMQSLSKDvntvkklVDDCLSCQLSSSlrphdavSALGPMYDVHDK------NHLPKMEACGRSITKLLE-- 373
Cdd:pfam04108  175 SLEEEMASLLESLTNH-------YDQCVTAVKLTE-------GGRAEMLEVLENdareldDVVPELQDRLDEMENNYErl 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   374 -FCKDKKNEMNIFVHNYMQKITYVSYIIKDAKLQFPVFREA-MVRQDDLFTDLKLVR-------GIGPAYRACLAEVVRR 444
Cdd:pfam04108  241 qKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERwEEEKETIEDYLSELEdlrefyeGFPSAYGSLLLEVERR 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 223532189   445 KASMKLYMGMAGQLAERLATKREVEVRRREEFLKAHSSYI 484
Cdd:pfam04108  321 REWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
812-1005 1.39e-05

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: 49.67  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   812 AKTSDVVLELQRALDEKSDQLGEIENKLkaamedvTVLTRELEMSRKLLDESQMNCAHLENCLHEAREEAQThlcaadrR 891
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEELESRLEELEEQLET-------L 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   892 ASEYNALRASAVKMRSLFERLKScvcapvgvagfadSLRALAQSLGNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREE 971
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEA-------------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
                          170       180       190
                   ....*....|....*....|....*....|....
gi 223532189   972 LLDKYPKLEAANEQLRKELEEKKELVTTLYKKHQ 1005
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
777-1013 8.00e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  777 KDKLVAQLGMSLANSSTAESMPEAQNVLPSDATVEAKTSDVVLELQRALDEKSDQLGEIENKLKAAMEDVTVLTRELEMS 856
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  857 RKLLDESQMNCAHLENCLHEAREEAQTHLCAAdrraseYNALRASAVKMRslferlkscvcapVGVAGFADSLRALAqsL 936
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRAL------YRLGRQPPLALL-------------LSPEDFLDAVRRLQ--Y 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223532189  937 GNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREELLDKYPKLEAANEQLRKELEEKKELVTTLYKKHQLEKQANKE 1013
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
 
Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
988-1133 1.09e-25

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 103.45  E-value: 1.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   988 KELEEKKELVTTLYKKHQLEK-----------QANKERISFGRLEIHEIAAFVINTAGH------YEAINRSSSNYYLSA 1050
Cdd:pfam10377    2 SAVIKRFKDVETLAKKLTKENkskrekleklqSEAHEKITLKNFKVGDLALFLPTRRHNdlstppWAAFNVGAPHYFLKA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  1051 ESValftdHLPSRPRYIVGQIVHIERQTAKPlparpehgrgnpvdhltsdtgtdlltlknLGSSSNPYNLPIGCEYFVVT 1130
Cdd:pfam10377   82 DSL-----LALKSREWFVGRITSIEERVVDL-----------------------------SDKDSNPFKLSKGTVWYLVT 127

                   ...
gi 223532189  1131 VAM 1133
Cdd:pfam10377  128 AEE 130
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
153-484 3.60e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 81.67  E-value: 3.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   153 THAKYAH--CERFLREQKVQGRAIDVARGNLDQYYRMISQNYSEFMKRYTQQHRMHSELLVNYRRDLEKLRSIKLHPALQ 230
Cdd:pfam04108   17 TDARSLLeeLVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALP 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   231 ATT--RTCLVDFVKEENLRKAVENCSNSHRQFEKKVSEFKQM-------FGEVKRKVEDLFACRASFPLKNLELtiKEHQ 301
Cdd:pfam04108   97 PGEekQKTLLDFIDEDSVEILRDALKELIDELQAAQESLDSDlkrfdddLRDLQKELESLSSPSESISLIPTLL--KELE 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   302 KFINEQKSIMQSLSKDvntvkklVDDCLSCQLSSSlrphdavSALGPMYDVHDK------NHLPKMEACGRSITKLLE-- 373
Cdd:pfam04108  175 SLEEEMASLLESLTNH-------YDQCVTAVKLTE-------GGRAEMLEVLENdareldDVVPELQDRLDEMENNYErl 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   374 -FCKDKKNEMNIFVHNYMQKITYVSYIIKDAKLQFPVFREA-MVRQDDLFTDLKLVR-------GIGPAYRACLAEVVRR 444
Cdd:pfam04108  241 qKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERwEEEKETIEDYLSELEdlrefyeGFPSAYGSLLLEVERR 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 223532189   445 KASMKLYMGMAGQLAERLATKREVEVRRREEFLKAHSSYI 484
Cdd:pfam04108  321 REWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
812-1005 1.39e-05

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: 49.67  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   812 AKTSDVVLELQRALDEKSDQLGEIENKLkaamedvTVLTRELEMSRKLLDESQMNCAHLENCLHEAREEAQThlcaadrR 891
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEELESRLEELEEQLET-------L 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   892 ASEYNALRASAVKMRSLFERLKScvcapvgvagfadSLRALAQSLGNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREE 971
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEA-------------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
                          170       180       190
                   ....*....|....*....|....*....|....
gi 223532189   972 LLDKYPKLEAANEQLRKELEEKKELVTTLYKKHQ 1005
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
777-1013 8.00e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  777 KDKLVAQLGMSLANSSTAESMPEAQNVLPSDATVEAKTSDVVLELQRALDEKSDQLGEIENKLKAAMEDVTVLTRELEMS 856
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189  857 RKLLDESQMNCAHLENCLHEAREEAQTHLCAAdrraseYNALRASAVKMRslferlkscvcapVGVAGFADSLRALAqsL 936
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRAL------YRLGRQPPLALL-------------LSPEDFLDAVRRLQ--Y 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223532189  937 GNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREELLDKYPKLEAANEQLRKELEEKKELVTTLYKKHQLEKQANKE 1013
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
753-1016 8.05e-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: 40.43  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   753 LNTQLDSLMTEPQREELQVSDKD----GKDKLVAQLGMSLANSSTAESMPEAQNVLPSDATVEAKtsDVVLELQRALDEK 828
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE--AEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   829 SDQLGEIENKLKAAMEDVTVLTRELEMSRKLLDEsqmncahLENCLHEAREEAQThlcAADRRASEYNALRASAVKMRSL 908
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDE-------LRAELTLLNEEAAN---LRERLESLERRIAATERRLEDL 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223532189   909 FERLKScvcapvgvagfadsLRALAQSLgNSNNDNEDDSTAEFRKCIRALSEKVSFLSRHREELLDKYPKL-------EA 981
Cdd:TIGR02168  844 EEQIEE--------------LSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELseelrelES 908
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 223532189   982 ANEQLRKELEEKKELVTTL---YKKHQLEKQANKERIS 1016
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLelrLEGLEVRIDNLQERLS 946
 
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