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Conserved domains on  [gi|985482087|ref|NP_001306231|]
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RILP-like protein 1 isoform 3 [Homo sapiens]

Protein Classification

RILP domain-containing protein( domain architecture ID 10568657)

RILP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 144-206 1.13e-21

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


:

Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 85.34  E-value: 1.13e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985482087  144 TLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEEN----RIPQPPPIAHPRTSP--QPESGIKRLF 206
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEipslRLESPSPRTKPQRSKikQEESGIKRLF 69
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-183 1.96e-05

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  17 EVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAEL 96
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  97 GKLRERLQ---GEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFT-LQELRDVLHERNELKSKVFLLQEELAYY 172
Cdd:COG4942  100 EAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEAL 179

                        170
                 ....*....|.
gi 985482087 173 KSEEMEEENRI 183
Cdd:COG4942  180 LAELEEERAAL 190
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 144-206 1.13e-21

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 85.34  E-value: 1.13e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985482087  144 TLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEEN----RIPQPPPIAHPRTSP--QPESGIKRLF 206
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEipslRLESPSPRTKPQRSKikQEESGIKRLF 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-183 1.96e-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: 45.14  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  17 EVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAEL 96
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  97 GKLRERLQ---GEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFT-LQELRDVLHERNELKSKVFLLQEELAYY 172
Cdd:COG4942  100 EAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEAL 179

                        170
                 ....*....|.
gi 985482087 173 KSEEMEEENRI 183
Cdd:COG4942  180 LAELEEERAAL 190
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-168 1.61e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087     6 ERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEA----LQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEAD 81
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    82 LQTKEQEMGSLRAELGKLRERLQ--GEHSQNGEEEPETEPVGE---ESISDAEKVAMDLKDPNrpRFTLQELRDVLHERN 156
Cdd:TIGR02169  912 IEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEdvqAELQRVEEEIRALEPVN--MLAIQEYEEVLKRLD 989

                          170
                   ....*....|..
gi 985482087   157 ELKSKVFLLQEE 168
Cdd:TIGR02169  990 ELKEKRAKLEEE 1001
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 6-180 9.25e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    6 ERERQVMKKLKEVVDKQRDEIRAK----DRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEAD 81
Cdd:pfam07888  58 EKEKERYKRDREQWERQRRELESRvaelKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087   82 LQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDpnrprftLQELRDVLHERN----E 157
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE-------FQELRNSLAQRDtqvlQ 210

                         170       180
                  ....*....|....*....|...
gi 985482087  158 LKSKVFLLQEELAYYKSEEMEEE 180
Cdd:pfam07888 211 LQDTITTLTQKLTTAHRKEAENE 233
 
Name Accession Description Interval E-value
RILP pfam11461
Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil ...
 144-206 1.13e-21

Rab interacting lysosomal protein; RILP contains a domain which contains two coiled-coil regions and is found mainly in the cytosol. RILP is recruited onto late endosomal and lysosomal membranes by Rab7 and acts as a downstream effector of Rab7. This recruitment process is important for phagosome maturation and fusion with late endosomes and lysosomes.


Pssm-ID: 463282 [Multi-domain]  Cd Length: 69  Bit Score: 85.34  E-value: 1.13e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985482087  144 TLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEEN----RIPQPPPIAHPRTSP--QPESGIKRLF 206
Cdd:pfam11461   1 TLQELRDVLQERNELKAQLFLLQEELAYYKSGLLNEEEipslRLESPSPRTKPQRSKikQEESGIKRLF 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-183 1.96e-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: 45.14  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  17 EVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAEL 96
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  97 GKLRERLQ---GEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFT-LQELRDVLHERNELKSKVFLLQEELAYY 172
Cdd:COG4942  100 EAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEAL 179

                        170
                 ....*....|.
gi 985482087 173 KSEEMEEENRI 183
Cdd:COG4942  180 LAELEEERAAL 190
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-168 1.61e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087     6 ERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEA----LQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEAD 81
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    82 LQTKEQEMGSLRAELGKLRERLQ--GEHSQNGEEEPETEPVGE---ESISDAEKVAMDLKDPNrpRFTLQELRDVLHERN 156
Cdd:TIGR02169  912 IEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEdvqAELQRVEEEIRALEPVN--MLAIQEYEEVLKRLD 989

                          170
                   ....*....|..
gi 985482087   157 ELKSKVFLLQEE 168
Cdd:TIGR02169  990 ELKEKRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-183 3.59e-04

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: 41.58  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087     5 SERERQVMKKLKEVvdkqRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQT 84
Cdd:TIGR02168  308 RERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    85 -------KEQEMGSLRAELGKLRERLQG-EHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFTLQELRDVLHERN 156
Cdd:TIGR02168  384 lrskvaqLELQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463

                          170       180
                   ....*....|....*....|....*...
gi 985482087   157 ELKSKVF-LLQEELAYYKSEEMEEENRI 183
Cdd:TIGR02168  464 EELREELeEAEQALDAAERELAQLQARL 491
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 6-180 9.25e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    6 ERERQVMKKLKEVVDKQRDEIRAK----DRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEAD 81
Cdd:pfam07888  58 EKEKERYKRDREQWERQRRELESRvaelKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087   82 LQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDpnrprftLQELRDVLHERN----E 157
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE-------FQELRNSLAQRDtqvlQ 210

                         170       180
                  ....*....|....*....|...
gi 985482087  158 LKSKVFLLQEELAYYKSEEMEEE 180
Cdd:pfam07888 211 LQDTITTLTQKLTTAHRKEAENE 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-183 1.79e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087   6 ERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTK 85
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087  86 EQEMGSLRAELGKLRERLQGEHSQNGEEEPETEpVGEESISDAEKVAMDLkdpnrprftLQELRDVLHERNELKSKVFLL 165
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELE-EAEAELAEAEEALLEA---------EAELAEAEEELEELAEELLEA 391

                        170
                 ....*....|....*...
gi 985482087 166 QEELAYYKSEEMEEENRI 183
Cdd:COG1196  392 LRAAAELAAQLEELEEAE 409
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-184 1.84e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087     6 ERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEAL-QQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQT 84
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    85 KEQEMGSLRAELGKLRERL---QGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFTLQE-LRDVLHERNELKS 160
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkLEKLKREINELKR 406

                          170       180
                   ....*....|....*....|....
gi 985482087   161 KVFLLQEELAYYKSEEMEEENRIP 184
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIA 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 13-175 2.18e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    13 KKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSL 92
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    93 RAELGKLRERLQGEHSQNGEEEPETEPVGE---ESISDAEKVAMDLKDPNRPRFTLQELRDvlhernELKSKVFLLQEEL 169
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLS------KYEQELYDLKEEY 478


                   ....*.
gi 985482087   170 AYYKSE 175
Cdd:TIGR02169  479 DRVEKE 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-183 2.96e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087     6 ERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTrlmkinhDLRHRVTVVEAQGKALIEQKVELEADLQTK 85
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------ELEEDLSSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985482087    86 EQEMGSLRAELGKLRERLQGEHSQNGEEEPETEpvgEESISDAEKVAMDLKdpnrprftlQELRDVLHERNELKSKVFLL 165
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSKL---EEEVSRIEARLREIE---------QKLNRLTLEKEYLEKEIQEL 838

                          170
                   ....*....|....*...
gi 985482087   166 QEELAYYKSEEMEEENRI 183
Cdd:TIGR02169  839 QEQRIDLKEQIKSIEKEI 856
 
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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