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Conserved domains on  [gi|1958751236|ref|XP_038958468|]
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small ribosomal subunit protein mS27 isoform X1 [Rattus norvegicus]

Protein Classification

MRP-S27 domain-containing protein( domain architecture ID 12103126)

MRP-S27 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MRP-S27 pfam10037
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ...
34-346 7.60e-139

Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.


:

Pssm-ID: 462947 [Multi-domain]  Cd Length: 395  Bit Score: 399.89  E-value: 7.60e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  34 RFRHSPNCWYLRDWTIHTWIRQCLKYGAPDKALYTLVNKVQYGIFPDNFTFNLLMDYFIKKENYKDALSVVFEIMKQEAF 113
Cdd:pfam10037  93 KLRHSPNCWYLRDWTSHAWIRQCLKYGAPDKALYTLKNKVQYGIFPDNFTFNLLMDSFLKNGDYKSAASVVTELMLQEAF 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 114 EVPSTQFLSLYVLYHCLAE-----------------------------KTDLTWEEERDFGASLLLPGLKQRNTVGLSSQ 164
Cdd:pfam10037 173 DNPSTQLLSLYSCYKYLATpkdwvkepqpepdkeivkkrvpyirnpyfDDHFDWTEERNLGASLLLLGLKQDNSLGLSSQ 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 165 LYGYALLGKVelqcglravyhgmpliwtpGYLDRALQVMERVASSPEDVKLCREVLDVLDGVLKVVMspdgqasetqpqe 244
Cdd:pfam10037 253 LLGYALLGKV-------------------GYLDRALSVMEKVASSPGDLKLHKEVLDVLQDILETLD------------- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 245 gedslgsanlveqlDTEEPEQSRLPQYLERFQASRSKLQELNRVESESLLTLTTQLVKENLSACEAQDLATYEQKLREWH 324
Cdd:pfam10037 301 --------------ELEESEQSKLPEYVKSFQELLSKLQSLGKVESESLLTLLENLVKESLPACEEKDLANYEQLYQEWE 366
                         330       340
                  ....*....|....*....|..
gi 1958751236 325 QERMQLVQREQEQREKAKQEYQ 346
Cdd:pfam10037 367 EERRQLIQREKEMREKAEREDE 388
 
Name Accession Description Interval E-value
MRP-S27 pfam10037
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ...
34-346 7.60e-139

Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.


Pssm-ID: 462947 [Multi-domain]  Cd Length: 395  Bit Score: 399.89  E-value: 7.60e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  34 RFRHSPNCWYLRDWTIHTWIRQCLKYGAPDKALYTLVNKVQYGIFPDNFTFNLLMDYFIKKENYKDALSVVFEIMKQEAF 113
Cdd:pfam10037  93 KLRHSPNCWYLRDWTSHAWIRQCLKYGAPDKALYTLKNKVQYGIFPDNFTFNLLMDSFLKNGDYKSAASVVTELMLQEAF 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 114 EVPSTQFLSLYVLYHCLAE-----------------------------KTDLTWEEERDFGASLLLPGLKQRNTVGLSSQ 164
Cdd:pfam10037 173 DNPSTQLLSLYSCYKYLATpkdwvkepqpepdkeivkkrvpyirnpyfDDHFDWTEERNLGASLLLLGLKQDNSLGLSSQ 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 165 LYGYALLGKVelqcglravyhgmpliwtpGYLDRALQVMERVASSPEDVKLCREVLDVLDGVLKVVMspdgqasetqpqe 244
Cdd:pfam10037 253 LLGYALLGKV-------------------GYLDRALSVMEKVASSPGDLKLHKEVLDVLQDILETLD------------- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 245 gedslgsanlveqlDTEEPEQSRLPQYLERFQASRSKLQELNRVESESLLTLTTQLVKENLSACEAQDLATYEQKLREWH 324
Cdd:pfam10037 301 --------------ELEESEQSKLPEYVKSFQELLSKLQSLGKVESESLLTLLENLVKESLPACEEKDLANYEQLYQEWE 366
                         330       340
                  ....*....|....*....|..
gi 1958751236 325 QERMQLVQREQEQREKAKQEYQ 346
Cdd:pfam10037 367 EERRQLIQREKEMREKAEREDE 388
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
195-355 2.24e-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: 40.04  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  195 YLDRALQVMERVASSPEDVKLCREVLDVLDGVLkvvmspdgQASETQPQEGEDSLGSAN-----LVEQLDTEEPEQSRLP 269
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRskvaqLELQIASLNNEIERLE 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  270 QYLERFQASRSKLQELNRVESESLLTLTTQLVKENLSACEAQdlatyEQKLREWHQERMQLVQREQEQREKAKQEYQSLS 349
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE-----LEELQEELERLEEALEELREELEEAEQALDAAE 481

                   ....*.
gi 1958751236  350 AVENAA 355
Cdd:TIGR02168  482 RELAQL 487
 
Name Accession Description Interval E-value
MRP-S27 pfam10037
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ...
34-346 7.60e-139

Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.


Pssm-ID: 462947 [Multi-domain]  Cd Length: 395  Bit Score: 399.89  E-value: 7.60e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  34 RFRHSPNCWYLRDWTIHTWIRQCLKYGAPDKALYTLVNKVQYGIFPDNFTFNLLMDYFIKKENYKDALSVVFEIMKQEAF 113
Cdd:pfam10037  93 KLRHSPNCWYLRDWTSHAWIRQCLKYGAPDKALYTLKNKVQYGIFPDNFTFNLLMDSFLKNGDYKSAASVVTELMLQEAF 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 114 EVPSTQFLSLYVLYHCLAE-----------------------------KTDLTWEEERDFGASLLLPGLKQRNTVGLSSQ 164
Cdd:pfam10037 173 DNPSTQLLSLYSCYKYLATpkdwvkepqpepdkeivkkrvpyirnpyfDDHFDWTEERNLGASLLLLGLKQDNSLGLSSQ 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 165 LYGYALLGKVelqcglravyhgmpliwtpGYLDRALQVMERVASSPEDVKLCREVLDVLDGVLKVVMspdgqasetqpqe 244
Cdd:pfam10037 253 LLGYALLGKV-------------------GYLDRALSVMEKVASSPGDLKLHKEVLDVLQDILETLD------------- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236 245 gedslgsanlveqlDTEEPEQSRLPQYLERFQASRSKLQELNRVESESLLTLTTQLVKENLSACEAQDLATYEQKLREWH 324
Cdd:pfam10037 301 --------------ELEESEQSKLPEYVKSFQELLSKLQSLGKVESESLLTLLENLVKESLPACEEKDLANYEQLYQEWE 366
                         330       340
                  ....*....|....*....|..
gi 1958751236 325 QERMQLVQREQEQREKAKQEYQ 346
Cdd:pfam10037 367 EERRQLIQREKEMREKAEREDE 388
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
195-355 2.24e-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: 40.04  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  195 YLDRALQVMERVASSPEDVKLCREVLDVLDGVLkvvmspdgQASETQPQEGEDSLGSAN-----LVEQLDTEEPEQSRLP 269
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRskvaqLELQIASLNNEIERLE 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958751236  270 QYLERFQASRSKLQELNRVESESLLTLTTQLVKENLSACEAQdlatyEQKLREWHQERMQLVQREQEQREKAKQEYQSLS 349
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE-----LEELQEELERLEEALEELREELEEAEQALDAAE 481

                   ....*.
gi 1958751236  350 AVENAA 355
Cdd:TIGR02168  482 RELAQL 487
 
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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