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Conserved domains on  [gi|1063725340|ref|NP_001328544|]
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intracellular protein transporter [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
100-257 4.90e-06

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: 47.07  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 100 SESGSDIFSKREVIQKLRQQLKRRDDMIVEMQEQILELQNSLNAqmghsshIQTQLDATNRDLFESEREVQRLRKAIADH 179
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 180 cVGHTGSNGWSGDVNSENNYESPENGIR-----------DGERIEMLRKEVGELKEVIDgkeyLLRSYKEQKTELLQKVK 248
Cdd:COG4942   110 -LRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELAALRA----ELEAERAELEALLAELE 184

                  ....*....
gi 1063725340 249 ELQQRLDSQ 257
Cdd:COG4942   185 EERAALEAL 193
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
100-257 4.90e-06

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: 47.07  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 100 SESGSDIFSKREVIQKLRQQLKRRDDMIVEMQEQILELQNSLNAqmghsshIQTQLDATNRDLFESEREVQRLRKAIADH 179
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 180 cVGHTGSNGWSGDVNSENNYESPENGIR-----------DGERIEMLRKEVGELKEVIDgkeyLLRSYKEQKTELLQKVK 248
Cdd:COG4942   110 -LRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELAALRA----ELEAERAELEALLAELE 184

                  ....*....
gi 1063725340 249 ELQQRLDSQ 257
Cdd:COG4942   185 EERAALEAL 193
PRK09039 PRK09039
peptidoglycan -binding protein;
116-252 3.06e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 116 LRQQLKRRDDMIVEMQEQILELQNSLNAQMGHSSHIQTQLDATNRDLFESEREVQRLRKAIADHCVGHTGSNGWSGDVNS 195
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063725340 196 ENNYESPEnGIRDGERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTE---------------LLQKVKELQQ 252
Cdd:PRK09039  124 ELDSEKQV-SARALAQVELLNQQIAALRRQLAALEAALDASEKRDREsqakiadlgrrlnvaLAQRVQELNR 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-255 2.32e-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: 39.27  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340  106 IFSKREVIQKLRQQLKrrddmivEMQEQILELQNSLNAQMGHSSHIQTQLDATNRDLFESEREVQRLRKAIAdhcvghtg 185
Cdd:TIGR02168  672 ILERRREIEELEEKIE-------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------- 736
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340  186 sngwsgdvNSENNYESPEngirdgERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTELLQKVKELQQRLD 255
Cdd:TIGR02168  737 --------RLEAEVEQLE------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
100-257 4.90e-06

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: 47.07  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 100 SESGSDIFSKREVIQKLRQQLKRRDDMIVEMQEQILELQNSLNAqmghsshIQTQLDATNRDLFESEREVQRLRKAIADH 179
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 180 cVGHTGSNGWSGDVNSENNYESPENGIR-----------DGERIEMLRKEVGELKEVIDgkeyLLRSYKEQKTELLQKVK 248
Cdd:COG4942   110 -LRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELAALRA----ELEAERAELEALLAELE 184

                  ....*....
gi 1063725340 249 ELQQRLDSQ 257
Cdd:COG4942   185 EERAALEAL 193
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
104-257 9.32e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 104 SDIFSKREVIQKLRQQLKRRDDMIVEMQEQILELQNSLNAQMGHSSHIQTQLDATNRDLFESEREVQRLRKAIADHCVG- 182
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAl 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063725340 183 -HTGSNGWSGDV--NSEnnyeSPENGIrdgERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTELLQKVKELQQRLDSQ 257
Cdd:COG3883    96 yRSGGSVSYLDVllGSE----SFSDFL---DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
PRK09039 PRK09039
peptidoglycan -binding protein;
116-252 3.06e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 116 LRQQLKRRDDMIVEMQEQILELQNSLNAQMGHSSHIQTQLDATNRDLFESEREVQRLRKAIADHCVGHTGSNGWSGDVNS 195
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063725340 196 ENNYESPEnGIRDGERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTE---------------LLQKVKELQQ 252
Cdd:PRK09039  124 ELDSEKQV-SARALAQVELLNQQIAALRRQLAALEAALDASEKRDREsqakiadlgrrlnvaLAQRVQELNR 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-255 2.32e-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: 39.27  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340  106 IFSKREVIQKLRQQLKrrddmivEMQEQILELQNSLNAQMGHSSHIQTQLDATNRDLFESEREVQRLRKAIAdhcvghtg 185
Cdd:TIGR02168  672 ILERRREIEELEEKIE-------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------- 736
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340  186 sngwsgdvNSENNYESPEngirdgERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTELLQKVKELQQRLD 255
Cdd:TIGR02168  737 --------RLEAEVEQLE------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
113-257 4.81e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063725340 113 IQKLRQQLKRRDDMIVEMQEQILELQNSLNAqmghsshIQTQLDATNRDLFESEREVQRLRKAIADhcvghtgsngwsgd 192
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEA-------AKTELEDLEKEIKRLELEIEEVEARIKK-------------- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063725340 193 vnsennYESPENGIRDGERIEMLRKEVGELKEVIDGKEYLLRSYKEQKTELLQKVKELQQRLDSQ 257
Cdd:COG1579    78 ------YEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
 
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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