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Conserved domains on  [gi|1063694861|ref|NP_001322454|]
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coiled-coil protein [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing 22 family protein( domain architecture ID 708562)

coiled-coil domain-containing 22 (CCDC22) family protein is a DUF812 domain-containing protein that may be involved in regulation of NF-kappa-B signaling

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CCDC22 super family cl25503
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
103-343 2.12e-28

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 116.28  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 103 QHDVLLEELESGSSQLcslESELELLQMAAERLLDDKKPggsyLEQLNQQLVVKRCNIMDLKKQWDDVRLTLETKKLLLL 182
Cdd:pfam05667 367 QVEEELEELKEQNEEL---EKQYKVKKKTLDLLPDAEEN----IAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALK 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 183 DQLHVEEPEAKEKFHKLRKTELDLQSLSSEIQKREDERCNLYNELERQPKAAPRKSYIHGIKEITKNSRKLDTDIQRISG 262
Cdd:pfam05667 440 EAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILS 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 263 ETRELQLEKNSIQERLHRSYAVVDEMVTREVKKDPAVRQVYKLLTSIHSIFEQISEKILMTDRFRRETVDYEKKLGSITA 342
Cdd:pfam05667 520 DTKSLQKEINSLTGKLDRTFTVTDELVFKDAKKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESG 599

                  .
gi 1063694861 343 R 343
Cdd:pfam05667 600 K 600
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
103-343 2.12e-28

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 116.28  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 103 QHDVLLEELESGSSQLcslESELELLQMAAERLLDDKKPggsyLEQLNQQLVVKRCNIMDLKKQWDDVRLTLETKKLLLL 182
Cdd:pfam05667 367 QVEEELEELKEQNEEL---EKQYKVKKKTLDLLPDAEEN----IAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALK 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 183 DQLHVEEPEAKEKFHKLRKTELDLQSLSSEIQKREDERCNLYNELERQPKAAPRKSYIHGIKEITKNSRKLDTDIQRISG 262
Cdd:pfam05667 440 EAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILS 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 263 ETRELQLEKNSIQERLHRSYAVVDEMVTREVKKDPAVRQVYKLLTSIHSIFEQISEKILMTDRFRRETVDYEKKLGSITA 342
Cdd:pfam05667 520 DTKSLQKEINSLTGKLDRTFTVTDELVFKDAKKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESG 599

                  .
gi 1063694861 343 R 343
Cdd:pfam05667 600 K 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-355 2.81e-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: 39.65  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861   92 ETNYETVELQNQHDVLLEELESGSSQLCSLESELELLQMAAERLLDDKKPGGSYLEQLNQQLVVKRCNIMDLKKQwddvr 171
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK----- 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861  172 ltletkklllLDQLHVEEPEAKEKFHKLRKTELDLQSLSSEIQKREDERCNLYNELERQpkaaprksyihgIKEITKNSR 251
Cdd:TIGR02168  346 ----------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------------IASLNNEIE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861  252 KLDTDIQRISGETRELQLEKNSIQERLHRsyAVVDEMVTREVKKDPAVRQVYKLLTSIHSIFEQISEKIlmtDRFRRETV 331
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREEL---EEAEQALD 478
                          250       260
                   ....*....|....*....|....
gi 1063694861  332 DYEKKLGSITARGMSLEKLQADLD 355
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLE 502
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
103-343 2.12e-28

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 116.28  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 103 QHDVLLEELESGSSQLcslESELELLQMAAERLLDDKKPggsyLEQLNQQLVVKRCNIMDLKKQWDDVRLTLETKKLLLL 182
Cdd:pfam05667 367 QVEEELEELKEQNEEL---EKQYKVKKKTLDLLPDAEEN----IAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALK 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 183 DQLHVEEPEAKEKFHKLRKTELDLQSLSSEIQKREDERCNLYNELERQPKAAPRKSYIHGIKEITKNSRKLDTDIQRISG 262
Cdd:pfam05667 440 EAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILS 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861 263 ETRELQLEKNSIQERLHRSYAVVDEMVTREVKKDPAVRQVYKLLTSIHSIFEQISEKILMTDRFRRETVDYEKKLGSITA 342
Cdd:pfam05667 520 DTKSLQKEINSLTGKLDRTFTVTDELVFKDAKKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESG 599

                  .
gi 1063694861 343 R 343
Cdd:pfam05667 600 K 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-355 2.81e-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: 39.65  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861   92 ETNYETVELQNQHDVLLEELESGSSQLCSLESELELLQMAAERLLDDKKPGGSYLEQLNQQLVVKRCNIMDLKKQwddvr 171
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK----- 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861  172 ltletkklllLDQLHVEEPEAKEKFHKLRKTELDLQSLSSEIQKREDERCNLYNELERQpkaaprksyihgIKEITKNSR 251
Cdd:TIGR02168  346 ----------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------------IASLNNEIE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694861  252 KLDTDIQRISGETRELQLEKNSIQERLHRsyAVVDEMVTREVKKDPAVRQVYKLLTSIHSIFEQISEKIlmtDRFRRETV 331
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREEL---EEAEQALD 478
                          250       260
                   ....*....|....*....|....
gi 1063694861  332 DYEKKLGSITARGMSLEKLQADLD 355
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLE 502
 
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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