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Conserved domains on  [gi|564398786|ref|XP_006256825|]
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protein Shroom4 isoform X2 [Rattus norvegicus]

Protein Classification

ASD2 domain-containing protein( domain architecture ID 10554662)

ASD2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1132-1364 6.90e-110

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


:

Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 348.09  E-value: 6.90e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1132 KQEFQHFSPPTGASGIPTSYSAYYNISVAKAELLNKLKQQPEMAEA----GLGEEGVDYELAQKKIQLIESISRKLSVLR 1207
Cdd:pfam08687   53 APSEEGSEEEASGTSSLSSCSAYYTTSAPKAELLTKMKDLTTLPSPdqpeEQGEEELDNDLQQKKVELIESLQRKLQVLR 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1208 EAQRGLLDDINANAALGEEVEVNLKAVCKSNELEKYHLFIGDLDKVVNLLLSLSGRLARVENALNSIDAESNQ-EKLVLR 1286
Cdd:pfam08687  133 EEQEALQEEIQANAALGAEVEALVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAeERQSLL 212
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398786  1287 EKKQQLTNQLADAKELKEHVDRREKLVFSMVSRYLPQDQLQDYQHFVKMKSALIIEQRELEEKIKLGEEQLKCLKESL 1364
Cdd:pfam08687  213 EKRRLLLRQLEDAKELKENLDRRERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1132-1364 6.90e-110

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 348.09  E-value: 6.90e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1132 KQEFQHFSPPTGASGIPTSYSAYYNISVAKAELLNKLKQQPEMAEA----GLGEEGVDYELAQKKIQLIESISRKLSVLR 1207
Cdd:pfam08687   53 APSEEGSEEEASGTSSLSSCSAYYTTSAPKAELLTKMKDLTTLPSPdqpeEQGEEELDNDLQQKKVELIESLQRKLQVLR 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1208 EAQRGLLDDINANAALGEEVEVNLKAVCKSNELEKYHLFIGDLDKVVNLLLSLSGRLARVENALNSIDAESNQ-EKLVLR 1286
Cdd:pfam08687  133 EEQEALQEEIQANAALGAEVEALVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAeERQSLL 212
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398786  1287 EKKQQLTNQLADAKELKEHVDRREKLVFSMVSRYLPQDQLQDYQHFVKMKSALIIEQRELEEKIKLGEEQLKCLKESL 1364
Cdd:pfam08687  213 EKRRLLLRQLEDAKELKENLDRRERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1163-1364 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1163 ELLNKLKQQPEMAEAGLGEEGVDYELAQKKIQLIESISRKLSVLREAQRGLLDDINanaALGEEVEVNLKAVCKSNELEK 1242
Cdd:PRK03918  300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELER 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1243 YHLFIGDL--DKVVNLLLSLSGRLARVENALNSIDAESNQEKLVLREKKQQLtNQLADAK--------ELKEHvDRREkl 1312
Cdd:PRK03918  377 LKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKgkcpvcgrELTEE-HRKE-- 452
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398786 1313 vfsMVSRYLPQ--DQLQDYQHFVKMKSALIIEQRELEEKIKLGE---------EQLKCLKESL 1364
Cdd:PRK03918  453 ---LLEEYTAElkRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKELEEKL 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1160-1365 1.04e-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: 43.51  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1160 AKAELLNKLKQQPEMAEAGLGEEGVDYELAQKKIQ----LIESISRKLSVLREAQRGLLDDINANAALGEEVEVNLKAVC 1235
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1236 K-----SNELEKYHLFIGDLDKVVNLLLSLSGRLA-RVENALNSIDA------ESNQEKLVLREKKQQLTNQLADA---- 1299
Cdd:TIGR02168  789 AqieqlKEELKALREALDELRAELTLLNEEAANLReRLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELeeli 868
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1300 ----KELKEHVDRREKLVFSMVSRYLPQDQLQDyqhfvkmksaliiEQRELEEKIKLGEEQLKCLKESLH 1365
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSE-------------ELRELESKRSELRRELEELREKLA 925
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1193-1364 9.52e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1193 IQLIESISRKLSVLREAQRGLLDDINANAALGEEVEvNLKAVCKS--NELEKYHLFIGDLDkVVNLLLSLSGRLARVENA 1270
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEElrEELEKLEKLLQLLP-LYQELEALEAELAELPER 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1271 LNSIDaesnQEKLVLREKKQQLTNQLADAKELKEHVDRREKLVFSMVSRYLpQDQLQDYQHFVKMKSALIIEQRELEEKI 1350
Cdd:COG4717   148 LEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEEL 222
                         170
                  ....*....|....
gi 564398786 1351 KLGEEQLKCLKESL 1364
Cdd:COG4717   223 EELEEELEQLENEL 236
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1132-1364 6.90e-110

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 348.09  E-value: 6.90e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1132 KQEFQHFSPPTGASGIPTSYSAYYNISVAKAELLNKLKQQPEMAEA----GLGEEGVDYELAQKKIQLIESISRKLSVLR 1207
Cdd:pfam08687   53 APSEEGSEEEASGTSSLSSCSAYYTTSAPKAELLTKMKDLTTLPSPdqpeEQGEEELDNDLQQKKVELIESLQRKLQVLR 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1208 EAQRGLLDDINANAALGEEVEVNLKAVCKSNELEKYHLFIGDLDKVVNLLLSLSGRLARVENALNSIDAESNQ-EKLVLR 1286
Cdd:pfam08687  133 EEQEALQEEIQANAALGAEVEALVQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAeERQSLL 212
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398786  1287 EKKQQLTNQLADAKELKEHVDRREKLVFSMVSRYLPQDQLQDYQHFVKMKSALIIEQRELEEKIKLGEEQLKCLKESL 1364
Cdd:pfam08687  213 EKRRLLLRQLEDAKELKENLDRRERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1163-1364 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1163 ELLNKLKQQPEMAEAGLGEEGVDYELAQKKIQLIESISRKLSVLREAQRGLLDDINanaALGEEVEVNLKAVCKSNELEK 1242
Cdd:PRK03918  300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELER 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1243 YHLFIGDL--DKVVNLLLSLSGRLARVENALNSIDAESNQEKLVLREKKQQLtNQLADAK--------ELKEHvDRREkl 1312
Cdd:PRK03918  377 LKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKgkcpvcgrELTEE-HRKE-- 452
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398786 1313 vfsMVSRYLPQ--DQLQDYQHFVKMKSALIIEQRELEEKIKLGE---------EQLKCLKESL 1364
Cdd:PRK03918  453 ---LLEEYTAElkRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaEQLKELEEKL 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1160-1365 1.04e-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: 43.51  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1160 AKAELLNKLKQQPEMAEAGLGEEGVDYELAQKKIQ----LIESISRKLSVLREAQRGLLDDINANAALGEEVEVNLKAVC 1235
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1236 K-----SNELEKYHLFIGDLDKVVNLLLSLSGRLA-RVENALNSIDA------ESNQEKLVLREKKQQLTNQLADA---- 1299
Cdd:TIGR02168  789 AqieqlKEELKALREALDELRAELTLLNEEAANLReRLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELeeli 868
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1300 ----KELKEHVDRREKLVFSMVSRYLPQDQLQDyqhfvkmksaliiEQRELEEKIKLGEEQLKCLKESLH 1365
Cdd:TIGR02168  869 eeleSELEALLNERASLEEALALLRSELEELSE-------------ELRELESKRSELRRELEELREKLA 925
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1173-1358 3.71e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1173 EMAEAGLGEEGvdYELAQKKIQLIESISRKLSVLREAQRGLLD-DINANAAL--------GEEVEVNLKAVCKSNELEKY 1243
Cdd:pfam02463  161 EAAGSRLKRKK--KEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALeyyqlkekLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786  1244 -HLFIGDLDKVVNLLLSLSGRLarvENALNSIDAESNQEKLVLREKKQQLTNQLADAKELKE-----------HVDRREK 1311
Cdd:pfam02463  239 iDLLQELLRDEQEEIESSKQEI---EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElksellklerrKVDDEEK 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564398786  1312 LVFSMVSRYLPQDQLQDYQHFV-----KMKSALIIEQRELEEKIKLGEEQLK 1358
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIeelekELKELEIKREAEEEEEEELEKLQEK 367
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1193-1364 9.52e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1193 IQLIESISRKLSVLREAQRGLLDDINANAALGEEVEvNLKAVCKS--NELEKYHLFIGDLDkVVNLLLSLSGRLARVENA 1270
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEElrEELEKLEKLLQLLP-LYQELEALEAELAELPER 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398786 1271 LNSIDaesnQEKLVLREKKQQLTNQLADAKELKEHVDRREKLVFSMVSRYLpQDQLQDYQHFVKMKSALIIEQRELEEKI 1350
Cdd:COG4717   148 LEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEEL 222
                         170
                  ....*....|....
gi 564398786 1351 KLGEEQLKCLKESL 1364
Cdd:COG4717   223 EELEEELEQLENEL 236
 
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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