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Conserved domains on  [gi|225690495|ref|NP_001139491|]
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tight junction-associated protein 1 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pilt super family cl21271
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 274-546 2.93e-61

Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight junction-proteins that binds to guanylate-kinase. Pilt is a component of TJs (Tight junctions) rather than AJs (Adhesin junctions). The protein is incorporated into TJs after TJ strands are formed, thereby suggesting the name Pilt for 'protein incorporated later into TJs'. Pilt binds to the guanylate-kinase region of hDlg otherwise known as Disk large homolog.


The actual alignment was detected with superfamily member pfam15453:

Pssm-ID: 464725  Cd Length: 362  Bit Score: 205.98  E-value: 2.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  274 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 352
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  353 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 408
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  409 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 454
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  455 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 508
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 225690495  509 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 546
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
PRK02224 super family cl32023
DNA double-strand break repair Rad50 ATPase;
17-153 3.22e-05

DNA double-strand break repair Rad50 ATPase;


The actual alignment was detected with superfamily member PRK02224:

Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  17 EHRELRLEIpgSRLEQE-----EPLTDAERmkllqeENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSR 85
Cdd:PRK02224 245 EHEERREEL--ETLEAEiedlrETIAETER------EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARR 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225690495  86 EELDKFKDKFR-RLQNSYTASQRTNQELE------DKLHTLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:PRK02224 317 EELEDRDEELRdRLEECRVAAQAHNEEAEslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 274-546 2.93e-61

Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight junction-proteins that binds to guanylate-kinase. Pilt is a component of TJs (Tight junctions) rather than AJs (Adhesin junctions). The protein is incorporated into TJs after TJ strands are formed, thereby suggesting the name Pilt for 'protein incorporated later into TJs'. Pilt binds to the guanylate-kinase region of hDlg otherwise known as Disk large homolog.


Pssm-ID: 464725  Cd Length: 362  Bit Score: 205.98  E-value: 2.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  274 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 352
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  353 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 408
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  409 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 454
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  455 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 508
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 225690495  509 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 546
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
17-153 3.22e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  17 EHRELRLEIpgSRLEQE-----EPLTDAERmkllqeENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSR 85
Cdd:PRK02224 245 EHEERREEL--ETLEAEiedlrETIAETER------EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARR 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225690495  86 EELDKFKDKFR-RLQNSYTASQRTNQELE------DKLHTLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:PRK02224 317 EELEDRDEELRdRLEECRVAAQAHNEEAEslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-159 1.96e-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: 44.28  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    50 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRK- 128
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLe 275

                           90       100       110
                   ....*....|....*....|....*....|...
gi 225690495   129 --TLDWEIVELTNKLLDAKNTINKLEELNERYR 159
Cdd:TIGR02168  276 vsELEEEIEELQKELYALANEISRLEQQKQILR 308
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-153 2.71e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  41 RMKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHT- 118
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLe 308

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 225690495 119 -LIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:COG1196  309 eRRRELEERLEELEEELAELEEELEELEEELEELEE 344
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 34-151 6.10e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   34 EPLTDAermkllQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 100
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225690495  101 sYTASQRT--------------NQELEDK---LHTLIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 151
Cdd:pfam13851 134 -QDVQQKTglknlllekklqalGETLEKKeaqLNEVLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 274-546 2.93e-61

Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight junction-proteins that binds to guanylate-kinase. Pilt is a component of TJs (Tight junctions) rather than AJs (Adhesin junctions). The protein is incorporated into TJs after TJ strands are formed, thereby suggesting the name Pilt for 'protein incorporated later into TJs'. Pilt binds to the guanylate-kinase region of hDlg otherwise known as Disk large homolog.


Pssm-ID: 464725  Cd Length: 362  Bit Score: 205.98  E-value: 2.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  274 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 352
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  353 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 408
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  409 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 454
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  455 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 508
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 225690495  509 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 546
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
17-153 3.22e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  17 EHRELRLEIpgSRLEQE-----EPLTDAERmkllqeENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSR 85
Cdd:PRK02224 245 EHEERREEL--ETLEAEiedlrETIAETER------EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARR 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225690495  86 EELDKFKDKFR-RLQNSYTASQRTNQELE------DKLHTLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:PRK02224 317 EELEDRDEELRdRLEECRVAAQAHNEEAEslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-158 4.55e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  17 EHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALEREL-EIGQDCLElELGQSREELDKFKDKF 95
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeELGFESVE-ELEERLKELEPFYNEY 604

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225690495  96 RRLQNSytasqrtNQELEDKLhtliKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNERY 158
Cdd:PRK03918 605 LELKDA-------EKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
15-159 1.25e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  15 PPEHRELRLEIPGSRLEQEEpltdaERMKLLQEENEELRRRLASATRRTEALERELEigqdclELELGQSREELDKFKDK 94
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREE-----KELKKLEEELDKAFEELAETEKRLEELRKELE------ELEKKYSEEEYEELREE 667

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225690495  95 FRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRKTLDwEIVELTNKLLDAKNTINKLEELNERYR 159
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVK 731
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-159 1.96e-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: 44.28  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    50 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRK- 128
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLe 275

                           90       100       110
                   ....*....|....*....|....*....|...
gi 225690495   129 --TLDWEIVELTNKLLDAKNTINKLEELNERYR 159
Cdd:TIGR02168  276 vsELEEEIEELQKELYALANEISRLEQQKQILR 308
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-153 2.71e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  41 RMKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHT- 118
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLe 308

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 225690495 119 -LIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:COG1196  309 eRRRELEERLEELEEELAELEEELEELEEELEELEE 344
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-157 2.89e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   43 KLLQEENEELRRRLASATRRTEAL-----ERELEIGQ---DCLELELGQSREELDKFKD----KFRRLQNSYTASQRTNQ 110
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLesekkEKESKISDledELNKDDFELKKENLEKEIDeknkEIEELKQTQKSLKKKQE 585

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 225690495  111 ELEDklhtLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNER 157
Cdd:TIGR04523 586 EKQE----LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-153 5.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   6 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL-----E 80
Cdd:COG4717   61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  81 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-----------IKKAEMDRKTLDWEIVELTNKLLDAKN 146
Cdd:COG4717  141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELleqlslateeeLQDLAEELEELQQRLAELEEELEEAQE 220


                 ....*..
gi 225690495 147 TINKLEE 153
Cdd:COG4717  221 ELEELEE 227
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 34-151 6.10e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   34 EPLTDAermkllQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 100
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225690495  101 sYTASQRT--------------NQELEDK---LHTLIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 151
Cdd:pfam13851 134 -QDVQQKTglknlllekklqalGETLEKKeaqLNEVLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
40-128 7.46e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  40 ERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLELELgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL 119
Cdd:COG2433  420 EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLDREIERLERELEEERERIEELKRKLERL 498


                 ....*....
gi 225690495 120 IKKAEMDRK 128
Cdd:COG2433  499 KELWKLEHS 507
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-158 1.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  17 EHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALE---RELEIGQDCLELELGQSRE------E 87
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEkvkelkE 287

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225690495  88 LDKFKDKFRRLQNSYTASQRTNQELEDKLHTLikkaEMDRKTLDWEIVELTNKLLDAKNTINKLEELNERY 158
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-152 1.69e-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: 41.21  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    11 YRKAPPEHRELRLEIPGsrLEQEEPLTDAERMKLLQEENEeLRRRLASATRRTEALERELEIgqdcLELELGQSREELDK 90
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG--LKRELSSLQSELRRIENRLDE-LSQELSDASRKIGEIEKEIEQ----LEQEEEKLKERLEE 741

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225690495    91 FKDKFRRLQnsytasqrtnQELEDklhtliKKAEMDRktLDWEIVELTNKLLDAKNTINKLE 152
Cdd:TIGR02169  742 LEEDLSSLE----------QEIEN------VKSELKE--LEARIEELEEDLHKLEEALNDLE 785
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-137 2.13e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   17 EHRELRLEIPGSRLEQeepltdaermklLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFR 96
Cdd:COG4913   327 ELEAQIRGNGGDRLEQ------------LEREIERLERELEERERRRARLEALLAA----LGLPLPASAEEFAALRAEAA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 225690495   97 RLQNSYTASQRTNQELEDKLHTLIKKAEMDRKTLDWEIVEL 137
Cdd:COG4913   391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 40-159 2.20e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.39  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   40 ERMKLLQEENEELR---RRLASATRRTEALERELEIgqDCLE------LELGQSREELDKFKDKFRRLQNSYTASQRTNQ 110
Cdd:pfam04849 171 EKLRGLEEENLKLRseaSHLKTETDTYEEKEQQLMS--DCVEqlseanQQMAELSEELARKMEENLRQQEEITSLLAQIV 248

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225690495  111 ELEDKLHTLIKKAEmdrktldweivELTNKLLDAKNTINKL----EELNERYR 159
Cdd:pfam04849 249 DLQHKCKELGIENE-----------ELQQHLQASKEAQRQLtselQELQDRYA 290
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-153 2.25e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   45 LQEENEELRRRLASATRRTEALERELEigqdclelelgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKlhtlIKKAE 124
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQ 418

                          90       100
                  ....*....|....*....|....*....
gi 225690495  125 MDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTN 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-124 3.06e-03

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: 40.13  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  39 AERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHT 118
Cdd:COG4942  152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231


                 ....*.
gi 225690495 119 LIKKAE 124
Cdd:COG4942  232 LEAEAA 237
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
40-153 3.12e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  40 ERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL---ELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKL 116
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 225690495 117 HTL---IKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:COG4372  118 EELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-178 5.83e-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: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    39 AERMKLLQEENEELRRRLASATRRTEALERELE---IGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDK 115
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225690495   116 LHTLIKKAEM---DRKTLDWEIVELTNKLLDAKNTINKLEELNERYRLDCNLAVQLLKCNKSHFRN 178
Cdd:TIGR02168  339 LAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 37-158 5.89e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  37 TDAERMKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELgqsREELDKFKDKFRRLQnsytasqrtnQELEDKL 116
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKEAEK----LKEEL---EEKKEKLQEEEDKLL----------EEAEKEA 575

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225690495 117 HTLIKKAemdRKTLDWEIVEL------TNKLLDAKNTINKLEELNERY 158
Cdd:PRK00409 576 QQAIKEA---KKEADEIIKELrqlqkgGYASVKAHELIEARKRLNKAN 620
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 39-153 7.21e-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: 38.37  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495  39 AERMKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNSYtASQRTNQELEDKLHT 118
Cdd:COG1579   23 EHRLKELPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYEALQKE 97

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 225690495 119 lIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:COG1579   98 -IESLKRRISDLEDEILELMERIEELEEELAELEA 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-157 9.26e-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: 38.88  E-value: 9.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    22 RLEIPGSRLEQEEPLTDAERMKLLQEEnEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS 101
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEI-EELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 225690495   102 YTASQRTNQELEDKLHTLIKKAEMDRKTLDW---EIVELTNKLLDAKNTINKLEELNER 157
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDleeQIEELSEDIESLAAEIEELEELIEE 870
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 43-159 9.40e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 36.39  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495   43 KLLQEENEELRRRLASATRRTEALEREleigqdclELELGQSREELDKFKdkfrrlqnsytasqrtnQELEDKLHTLIKK 122
Cdd:pfam13863  13 LALDAKREEIERLEELLKQREEELEKK--------EQELKEDLIKFDKFL-----------------KENDAKRRRALKK 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 225690495  123 AEMDRK---TLDWEIVELTNKLLDAKNTINKLEELNERYR 159
Cdd:pfam13863  68 AEEETKlkkEKEKEIKKLTAQIEELKSEISKLEEKLEEYK 107
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-153 9.57e-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: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225690495    11 YRKAPPEHRELRLEIPGSRLE----QEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELE----------IGQDC 76
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkreinelkRELDR 410

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225690495    77 LELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKlhtlIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 153
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE----IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
 
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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