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Conserved domains on  [gi|1182921667|ref|NP_001337494|]
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tight junction-associated protein 1 isoform a [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 ...
 284-556 2.27e-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: 206.36  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 284 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 362
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 363 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 418
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 419 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 464
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 465 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 518
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1182921667 519 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 556
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-163 1.19e-05

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   6 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL-----E 80
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  81 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 156
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1182921667 157 TINKLEE 163
Cdd:COG4717   221 ELEELEE 227
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 284-556 2.27e-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: 206.36  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 284 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 362
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 363 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 418
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 419 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 464
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 465 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 518
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1182921667 519 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 556
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-163 1.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   6 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL-----E 80
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  81 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 156
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1182921667 157 TINKLEE 163
Cdd:COG4717   221 ELEELEE 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-168 1.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  17 EHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALE---RELEIGQDCLELELGQSRE------E 87
Cdd:PRK03918  208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEkvkelkE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  88 LDKFKDKFRRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKtldwEIVELTNKLLDAKNTINKLEELNER 167
Cdd:PRK03918  288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHEL 363


                  .
gi 1182921667 168 Y 168
Cdd:PRK03918  364 Y 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-169 2.88e-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: 43.89  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   50 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL-ASLShswIF 128
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeEKLE---EL 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1182921667  129 AIKKAEMDRktldwEIVELTNKLLDAKNTINKLEELNERYR 169
Cdd:TIGR02168  273 RLEVSELEE-----EIEELQKELYALANEISRLEQQKQILR 308
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 34-161 2.96e-03

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: 39.12  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  34 EPLTDAermkllQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 100
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182921667 101 sYTASQRT---NQELEDKLHTL--------ASLSHswifAIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 161
Cdd:pfam13851 134 -QDVQQKTglkNLLLEKKLQALgetlekkeAQLNE----VLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 284-556 2.27e-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: 206.36  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 284 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 362
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 363 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 418
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 419 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 464
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667 465 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 518
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1182921667 519 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 556
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-163 1.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   6 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL-----E 80
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  81 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 156
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1182921667 157 TINKLEE 163
Cdd:COG4717   221 ELEELEE 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-168 1.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  17 EHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALE---RELEIGQDCLELELGQSRE------E 87
Cdd:PRK03918  208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEkvkelkE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  88 LDKFKDKFRRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKtldwEIVELTNKLLDAKNTINKLEELNER 167
Cdd:PRK03918  288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHEL 363


                  .
gi 1182921667 168 Y 168
Cdd:PRK03918  364 Y 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-169 2.88e-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: 43.89  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   50 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL-ASLShswIF 128
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeEKLE---EL 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1182921667  129 AIKKAEMDRktldwEIVELTNKLLDAKNTINKLEELNERYR 169
Cdd:TIGR02168  273 RLEVSELEE-----EIEELQKELYALANEISRLEQQKQILR 308
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-168 3.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  17 EHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALEREL-EIGQDCLElELGQSREELDKFKDKF 95
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeELGFESVE-ELEERLKELEPFYNEY 604

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182921667  96 RRLQNSytasqrtNQELEDKLHTLASLshswifaikkaemdRKTLDWEIVELTNKLLDAKNTINKLEELNERY 168
Cdd:PRK03918  605 LELKDA-------EKELEREEKELKKL--------------EEELDKAFEELAETEKRLEELRKELEELEKKY 656
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
17-163 7.25e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  17 EHRELRLEIpgSRLEQE-----EPLTDAERmkllqeENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSR 85
Cdd:PRK02224  245 EHEERREEL--ETLEAEiedlrETIAETER------EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  86 EELDKFKDKFR-RLQNSYTASQRTNQELE---DKLHTLASLShswifaiKKAEMDRKTLDWEIVELTNKLLDAKNTINKL 161
Cdd:PRK02224  317 EELEDRDEELRdRLEECRVAAQAHNEEAEslrEDADDLEERA-------EELREEAAELESELEEAREAVEDRREEIEEL 389


                  ..
gi 1182921667 162 EE 163
Cdd:PRK02224  390 EE 391
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
40-116 1.08e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1182921667  40 ERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLELELgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKL 116
Cdd:COG2433   420 EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLDREIERLERELEEERERIEELKRKL 495
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 17-204 1.17e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   17 EHRELRLEIPGSRLEQEEP-LTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQdcLELELGQSREELDKFKDKF 95
Cdd:TIGR00606  768 EEQETLLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKI 845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   96 RRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKA---EMDRKTLDWEIVELTNKLLDAKNTINKLEELNERYRLDC 172
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1182921667  173 NLAVqllkcNKSHFRNHKFADlpcELQDMVRK 204
Cdd:TIGR00606  926 EELI-----SSKETSNKKAQD---KVNDIKEK 949
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
15-169 1.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  15 PPEHRELRLEIPGSRLEQEEpltdaERMKLLQEENEELRRRLASATRRTEALERELEigqdclELELGQSREELDKFKDK 94
Cdd:PRK03918  599 PFYNEYLELKDAEKELEREE-----KELKKLEEELDKAFEELAETEKRLEELRKELE------ELEKKYSEEEYEELREE 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182921667  95 FRRLQNSYTASQRTNQELEDKLHTLASLshswifaIKKAEMDRKtldwEIVELTNKLLDAKNTINKLEELNERYR 169
Cdd:PRK03918  668 YLELSRELAGLRAELEELEKRREEIKKT-------LEKLKEELE----EREKAKKELEKLEKALERVEELREKVK 731
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-163 1.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  41 RMKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHTL 119
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLE 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1182921667 120 ASLSHswifaikkAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 163
Cdd:COG1196   309 ERRRE--------LEERLEELEEELAELEEELEELEEELEELEE 344
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-163 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   11 YRKAPPEHRELRLEIPGSRLE----QEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDclelELGQSRE 86
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR----EINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   87 ELDKFKDKFRRLQnsyTASQRTNQEL---EDKLHTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 163
Cdd:TIGR02169  407 ELDRLQEELQRLS---EELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
40-163 2.10e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  40 ERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL---ELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKL 116
Cdd:COG4372    38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1182921667 117 HTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 163
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-175 2.54e-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: 40.81  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   22 RLEIPGSRLEQEEPLTDAERMKLLQEEnEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS 101
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEI-EELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182921667  102 YTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE-----LNERYRLDCNLA 175
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESelealLNERASLEEALA 890
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 34-161 2.96e-03

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: 39.12  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  34 EPLTDAermkllQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 100
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1182921667 101 sYTASQRT---NQELEDKLHTL--------ASLSHswifAIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 161
Cdd:pfam13851 134 -QDVQQKTglkNLLLEKKLQALgetlekkeAQLNE----VLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-167 5.50e-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: 39.62  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  43 KLLQEENEELRRRLASATRRTEAL-----ERELEIGQ---DCLELELGQSREELDKFKD----KFRRLQNSYTASQRTNQ 110
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLesekkEKESKISDledELNKDDFELKKENLEKEIDeknkEIEELKQTQKSLKKKQE 585

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1182921667 111 ELEDKlhtlaslshswifaIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNER 167
Cdd:TIGR04523 586 EKQEL--------------IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-166 6.03e-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: 39.67  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   11 YRKAPPEHRELRLEIPGsrLEQEEPLTDAERMKLLQEENEeLRRRLASATRRTEALERELEIgqdcLELELGQSREELDK 90
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG--LKRELSSLQSELRRIENRLDE-LSQELSDASRKIGEIEKEIEQ----LEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667   91 FKDKFRRLQNSYTASQRTNQEL-------EDKLHTL--------ASLSHSwIFAIKKAEMDRktLDWEIVELTNKLLDAK 155
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELearieelEEDLHKLeealndleARLSHS-RIPEIQAELSK--LEEEVSRIEARLREIE 818

                          170
                   ....*....|.
gi 1182921667  156 NTINKLEELNE 166
Cdd:TIGR02169  819 QKLNRLTLEKE 829
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 40-121 6.65e-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: 38.85  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  40 ERMKLLQEENEELR---RRLASATRRTEALERELEIgqDCLE------LELGQSREELDKFKDKFRRLQNSYTASQRTNQ 110
Cdd:pfam04849 171 EKLRGLEEENLKLRseaSHLKTETDTYEEKEQQLMS--DCVEqlseanQQMAELSEELARKMEENLRQQEEITSLLAQIV 248

                          90
                  ....*....|.
gi 1182921667 111 ELEDKLHTLAS 121
Cdd:pfam04849 249 DLQHKCKELGI 259
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 17-169 9.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182921667  17 EHRELRLEIpgSRLEQEEPLTDAERMKLLQEEN--EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDK 94
Cdd:COG1196   275 ELEELELEL--EEAQAEEYELLAELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1182921667  95 FRRLQNSYTASQRTNQELEDKLHTLASLshswIFAIKKAEMDRKTldwEIVELTNKLLDAKNTINKLEELNERYR 169
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALR---AAAELAAQLEELEEAEEALLERLERLE 420
 
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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