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Conserved domains on  [gi|1622933589|ref|XP_028703357|]
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tight junction-associated protein 1 isoform X1 [Macaca mulatta]

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 ...
 288-559 8.48e-62

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: 207.90  E-value: 8.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 288 QPNGECHSLGTARGSPEEelpLPAFEKLSPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSLV- 365
Cdd:pfam15453  15 QQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSLVq 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 366 --EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPPTLSAPASSassEEDLLASWQRAFVD 422
Cdd:pfam15453  92 neDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMFVE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 423 RTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPS----------------------- 463
Cdd:pfam15453 169 KMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSwtpsrgssldtdttdslrarrsh 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 464 -----PRPEESELLLPIEPD------------SGFPREEEEELNLPISPEEERQSLLPINSGTGEGS-GTSHTEGRAWPL 525
Cdd:pfam15453 249 ygtdfSEEEGEKLLMAADEEgaagdasvpvesSPKKHKDYVDLGSPGSSAEERDVLLQDLPVISSRVlGELSDEADKDPA 328

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622933589 526 PSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 559
Cdd:pfam15453 329 APSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-165 9.53e-06

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: 48.61  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   8 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALERELEIGQDCLEL-----E 82
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  83 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 158
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1622933589 159 TINKLEE 165
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 ...
 288-559 8.48e-62

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: 207.90  E-value: 8.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 288 QPNGECHSLGTARGSPEEelpLPAFEKLSPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSLV- 365
Cdd:pfam15453  15 QQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSLVq 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 366 --EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPPTLSAPASSassEEDLLASWQRAFVD 422
Cdd:pfam15453  92 neDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMFVE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 423 RTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPS----------------------- 463
Cdd:pfam15453 169 KMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSwtpsrgssldtdttdslrarrsh 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 464 -----PRPEESELLLPIEPD------------SGFPREEEEELNLPISPEEERQSLLPINSGTGEGS-GTSHTEGRAWPL 525
Cdd:pfam15453 249 ygtdfSEEEGEKLLMAADEEgaagdasvpvesSPKKHKDYVDLGSPGSSAEERDVLLQDLPVISSRVlGELSDEADKDPA 328

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622933589 526 PSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 559
Cdd:pfam15453 329 APSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-165 9.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   8 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALERELEIGQDCLEL-----E 82
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  83 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 158
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1622933589 159 TINKLEE 165
Cdd:COG4717   221 ELEELEE 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-170 2.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  19 EHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALEREL-EIGQDCLElELGQSREELDKFKDKF 97
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeELGFESVE-ELEERLKELEPFYNEY 604

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622933589  98 RRLQNSytasqrtNQELEDKLHTLASLshswifaikkaemdRKTLDWEIVELTNKLLDAKNTINKLEELNERY 170
Cdd:PRK03918  605 LELKDA-------EKELEREEKELKKL--------------EEELDKAFEELAETEKRLEELRKELEELEKKY 656
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-171 2.30e-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: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   52 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL-ASLShswIF 130
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeEKLE---EL 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622933589  131 AIKKAEMDRktldwEIVELTNKLLDAKNTINKLEELNERYR 171
Cdd:TIGR02168  273 RLEVSELEE-----EIEELQKELYALANEISRLEQQKQILR 308
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 36-163 1.87e-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: 39.89  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  36 EPLTDAermkllQQENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 102
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622933589 103 sYTASQRT---NQELEDKLHTL--------ASLSHswifAIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 163
Cdd:pfam13851 134 -QDVQQKTglkNLLLEKKLQALgetlekkeAQLNE----VLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 370-495 8.44e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  370 ERARPSPVPSTPASAQASPHHQPSPAPPTLSAPASSASSEEDLLASWQRAFVDRTPPPAAVAQRTAFGRDALPELQRHFA 449
Cdd:PRK10263   378 EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA 457

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622933589  450 HSP-ADRDEVVQAPSPRPEESELLLPIEPDSGFPREEEEELNLPISP 495
Cdd:PRK10263   458 PQStYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARP 504
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 288-559 8.48e-62

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: 207.90  E-value: 8.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 288 QPNGECHSLGTARGSPEEelpLPAFEKLSPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSLV- 365
Cdd:pfam15453  15 QQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSLVq 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 366 --EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPPTLSAPASSassEEDLLASWQRAFVD 422
Cdd:pfam15453  92 neDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMFVE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 423 RTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPS----------------------- 463
Cdd:pfam15453 169 KMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSwtpsrgssldtdttdslrarrsh 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 464 -----PRPEESELLLPIEPD------------SGFPREEEEELNLPISPEEERQSLLPINSGTGEGS-GTSHTEGRAWPL 525
Cdd:pfam15453 249 ygtdfSEEEGEKLLMAADEEgaagdasvpvesSPKKHKDYVDLGSPGSSAEERDVLLQDLPVISSRVlGELSDEADKDPA 328

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622933589 526 PSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 559
Cdd:pfam15453 329 APSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-165 9.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   8 PAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALERELEIGQDCLEL-----E 82
Cdd:COG4717    61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  83 LGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKLHTL-ASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKN 158
Cdd:COG4717   141 LAELPERLEELEERleeLRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220


                  ....*..
gi 1622933589 159 TINKLEE 165
Cdd:COG4717   221 ELEELEE 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-170 2.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  19 EHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALEREL-EIGQDCLElELGQSREELDKFKDKF 97
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeELGFESVE-ELEERLKELEPFYNEY 604

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622933589  98 RRLQNSytasqrtNQELEDKLHTLASLshswifaikkaemdRKTLDWEIVELTNKLLDAKNTINKLEELNERY 170
Cdd:PRK03918  605 LELKDA-------EKELEREEKELKKL--------------EEELDKAFEELAETEKRLEELRKELEELEKKY 656
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-171 2.30e-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: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   52 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL-ASLShswIF 130
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeEKLE---EL 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622933589  131 AIKKAEMDRktldwEIVELTNKLLDAKNTINKLEELNERYR 171
Cdd:TIGR02168  273 RLEVSELEE-----EIEELQKELYALANEISRLEQQKQILR 308
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-170 2.95e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  19 EHRELRLEIPGSRLEQEEPLTDAERMKLLQQENEELRRRLASATRRTEALE---RELEIGQDCLELELGQSRE------E 89
Cdd:PRK03918  208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEkvkelkE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  90 LDKFKDKFRRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKtldwEIVELTNKLLDAKNTINKLEELNER 169
Cdd:PRK03918  288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHEL 363


                  .
gi 1622933589 170 Y 170
Cdd:PRK03918  364 Y 364
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
19-165 4.56e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  19 EHRELRLEIpgSRLEQE-----EPLTDAERmkllqqENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSR 87
Cdd:PRK02224  245 EHEERREEL--ETLEAEiedlrETIAETER------EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  88 EELDKFKDKFR-RLQNSYTASQRTNQELE---DKLHTLASLShswifaiKKAEMDRKTLDWEIVELTNKLLDAKNTINKL 163
Cdd:PRK02224  317 EELEDRDEELRdRLEECRVAAQAHNEEAEslrEDADDLEERA-------EELREEAAELESELEEAREAVEDRREEIEEL 389


                  ..
gi 1622933589 164 EE 165
Cdd:PRK02224  390 EE 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 13-165 4.67e-04

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: 43.13  E-value: 4.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   13 YRKAPPEHRELRLEIPGSRLE----QEEPLTDAERMKLLQQENEELRRRLASATRRTEALERELEIGQDclelELGQSRE 88
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR----EINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   89 ELDKFKDKFRRLQnsyTASQRTNQEL---EDKLHTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 165
Cdd:TIGR02169  407 ELDRLQEELQRLS---EELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 43-165 1.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  43 RMKLLQQENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHTL 121
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLE 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622933589 122 ASLSHswifaikkAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 165
Cdd:COG1196   309 ERRRE--------LEERLEELEEELAELEEELEELEEELEELEE 344
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-177 1.56e-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: 41.58  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   24 RLEIPGSRLEQEEPLTDAERMKLLQQEnEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS 103
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEI-EELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622933589  104 YTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE-----LNERYRLDCNLA 177
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESelealLNERASLEEALA 890
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
42-165 1.67e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  42 ERMKLLQQENEELRRRLASATRRTEALERELEIGQDCLEL---ELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKL 118
Cdd:COG4372    38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622933589 119 HTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 165
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 36-163 1.87e-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: 39.89  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  36 EPLTDAermkllQQENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQn 102
Cdd:pfam13851  61 EPLQKA------QEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622933589 103 sYTASQRT---NQELEDKLHTL--------ASLSHswifAIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 163
Cdd:pfam13851 134 -QDVQQKTglkNLLLEKKLQALgetlekkeAQLNE----VLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 13-168 1.92e-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: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   13 YRKAPPEHRELRLEIPGsrLEQEEPLTDAERMKLlQQENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDK 92
Cdd:TIGR02169  669 SRSEPAELQRLRERLEG--LKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEIEQ----LEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   93 FKDKFRRLQNSYTASQRTNQEL-------EDKLHTL--------ASLSHSwIFAIKKAEMDRktLDWEIVELTNKLLDAK 157
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELearieelEEDLHKLeealndleARLSHS-RIPEIQAELSK--LEEEVSRIEARLREIE 818

                          170
                   ....*....|.
gi 1622933589  158 NTINKLEELNE 168
Cdd:TIGR02169  819 QKLNRLTLEKE 829
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-168 1.95e-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: 41.20  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   30 SRLEQEEPLTDaERMKLLQQENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNSYTASQR 109
Cdd:TIGR02168  298 SRLEQQKQILR-ERLANLERQLEELEAQLEELESKLDELAEELAE----LEEKLEELKEELESLEAELEELEAELEELES 372

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622933589  110 TNQELEDKLHTLASlshswifAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNE 168
Cdd:TIGR02168  373 RLEELEEQLETLRS-------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 19-206 2.09e-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: 41.19  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   19 EHRELRLEIPGSRLEQEEP-LTDAERMKLLQQENEELRRRLASATRRTEALERELEIGQdcLELELGQSREELDKFKDKF 97
Cdd:TIGR00606  768 EEQETLLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKI 845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   98 RRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKA---EMDRKTLDWEIVELTNKLLDAKNTINKLEELNERYRLDC 174
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622933589  175 NLAVqllkcNKSHFRNHKFADlpcELQDMVRK 206
Cdd:TIGR00606  926 EELI-----SSKETSNKKAQD---KVNDIKEK 949
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-171 2.39e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  17 PPEHRELRLEIPGSRLEQEEpltdaERMKLLQQENEELRRRLASATRRTEALERELEigqdclELELGQSREELDKFKDK 96
Cdd:PRK03918  599 PFYNEYLELKDAEKELEREE-----KELKKLEEELDKAFEELAETEKRLEELRKELE------ELEKKYSEEEYEELREE 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622933589  97 FRRLQNSYTASQRTNQELEDKLHTLASLshswifaIKKAEMDRKtldwEIVELTNKLLDAKNTINKLEELNERYR 171
Cdd:PRK03918  668 YLELSRELAGLRAELEELEKRREEIKKT-------LEKLKEELE----EREKAKKELEKLEKALERVEELREKVK 731
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
6-118 3.50e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589   6 PAPAKKPYRKAPPEHRELR-LEIPGSRLEqeepltdaERMKLLQQENEELRRRLASATRRTEALERELEIGQDCLELELg 84
Cdd:COG2433   391 PEEEPEAEREKEHEERELTeEEEEIRRLE--------EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI- 461

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622933589  85 QSREELDKFKDKFRRLQNSYTASQRTNQELEDKL 118
Cdd:COG2433   462 RKDREISRLDREIERLERELEEERERIEELKRKL 495
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 45-169 4.87e-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: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  45 KLLQQENEELRRRLASATRRTEAL-----ERELEIGQ---DCLELELGQSREELDKFKD----KFRRLQNSYTASQRTNQ 112
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLesekkEKESKISDledELNKDDFELKKENLEKEIDeknkEIEELKQTQKSLKKKQE 585

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622933589 113 ELEDKlhtlaslshswifaIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNER 169
Cdd:TIGR04523 586 EKQEL--------------IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-171 6.53e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  19 EHRELRLEIpgSRLEQEEPLTDAERMKLLQQEN--EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDK 96
Cdd:COG1196   275 ELEELELEL--EEAQAEEYELLAELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622933589  97 FRRLQNSYTASQRTNQELEDKLHTLASLshswIFAIKKAEMDRKTldwEIVELTNKLLDAKNTINKLEELNERYR 171
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALR---AAAELAAQLEELEEAEEALLERLERLE 420
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 370-495 8.44e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589  370 ERARPSPVPSTPASAQASPHHQPSPAPPTLSAPASSASSEEDLLASWQRAFVDRTPPPAAVAQRTAFGRDALPELQRHFA 449
Cdd:PRK10263   378 EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA 457

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622933589  450 HSP-ADRDEVVQAPSPRPEESELLLPIEPDSGFPREEEEELNLPISP 495
Cdd:PRK10263   458 PQStYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARP 504
PHA03379 PHA03379
EBNA-3A; Provisional
 374-540 8.96e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 38.89  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 374 PSPVPSTPASAQASPHHQP--SPAPPTLSAPASSASSEEDLLASWQRAFVDRTPPPA--------AVAQRTAFGRDALPE 443
Cdd:PHA03379  421 EKPRPEVPQSLETATSHGSaqVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDlepgdqlpGVVQDGRPACAPVPA 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622933589 444 LQRHFAH--SPADRDEVVQAPSP-RPEEsellLPIEPDSgFPREEEEELNLPISPEEERQsllpinsGTGEGSGTSHTEG 520
Cdd:PHA03379  501 PAGPIVRpwEASLSQVPGVAFAPvMPQP----MPVEPVP-VPTVALERPVCPAPPLIAMQ-------GPGETSGIVRVRE 568

                         170       180
                  ....*....|....*....|
gi 1622933589 521 RAWPLPSSSRPQRSPKRMGV 540
Cdd:PHA03379  569 RWRPAPWTPNPPRSPSQMSV 588
 
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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