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Conserved domains on  [gi|2029126895|ref|NP_001381473|]
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tight junction-associated protein 1 isoform d [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 ...
 233-505 1.06e-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: 208.67  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 233 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 311
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 312 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 367
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 368 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 413
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 414 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 467
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2029126895 468 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 505
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-118 1.43e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895    9 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRK- 87
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLe 275

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2029126895   88 --TLDWEIVELTNKLLDAKNTINKLEELNERYR 118
Cdd:TIGR02168  276 vsELEEEIEELQKELYALANEISRLEQQKQILR 308
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 233-505 1.06e-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: 208.67  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 233 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 311
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 312 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 367
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 368 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 413
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 414 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 467
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2029126895 468 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 505
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-118 1.43e-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: 44.66  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895    9 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRK- 87
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLe 275

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2029126895   88 --TLDWEIVELTNKLLDAKNTINKLEELNERYR 118
Cdd:TIGR02168  276 vsELEEEIEELQKELYALANEISRLEQQKQILR 308
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-112 4.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   1 MKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHT-- 77
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLee 309

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2029126895  78 LIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEE 344
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 4-110 1.15e-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: 40.27  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   4 LQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQnsYTASQRT--- 67
Cdd:pfam13851  66 AQEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI--QDVQQKTglk 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126895  68 -----------NQELEDK---LHTLIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 110
Cdd:pfam13851 144 nlllekklqalGETLEKKeaqLNEVLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-112 1.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   7 ENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSREELDKFKDKFR-RLQNSYTASQRTNQELE------D 73
Cdd:PRK02224  273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARREELEDRDEELRdRLEECRVAAQAHNEEAEslredaD 352

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2029126895  74 KLHTLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:PRK02224  353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
 
Name Accession Description Interval E-value
Pilt pfam15453
Protein incorporated later into Tight Junctions; Pilt is a family of eukaryotic tight ...
 233-505 1.06e-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: 208.67  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 233 TPQPNGECHSLGTARGSPEEelpLPAFEKLNPYPTPSPPHPLYPGRRVIEF-SEDKVRIPRNSPLPNCTYATRQAISLSL 311
Cdd:pfam15453  13 GKQQNGSCRSQSSLESPPGE---APAFEKLNPYPTPPPPHPLYPGRKVIEFsSDDKVKIPKNSPLPNCTYATRQAISLSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 312 V---EEGSERARP---SPVPS------------------TPASAQASPHHQPSPAPLTLSAPASSassEEDLLVSWQRAF 367
Cdd:pfam15453  90 VqneDESGERQRTvpnSPASSgggsasscslqrtpkagsAPGSSQSSPFSSPPQAPSAFASSGSS---EEDLLANWQRMF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 368 VDRTPPPA--AVAQRTAFGRDALPELQRHFA------------HSPA--DRDEVVQAPSARP------------------ 413
Cdd:pfam15453 167 VEKMAPSSerSLVNRTSFSSDTAQELQRRRNakggrsmqelgrARAAysDGEEGSSSCSWTPsrgssldtdttdslrarr 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895 414 ---------EESELLL--------------PTEPDSGFPREEEELNLPISPEEERQSLL---PINrgTEEGPGTSHTEGR 467
Cdd:pfam15453 247 shygtdfseEEGEKLLmaadeegaagdasvPVESSPKKHKDYVDLGSPGSSAEERDVLLqdlPVI--SSRVLGELSDEAD 324

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2029126895 468 AWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLL 505
Cdd:pfam15453 325 KDPAAPSSRPHRSPKRMGVHHLHRKDSLTRAQEQGNLL 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-118 1.43e-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: 44.66  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895    9 EELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKKAEMDRK- 87
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLe 275

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2029126895   88 --TLDWEIVELTNKLLDAKNTINKLEELNERYR 118
Cdd:TIGR02168  276 vsELEEEIEELQKELYALANEISRLEQQKQILR 308
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-116 2.29e-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: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   2 KLLQEENEELRRRLASATRRTEAL-----ERELEIGQ---DCLELELGQSREELDKFKD----KFRRLQNSYTASQRTNQ 69
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLesekkEKESKISDledELNKDDFELKKENLEKEIDeknkEIEELKQTQKSLKKKQE 585

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2029126895  70 ELEDklhtLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNER 116
Cdd:TIGR04523 586 EKQE----LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-112 4.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   1 MKLLQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNS-YTASQRTNQELEDKLHT-- 77
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEeYELLAELARLEQDIARLee 309

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2029126895  78 LIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEE 344
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-127 9.77e-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: 41.97  E-value: 9.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895    1 MKLLQEENEELRRRLASATRRTEALERELEigqdclelelgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTL-- 78
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIE-----------ELEELIEELESELEALLNERASLEEALALLRSELEELse 901

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126895   79 -IKKAEMDRKTLDWEIVELTNKLLDAKNTINKL--------EELNERYRLDCNLAVQL 127
Cdd:TIGR02168  902 eLRELESKRSELRRELEELREKLAQLELRLEGLevridnlqERLSEEYSLTLEEAEAL 959
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 4-110 1.15e-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: 40.27  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   4 LQEENEELRR----------RLASATRRTEALE---RELEIGQDCLELELGQSREELDKFKDKFRRLQnsYTASQRT--- 67
Cdd:pfam13851  66 AQEEVEELRKqlenyekdkqSLKNLKARLKVLEkelKDLKWEHEVLEQRFEKVERERDELYDKFEAAI--QDVQQKTglk 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2029126895  68 -----------NQELEDK---LHTLIKKAEMDRKTLDwEIVELTNKLLDAKN-TINKL 110
Cdd:pfam13851 144 nlllekklqalGETLEKKeaqLNEVLAAANLDPDALQ-AVTEKLEDVLESKNqLIKDL 200
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-112 1.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   7 ENEELRRRLASATRRTEALERELEIGQDCLELE------LGQSREELDKFKDKFR-RLQNSYTASQRTNQELE------D 73
Cdd:PRK02224  273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaVEARREELEDRDEELRdRLEECRVAAQAHNEEAEslredaD 352

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2029126895  74 KLHTLIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:PRK02224  353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-87 1.59e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   2 KLLQEENEELRRRLASATRRTEALERELEIGQDCLELELgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIKK 81
Cdd:COG2433   423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501


                  ....*.
gi 2029126895  82 AEMDRK 87
Cdd:COG2433   502 WKLEHS 507
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 4-112 1.79e-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: 41.16  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   4 LQEENEELRRRLASATRRTEALERELEigqdclelelgQSREELDKFKDKFRRLQNSYTASQRTNQELEDKlhtlIKKAE 83
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQ 418

                          90       100
                  ....*....|....*....|....*....
gi 2029126895  84 MDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTN 447
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-118 3.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   1 MKLLQEENEELRRRLASATRRTEALERELEigqdclELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLIK 80
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKELE------ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2029126895  81 KAEMDRKTLDwEIVELTNKLLDAKNTINKLEELNERYR 118
Cdd:PRK03918  695 TLEKLKEELE-EREKAKKELEKLEKALERVEELREKVK 731
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-112 3.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   1 MKLLQEENEELRRRLASATRRTEALERELEIGQDCLEL---ELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHT 77
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2029126895  78 L---IKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:COG4372   120 LqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 2-118 4.14e-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: 37.16  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   2 KLLQEENEELRRRLASATRRTEALEREleigqdclELELgqsREELDKFkDKFRrlqnsytasqrtnQELEDKLHTLIKK 81
Cdd:pfam13863  13 LALDAKREEIERLEELLKQREEELEKK--------EQEL---KEDLIKF-DKFL-------------KENDAKRRRALKK 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2029126895  82 AEMDRK---TLDWEIVELTNKLLDAKNTINKLEELNERYR 118
Cdd:pfam13863  68 AEEETKlkkEKEKEIKKLTAQIEELKSEISKLEEKLEEYK 107
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-112 6.00e-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: 39.28  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895    4 LQEENEELRRRLASATRRTEALERE---LEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKlhtlIK 80
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKREineLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE----IK 451

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2029126895   81 KAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-117 7.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   2 KLLQEENEELRRRLASATRRTEALEREL-EIGQDCLElELGQSREELDKFKDKFRRLQNSytasqrtNQELEDKLhtliK 80
Cdd:PRK03918  552 EELKKKLAELEKKLDELEEELAELLKELeELGFESVE-ELEERLKELEPFYNEYLELKDA-------EKELEREE----K 619

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2029126895  81 KAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNERY 117
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1-118 7.77e-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: 38.47  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   1 MKLLQEENEELR---RRLASATRRTEALERELEIgqDCLE------LELGQSREELDKFKDKFRRLQNSYTASQRTNQEL 71
Cdd:pfam04849 173 LRGLEEENLKLRseaSHLKTETDTYEEKEQQLMS--DCVEqlseanQQMAELSEELARKMEENLRQQEEITSLLAQIVDL 250

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2029126895  72 EDKLHTLIKKAEmdrktldweivELTNKLLDAKNTINKL----EELNERYR 118
Cdd:pfam04849 251 QHKCKELGIENE-----------ELQQHLQASKEAQRQLtselQELQDRYA 290
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 4-112 8.25e-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: 37.98  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   4 LQEENEELRRRLASATRRTEALERELEIgqdcLELELGQSREELDKFKDKFRRLQNSYtASQRTNQELEDKLHTlIKKAE 83
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYEALQKE-IESLK 102

                          90       100
                  ....*....|....*....|....*....
gi 2029126895  84 MDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:COG1579   103 RRISDLEDEILELMERIEELEEELAELEA 131
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-116 9.07e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   11 LRRRL---ASATRRTEALERELeigqDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLhtlikkaemDRK 87
Cdd:COG4913    598 IRSRYvlgFDNRAKLAALEAEL----AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI---------DVA 664

                           90       100
                   ....*....|....*....|....*....
gi 2029126895   88 TLDWEIVELTNKLLDAKNTINKLEELNER 116
Cdd:COG4913    665 SAEREIAELEAELERLDASSDDLAALEEQ 693
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-112 9.34e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029126895   4 LQEENEELRRRLASATRRTEALERELEIGQDCLEL-----ELGQSREELDKFKDK---FRRLQNSYTASQRTNQELEDKL 75
Cdd:COG4717   100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaELAELPERLEELEERleeLRELEEELEELEAELAELQEEL 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2029126895  76 HTL-----------IKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEE 112
Cdd:COG4717   180 EELleqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
 
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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