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Conserved domains on  [gi|1063720758|ref|NP_001329454|]
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RING/U-box superfamily protein [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF6592 super family cl48402
Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase ...
 124-209 3.24e-14

Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase proteins. The function of this domain is unknown. The domain is about 120 amino acids in length.


The actual alignment was detected with superfamily member pfam20235:

Pssm-ID: 466386  Cd Length: 116  Bit Score: 69.25  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 124 LKAISSSRFYCGGTDLVSNIVNDTLSFLKSGK--KVAGSRDYV-FEDLQQLVAYSLVEKISLVREVRPSLSTDEAMWRLL 200
Cdd:pfam20235  23 HRALLDAGHCYGPLDPVSNIILNTIWYPATREspGEDLKGDMIsTDDLRRLESRSLDGLVAFLRSYFPYLTTGDALWYLL 102


                  ....*....
gi 1063720758 201 ICDLNVLKA 209
Cdd:pfam20235 103 LADADLLVA 111
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 1.95e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELqdwtdwanqKVKQATVRLLKdqpeLKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTN 553
Cdd:COG1196   214 RYRELKEEL---------KELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 554 NTIRRL-ELEQSLLKREREAANIRASESAEScREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG1196   281 LELEEAqAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359


                  ....*
gi 1063720758 633 QNQIE 637
Cdd:COG1196   360 LAEAE 364
 
Name Accession Description Interval E-value
DUF6592 pfam20235
Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase ...
 124-209 3.24e-14

Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase proteins. The function of this domain is unknown. The domain is about 120 amino acids in length.


Pssm-ID: 466386  Cd Length: 116  Bit Score: 69.25  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 124 LKAISSSRFYCGGTDLVSNIVNDTLSFLKSGK--KVAGSRDYV-FEDLQQLVAYSLVEKISLVREVRPSLSTDEAMWRLL 200
Cdd:pfam20235  23 HRALLDAGHCYGPLDPVSNIILNTIWYPATREspGEDLKGDMIsTDDLRRLESRSLDGLVAFLRSYFPYLTTGDALWYLL 102


                  ....*....
gi 1063720758 201 ICDLNVLKA 209
Cdd:pfam20235 103 LADADLLVA 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 1.95e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELqdwtdwanqKVKQATVRLLKdqpeLKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTN 553
Cdd:COG1196   214 RYRELKEEL---------KELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 554 NTIRRL-ELEQSLLKREREAANIRASESAEScREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG1196   281 LELEEAqAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359


                  ....*
gi 1063720758 633 QNQIE 637
Cdd:COG1196   360 LAEAE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 474-638 1.97e-08

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: 58.14  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQ--DWTDWANQkVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLER 551
Cdd:TIGR02168  214 RYKELKAELRelELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  552 TNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKT 631
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372


                   ....*..
gi 1063720758  632 RQNQIEV 638
Cdd:TIGR02168  373 RLEELEE 379
PRK12704 PRK12704
phosphodiesterase; Provisional
 494-629 2.27e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 494 KQATVRLLKDQPELKALRKE-KEEAEEFRKEKQL-LEENTIKRRSEMELALNNATNQLERTNNtirRLELEQSLLKRERE 571
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEK---RLLQKEENLDRKLE 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063720758 572 AANIRAsesaescREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDK---VAGLQQEVAKA 629
Cdd:PRK12704  104 LLEKRE-------EELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAEEAKE 157
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 470-633 7.55e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.68  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 470 KLVPRMK-DLQKELQDWTDWANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQ 548
Cdd:pfam05262 181 KVVEALReDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 549 LERTNNTIRRLELE-QSLLKREREAANIRASESAESCREAKE-RVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEV 626
Cdd:pfam05262 261 PKPADTSSPKEDKQvAENQKREIEKAQIEIKKNDEEALKAKDhKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKT 340


                  ....*..
gi 1063720758 627 AKAKTRQ 633
Cdd:pfam05262 341 KPQVEAQ 347
 
Name Accession Description Interval E-value
DUF6592 pfam20235
Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase ...
 124-209 3.24e-14

Family of unknown function (DUF6592); This putative domain is found in plant E3-ligase proteins. The function of this domain is unknown. The domain is about 120 amino acids in length.


Pssm-ID: 466386  Cd Length: 116  Bit Score: 69.25  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 124 LKAISSSRFYCGGTDLVSNIVNDTLSFLKSGK--KVAGSRDYV-FEDLQQLVAYSLVEKISLVREVRPSLSTDEAMWRLL 200
Cdd:pfam20235  23 HRALLDAGHCYGPLDPVSNIILNTIWYPATREspGEDLKGDMIsTDDLRRLESRSLDGLVAFLRSYFPYLTTGDALWYLL 102


                  ....*....
gi 1063720758 201 ICDLNVLKA 209
Cdd:pfam20235 103 LADADLLVA 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 1.95e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELqdwtdwanqKVKQATVRLLKdqpeLKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTN 553
Cdd:COG1196   214 RYRELKEEL---------KELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 554 NTIRRL-ELEQSLLKREREAANIRASESAEScREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG1196   281 LELEEAqAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359


                  ....*
gi 1063720758 633 QNQIE 637
Cdd:COG1196   360 LAEAE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 474-638 1.97e-08

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: 58.14  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQ--DWTDWANQkVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLER 551
Cdd:TIGR02168  214 RYKELKAELRelELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  552 TNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKT 631
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372


                   ....*..
gi 1063720758  632 RQNQIEV 638
Cdd:TIGR02168  373 RLEELEE 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 489-637 1.45e-07

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: 55.06  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  489 ANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTNNTIRRLELEQSLLKR 568
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063720758  569 EREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 1.57e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTN 553
Cdd:COG1196   240 ELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 554 NTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQ 633
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395


                  ....
gi 1063720758 634 NQIE 637
Cdd:COG1196   396 AELA 399
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
457-633 2.51e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 457 IYIPRNKRDELILKlvpRMKDLQKELQDWTDwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEEN--TIKR 534
Cdd:COG4717    58 LFKPQGRKPELNLK---ELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 535 RSEMELALNNATNQLERTNNTIRRL-ELEQSLLKREREAANIRAS----------ESAESCREAKERVQRLLKNSQSWEG 603
Cdd:COG4717   134 LEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEEleelleqlslATEEELQDLAEELEELQQRLAELEE 213

                         170       180       190
                  ....*....|....*....|....*....|
gi 1063720758 604 QKNLLQEELKSQRDKVAGLQQEVAKAKTRQ 633
Cdd:COG4717   214 ELEEAQEELEELEEELEQLENELEAAALEE 243
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 1.03e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELQDWTdwANQKVKQATVRLLKDqpELKALRKEKEEA-EEFRKEKQLLEENTIKRRSEMELaLNNATNQLERT 552
Cdd:COG1196   247 ELEELEAELEELE--AELAELEAELEELRL--ELEELELELEEAqAEEYELLAELARLEQDIARLEER-RRELEERLEEL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 553 NNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401


                  ....*
gi 1063720758 633 QNQIE 637
Cdd:COG1196   402 LEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 507-637 1.42e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 507 LKALRKEKEEAEEFRKEKQLLEEntiKRRSEMELALNNATNQLERTNNTIRRLELEQSLLKREREAANIRASESAESCRE 586
Cdd:COG1196   202 LEPLERQAEKAERYRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063720758 587 AKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:COG1196   279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 474-627 3.05e-06

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: 50.84  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQDWTDWANQKVKQATVRLLKD-QPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNAT-NQLER 551
Cdd:TIGR02169  212 RYQALLKEKREYEGYELLKEKEALERQKEAiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLR 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  552 TNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLL-------KNSQSWEGQKNLLQEELKSQRDKVAGLQQ 624
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieeleREIEEERKRRDKLTEEYAELKEELEDLRA 371


                   ...
gi 1063720758  625 EVA 627
Cdd:TIGR02169  372 ELE 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
466-637 3.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  466 ELILKLVPRMKDLQKELQDWTDWANQKVKQATVRLLKD--------------QPELKALRKEKEEAEEFRKEKQLLEENT 531
Cdd:COG4913    242 EALEDAREQIELLEPIRELAERYAAARERLAELEYLRAalrlwfaqrrlellEAELEELRAELARLEAELERLEARLDAL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  532 IKRRSEMELALNNA-TNQLERTNNTIRRLELEQSLLKRERE-------AANIRASESAESCREAKERVQRLLknsQSWEG 603
Cdd:COG4913    322 REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRArleallaALGLPLPASAEEFAALRAEAAALL---EALEE 398

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1063720758  604 QKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:COG4913    399 ELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 474-637 7.11e-06

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: 49.67  E-value: 7.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQDWTDwANQKVKQatvRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTN 553
Cdd:TIGR02168  310 RLANLERQLEELEA-QLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  554 NTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWE-----GQKNLLQEELKSQRDKVAGLQQEVAK 628
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEE 465


                   ....*....
gi 1063720758  629 AKTRQNQIE 637
Cdd:TIGR02168  466 LREELEEAE 474
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 463-637 1.11e-05

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: 47.23  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 463 KRDELILKLVPRMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQlleentiKRRSEMELAL 542
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 543 NNATNQLErtnntIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNsqsWEGQKNLLQEELKSQRDKVAGL 622
Cdd:COG1579    83 GNVRNNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAEL 154

                         170
                  ....*....|....*
gi 1063720758 623 QQEVAKAKTRQNQIE 637
Cdd:COG1579   155 EAELEELEAEREELA 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 461-638 1.11e-05

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: 48.90  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  461 RNKRDELILKLVPRMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMEL 540
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  541 ALNNATNQLERTNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVA 620
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          170
                   ....*....|....*...
gi 1063720758  621 GLQQEVAKAKTRQNQIEV 638
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEV 936
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 495-638 1.26e-05

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: 48.91  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  495 QATVRLLKDQpeLKALRKEKEEAEEFRKEKQLLEEntiKRRSEMELALNNATNQLERTNNTIRRLELEQSLLKREREAAN 574
Cdd:TIGR02169  190 DLIIDEKRQQ--LERLRREREKAERYQALLKEKRE---YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063720758  575 IRASESAESCREAKERVQRLLKNSQSwEGQKNL--LQEELKSQRDKVAGLQQEVAKAKTRQNQIEV 638
Cdd:TIGR02169  265 KRLEEIEQLLEELNKKIKDLGEEEQL-RVKEKIgeLEAEIASLERSIAEKERELEDAEERLAKLEA 329
PRK12704 PRK12704
phosphodiesterase; Provisional
 494-629 2.27e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 494 KQATVRLLKDQPELKALRKE-KEEAEEFRKEKQL-LEENTIKRRSEMELALNNATNQLERTNNtirRLELEQSLLKRERE 571
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEK---RLLQKEENLDRKLE 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063720758 572 AANIRAsesaescREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDK---VAGLQQEVAKA 629
Cdd:PRK12704  104 LLEKRE-------EELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAEEAKE 157
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
470-642 2.45e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 470 KLVPRMKDLQKELQDWTDwanqkvkqatvrllkdqpELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQL 549
Cdd:COG4372    35 KALFELDKLQEELEQLRE------------------ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 550 ERTNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKA 629
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                         170
                  ....*....|...
gi 1063720758 630 KTRQNQIEVSSFV 642
Cdd:COG4372   177 SEAEAEQALDELL 189
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 474-637 7.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKE-KEEAEEfRKEKQLLEENTIKRRSEMELALNNATNQLERT 552
Cdd:COG1196   310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEElEEAEEE-LEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 553 NNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464


                  ....*
gi 1063720758 633 QNQIE 637
Cdd:COG1196   465 LAELL 469
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 479-633 8.25e-05

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: 46.20  E-value: 8.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  479 QKELQDWTDwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTNNTIRR 558
Cdd:TIGR02168  743 EQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063720758  559 LELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQ 633
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 478-636 1.03e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  478 LQKELQDWTDWANQKVKQATVRLLKDQPELKALR----KEKEEAEEFRKEKQLLEEntikrRSEMELALNNATNQLERTN 553
Cdd:TIGR00618  199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRealqQTQQSHAYLTQKREAQEE-----QLKKQQLLKQLRARIEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  554 NTIRRLELEQSLLKREREAANIRA-SESAESCREAKERV------------------QRLLKNSQSWEGQKNLLQ----- 609
Cdd:TIGR00618  274 AQEAVLEETQERINRARKAAPLAAhIKAVTQIEQQAQRIhtelqskmrsrakllmkrAAHVKQQSSIEEQRRLLQtlhsq 353

                          170       180
                   ....*....|....*....|....*...
gi 1063720758  610 -EELKSQRDKVAGLQQEVAKAKTRQNQI 636
Cdd:TIGR00618  354 eIHIRDAHEVATSIREISCQQHTLTQHI 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 461-630 1.46e-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: 45.44  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  461 RNKRDELILKLVPRMKDLQKE---LQDWTDWANQKVKQATVRLLKDQPELKALRKEKE----EAEEFRKEKQLLEENTIK 533
Cdd:TIGR02169  282 KDLGEEEQLRVKEKIGELEAEiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelerEIEEERKRRDKLTEEYAE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  534 RRSEMELALNNAtNQLERTNNTIR------RLELEQslLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNL 607
Cdd:TIGR02169  362 LKEELEDLRAEL-EEVDKEFAETRdelkdyREKLEK--LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438

                          170       180
                   ....*....|....*....|...
gi 1063720758  608 LQEELKSQRDKVAGLQQEVAKAK 630
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEWKLEQLA 461
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 479-632 2.20e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  479 QKELQDWTDWANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEE---------------NTIK-RRSEMELAL 542
Cdd:TIGR00618  248 KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHikavtqieqqaqrihTELQsKMRSRAKLL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  543 NNATNQLERTNNTIRRLELEQSLLKREREaaNIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGL 622
Cdd:TIGR00618  328 MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405

                          170
                   ....*....|
gi 1063720758  623 QQEVAKAKTR 632
Cdd:TIGR00618  406 QREQATIDTR 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 489-637 2.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 489 ANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTNNtiRRLELEQSLLKR 568
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE--ELEELEEELEEA 349

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063720758 569 EREAANIRASESAEScREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:COG1196   350 EEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 506-637 3.15e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 506 ELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTNNTIRRLELEQSLLKREREAANIRASESAESCR 585
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063720758 586 EAKERVQR--------LLKNSQSWEGQKNLLQ-------------EELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:COG4942   108 ELLRALYRlgrqpplaLLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALL 180
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
473-574 5.40e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 473 PRMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKE--KQLLE--ENTIKRRSEMELALNNATNQ 548
Cdd:COG3206   263 PVIQQLRAQLAE----LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeaQRILAslEAELEALQAREASLQAQLAQ 338

                          90       100
                  ....*....|....*....|....*.
gi 1063720758 549 LERTNNTIRRLELEQSLLKREREAAN 574
Cdd:COG3206   339 LEARLAELPELEAELRRLEREVEVAR 364
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 470-633 7.55e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.68  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 470 KLVPRMK-DLQKELQDWTDWANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQ 548
Cdd:pfam05262 181 KVVEALReDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 549 LERTNNTIRRLELE-QSLLKREREAANIRASESAESCREAKE-RVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEV 626
Cdd:pfam05262 261 PKPADTSSPKEDKQvAENQKREIEKAQIEIKKNDEEALKAKDhKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKT 340


                  ....*..
gi 1063720758 627 AKAKTRQ 633
Cdd:pfam05262 341 KPQVEAQ 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 474-637 8.05e-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: 8.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQDwtdwanqkVKQATVRLLKDQPELKA-LRKEKEEAEEFRKEKQLLEENTIKRRSEMElALNNATNQLERT 552
Cdd:TIGR02169  703 RLDELSQELSD--------ASRKIGEIEKEIEQLEQeEEKLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  553 NNtirrlELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTR 632
Cdd:TIGR02169  774 LH-----KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848


                   ....*
gi 1063720758  633 QNQIE 637
Cdd:TIGR02169  849 IKSIE 853
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 465-627 1.12e-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: 42.35  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  465 DELILKLVPRMKDLQKELQDWTdwANQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLE-ENTIKRRSEMELALN 543
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALR--EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLA 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  544 NATNQLERTNNTIRR----LELEQSLLKREREAANIRASESAESCREAKERVQRLlknsqswEGQKNLLQEELKSQRDKV 619
Cdd:TIGR02168  859 AEIEELEELIEELESeleaLLNERASLEEALALLRSELEELSEELRELESKRSEL-------RRELEELREKLAQLELRL 931


                   ....*...
gi 1063720758  620 AGLQQEVA 627
Cdd:TIGR02168  932 EGLEVRID 939
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
474-637 1.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  474 RMKDLQKELQDWTDWANQ--KVKQATVRLLKDQPELKALRKEKEEAEEfrkekqlleentikrrsemelALNNATNQLER 551
Cdd:COG4913    652 RLAEYSWDEIDVASAEREiaELEAELERLDASSDDLAALEEQLEELEA---------------------ELEELEEELDE 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  552 TNNTIRRLELEQSLLKREREAANIRASESAESCREAkervqrllknsQSWEGQKNLLQEELKSQRDKV-AGLQQEVAKAK 630
Cdd:COG4913    711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-----------LRALLEERFAAALGDAVERELrENLEERIDALR 779


                   ....*..
gi 1063720758  631 TRQNQIE 637
Cdd:COG4913    780 ARLNRAE 786
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
489-637 1.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 489 ANQKVKQATVRLLKDQPELKALRKEKEEAeefRKEKQLLEENTIKRRSEMElalnNATNQLERTNNTIRRLELEQSLLKR 568
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQA---REELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQAQE 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063720758 569 EREAANirasesaESCREAKERVQRLLKnsqswegQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:COG4372   102 ELESLQ-------EEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 474-657 1.96e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 474 RMKDLQKELQDwtdwANQKVKQATVRLLKDQPELKALRKEKEEAEEfRKEKQLLEENTIKRRSEMELALN---------- 543
Cdd:COG4942    63 RIAALARRIRA----LEQELAALEAELAELEKEIAELRAELEAQKE-ELAELLRALYRLGRQPPLALLLSpedfldavrr 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 544 ------------NATNQLERTNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLL----KNSQSWEGQKNL 607
Cdd:COG4942   138 lqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLarleKELAELAAELAE 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063720758 608 LQEELKSQRDKVAGLQQEVAKAKTRQNQIEVSSFVGKMPLHVLGLLV--FGA 657
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSGRVVrrFGE 269
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 506-624 2.39e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 38.77  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 506 ELKALRKEKEEAEEfrKEKQLLEENTiKRRSEMELALNNATNQLERTNNTIRRLEleqsllkREREAANIRASESAESCR 585
Cdd:pfam07926   9 EIKRLKEEAADAEA--QLQKLQEDLE-KQAEIAREAQQNYERELVLHAEDIKALQ-------ALREELNELKAEIAELKA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063720758 586 EAKERVQRLLKNSQSWEGQKNLLQEELKSQRDKVAGLQQ 624
Cdd:pfam07926  79 EAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNE 117
mukB PRK04863
chromosome partition protein MukB;
508-635 3.24e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  508 KALRKEKEEAEEFRKEKQLLEENtikrRSEMELALNNATNQLERTNNTIRRLEleqsllKRER-----EAANIRASESAE 582
Cdd:PRK04863   300 RQLAAEQYRLVEMARELAELNEA----ESDLEQDYQAASDHLNLVQTALRQQE------KIERyqadlEELEERLEEQNE 369

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063720758  583 SCREAKERVQRLlknsqswEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQ 635
Cdd:PRK04863   370 VVEEADEQQEEN-------EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
PRK11281 PRK11281
mechanosensitive channel MscK;
469-627 3.25e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  469 LKLVPRMKDLQKELQDWtdwaNQKVKQATVRLLKDQPELKALRKE--KEEAEEFRKE--KQlLEENTIKRRSEME---LA 541
Cdd:PRK11281    69 LALLDKIDRQKEETEQL----KQQLAQAPAKLRQAQAELEALKDDndEETRETLSTLslRQ-LESRLAQTLDQLQnaqND 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  542 LNNATNQL-------ER-----TNNTIRRLELEQSLLKREREAANIRASE----SAE-SCREAKERVQR-LLKNSqsweg 603
Cdd:PRK11281   144 LAEYNSQLvslqtqpERaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQrvllQAEqALLNAQNDLQRkSLEGN----- 218

                          170       180
                   ....*....|....*....|....*...
gi 1063720758  604 qkNLLQEELKSQRD----KVAGLQQEVA 627
Cdd:PRK11281   219 --TQLQDLLQKQRDyltaRIQRLEHQLQ 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 459-627 3.66e-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: 40.82  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  459 IPRNKRDELILKLVPRMKDLQKELQDWtdwaNQKVKQATVRLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEM 538
Cdd:TIGR02169  784 LEARLSHSRIPEIQAELSKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  539 ELALNNATNQLERTNNTIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDK 618
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939


                   ....*....
gi 1063720758  619 VAGLQQEVA 627
Cdd:TIGR02169  940 KGEDEEIPE 948
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 506-637 3.71e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.59  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 506 ELKALRKEKEEAEEFRKEKQLLE---------ENTIKRRSEMELALNNATNQLErtnnTIRRlELEQSLLKREREAANIR 576
Cdd:pfam12795   1 KLDELEKAKLDEAAKKKLLQDLQqalslldkiDASKQRAAAYQKALDDAPAELR----ELRQ-ELAALQAKAEAAPKEIL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063720758 577 ASESAEscreakERVQRLLKNS---QSWEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQIE 637
Cdd:pfam12795  76 ASLSLE------ELEQRLLQTSaqlQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIR 133
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 514-618 3.84e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 514 KEEAEefrKEKQLLEENTIKRRSEMELALNNATNQLERT---NNTIRRLELEQSLLKRER---EAANIRASESAES---- 583
Cdd:pfam20492   1 REEAE---REKQELEERLKQYEEETKKAQEELEESEETAeelEEERRQAEEEAERLEQKRqeaEEEKERLEESAEMeaee 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063720758 584 -------CREAKERVQRLLKNSQSWEGQKNLLQEELKSQRDK 618
Cdd:pfam20492  78 keqleaeLAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 463-648 4.09e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 463 KRDELILKLVPRMKDLQKELQDWTDWANQKVKQAtvrllKDQPELKaLRKEKEEAEEFRKEKQLLEentiKRRSEMELAL 542
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQK-----GDEVKCK-LDKSEENARSIEYEVLKKE----KQMKILENKC 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 543 NNATNQLERTNNTIRRLELEQSLLKREREAAN-------IRASESAESCREAKERVQRLLKNSQSWEGQKNLLQEELKSQ 615
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063720758 616 RDKVAGLQQEVAKAKT---RQNQIEVSSFVGKMPLH 648
Cdd:pfam05483 677 VEKAKAIADEAVKLQKeidKRCQHKIAEMVALMEKH 712
Caldesmon pfam02029
Caldesmon;
503-639 4.96e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 503 DQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELALNNATNQLERTNNTIRRLELEQSLLKREREAANIRASESAE 582
Cdd:pfam02029   2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 583 SCREAKERVQRLLKNSQSWEGQKNLLQEELKS---QRDKVAGLQQEVAKAKTRQNQIEVS 639
Cdd:pfam02029  82 ALERQKEFDPTIADEKESVAERKENNEEEENSsweKEEKRDSRLGRYKEEETEIREKEYQ 141
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 525-638 5.13e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 38.62  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 525 QLLEENTIKRRSEMELALNNATNQLERTNN------TIRRLELEQSLLKREREAANIRASESAESCREAKERVQRLLKNS 598
Cdd:pfam14662  18 QKLLQENSKLKATVETREETNAKLLEENLNlrkqakSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKEN 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063720758 599 QSWEGQKNLLQEELK---SQRDKVAGLQQEVAKAK-TRQNQIEV 638
Cdd:pfam14662  98 QSLLQEIESLQEENKknqAERDKLQKKKKELLKSKaCLKEQLHS 141
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 494-616 5.38e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 494 KQATVRLLKDQPELKalRKEKEEAEEFRKE--KQLLEENTIKR-----RSEMELALNNATNQLERTNNTIRRLELE---Q 563
Cdd:pfam05672  19 KRRQAREQREREEQE--RLEKEEEERLRKEelRRRAEEERARReeearRLEEERRREEEERQRKAEEEAEEREQREqeeQ 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063720758 564 SLLKREREAANIRASESAESCReaKERVQRLLKNSQSWEGQKNLLQEELKSQR 616
Cdd:pfam05672  97 ERLQKQKEEAEAKAREEAERQR--QEREKIMQQEEQERLERKKRIEEIMKRTR 147
COG5022 COG5022
Myosin heavy chain [General function prediction only];
463-632 5.63e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.06  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  463 KRDELILKLVPRMKDLQKELQDwTDWANQKVKQatVRLLKDQPELKALRKEKEEAEEFRKE-----------KQLLEENT 531
Cdd:COG5022    865 KKETIYLQSAQRVELAERQLQE-LKIDVKSISS--LKLVNLELESEIIELKKSLSSDLIENlefkteliarlKKLLNNID 941

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  532 IKRRSEMELALNNATNQLERTNNTIRRLEleqsllkREREAANIRASESAESCREAKERVQRLLKNSQSWEGQKNLLQE- 610
Cdd:COG5022    942 LEEGPSIEYVKLPELNKLHEVESKLKETS-------EEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEs 1014

                          170       180
                   ....*....|....*....|....
gi 1063720758  611 --ELKSQRDKVAGLQQEVAKAKTR 632
Cdd:COG5022   1015 tkQLKELPVEVAELQSASKIISSE 1038
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 481-636 5.90e-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: 40.03  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  481 ELQDWTDWANQKVKQATVRLLKDQPELKALRKEKEEAEEfrKEKQLLEENTIKRRSEMELALNNATNQLERTNNTIRRLE 560
Cdd:TIGR00606  430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG--SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQ 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  561 LEQSLLKREREAaniRASESAESCREAKERVQRLL-------KNSQ----SWEGQKNL-------------------LQE 610
Cdd:TIGR00606  508 NEKADLDRKLRK---LDQEMEQLNHHTTTRTQMEMltkdkmdKDEQirkiKSRHSDELtsllgyfpnkkqledwlhsKSK 584

                          170       180
                   ....*....|....*....|....*.
gi 1063720758  611 ELKSQRDKVAGLQQEVAKAKTRQNQI 636
Cdd:TIGR00606  585 EINQTRDRLAKLNKELASLEQNKNHI 610
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 508-635 6.41e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758  508 KALRKEKEEAEEFRKEKQLLEEntikRRSEMELALNNATNQLERTNNTIRRLEleqsllKRER-----EAANIRASESAE 582
Cdd:COG3096    299 RQLAEEQYRLVEMARELEELSA----RESDLEQDYQAASDHLNLVQTALRQQE------KIERyqedlEELTERLEEQEE 368

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063720758  583 SCREAKERVQRLlknsqswEGQKNLLQEELKSQRDKVAGLQQEVAKAKTRQNQ 635
Cdd:COG3096    369 VVEEAAEQLAEA-------EARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQ 414
PRK12705 PRK12705
hypothetical protein; Provisional
 476-599 7.36e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720758 476 KDLQKELQDWTDWANQKVKQAtvrLLKDQPELKALRKEKEEAEEFRKEKQLLEENTIKRRSEMELA----LNNATNQLER 551
Cdd:PRK12705   33 KEAERILQEAQKEAEEKLEAA---LLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraekLDNLENQLEE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063720758 552 TNNTIRRLELEQSLLKRER-----EAANIRASES---------AESCREAKERVQRLLKNSQ 599
Cdd:PRK12705  110 REKALSARELELEELEKQLdnelyRVAGLTPEQArklllklldAELEEEKAQRVKKIEEEAD 171
 
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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