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Conserved domains on  [gi|530396379|ref|XP_005273859|]
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deuterosome assembly protein 1 isoform X2 [Homo sapiens]

Protein Classification

CEP63 and SMC_N domain-containing protein( domain architecture ID 12181506)

CEP63 and SMC_N domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
11-280 4.72e-100

Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.


:

Pssm-ID: 465338 [Multi-domain]  Cd Length: 264  Bit Score: 304.82  E-value: 4.72e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   11 TSPCEAELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYE 90
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   91 GQLQSLKAQFSKLTNNFEKLRLHQMKQNKVPrkelPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQ 170
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREE----AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  171 QKLLSEKCNQFQKQAqsYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEIALSRNKLQDENQK 250
Cdd:pfam17045 157 RKALAEQSSLIQSAA--YQVQLEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQR 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 530396379  251 LLQELKMYQRQCQAMEAGLSEVKSELQSRD 280
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELKATLQSQD 264
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
242-413 6.07e-05

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 242 NKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLESSYLPSI 321
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 322 KEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYhNSEQERMRNEISDLTEELHQKEITIATVTKKAALLEKQLKmE 401
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
                        170
                 ....*....|..
gi 530396379 402 LEIKEKMLAKQK 413
Cdd:PRK03918 333 LEEKEERLEELK 344
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
11-280 4.72e-100

Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.


Pssm-ID: 465338 [Multi-domain]  Cd Length: 264  Bit Score: 304.82  E-value: 4.72e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   11 TSPCEAELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYE 90
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   91 GQLQSLKAQFSKLTNNFEKLRLHQMKQNKVPrkelPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQ 170
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREE----AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  171 QKLLSEKCNQFQKQAqsYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEIALSRNKLQDENQK 250
Cdd:pfam17045 157 RKALAEQSSLIQSAA--YQVQLEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQR 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 530396379  251 LLQELKMYQRQCQAMEAGLSEVKSELQSRD 280
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELKATLQSQD 264
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
50-385 1.90e-09

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: 60.84  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    50 RDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYEG---QLQSLKAQFSKLTNNFEKLRLHQMK---QNKVPRK 123
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkELEELSRQISALRKDLARLEAEVEQleeRIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   124 ELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSS 203
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   204 SEIPRLicdpdpnceinERDEFIIEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLL 283
Cdd:TIGR02168  835 ATERRL-----------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   284 RIIEMERLQLHRELLKIGEC------------QNAQGNKTRLESSYlpsIKEPERKIKELFSVMQDQPNHEKELNKIRSQ 351
Cdd:TIGR02168  904 RELESKRSELRRELEELREKlaqlelrlegleVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKRLENK 980
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 530396379   352 LQQ--------VEEYhNSEQER---MRNEISDLTEELHQKEITIA 385
Cdd:TIGR02168  981 IKElgpvnlaaIEEY-EELKERydfLTAQKEDLTEAKETLEEAIE 1024
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
142-418 4.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 142 KLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINE 221
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 222 RDEfiiEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIG 301
Cdd:COG1196  313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 302 ECQNAQGNKTRLessylpsIKEPERKIKELfsvMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELHQKE 381
Cdd:COG1196  390 EALRAAAELAAQ-------LEELEEAEEAL---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 530396379 382 ITIATVTKKAALLEKQLKMELEIKEKMLAKQKVSDMK 418
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
242-413 6.07e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 242 NKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLESSYLPSI 321
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 322 KEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYhNSEQERMRNEISDLTEELHQKEITIATVTKKAALLEKQLKmE 401
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
                        170
                 ....*....|..
gi 530396379 402 LEIKEKMLAKQK 413
Cdd:PRK03918 333 LEEKEERLEELK 344
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
227-474 1.21e-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: 45.43  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   227 IEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGEcqNA 306
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   307 QGNKTRLESSYlPSIKEPERKIKELFSVMQDQpnhEKELNKIRSQLQQVEEYHN----------SEQERMRNEISDLTEE 376
Cdd:TIGR02168  764 EELEERLEEAE-EELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELTllneeaanlrERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   377 LHQKEITIATVTKKAALLEKQL----KMELEIKEKMLAKQKVSDMKYKAVRTENTHLKGMMGDLDPGEYMSMDFTNREQS 452
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIeeleELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260
                   ....*....|....*....|..
gi 530396379   453 RHTSINKLQYENERLRNDLAKL 474
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNL 941
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
224-406 6.73e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  224 EFIIEKLKSAVNEIAL-SRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLriiEMERLQLHRELLKIGE 302
Cdd:pfam09787  24 EKLIASLKEGSGVEGLdSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ---QEEAESSREQLQELEE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  303 CQNAQGNKTRLESSYLPSIKEPERKIKE--------LFSVMQDQpnhEKELNKIRSQLQqVEEYHNSEQERMRNEISDLT 374
Cdd:pfam09787 101 QLATERSARREAEAELERLQEELRYLEEelrrskatLQSRIKDR---EAEIEKLRNQLT-SKSQSSSSQSELENRLHQLT 176
                         170       180       190
                  ....*....|....*....|....*....|...
gi 530396379  375 EELHQKEITIATVTKKAALLEKQLK-MELEIKE 406
Cdd:pfam09787 177 ETLIQKQTMLEALSTEKNSLVLQLErMEQQIKE 209
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
227-416 7.51e-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: 38.98  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 227 IEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLL--RIIEMERLQLHRELLKIGECQ 304
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaeLLRALYRLGRQPPLALLLSPE 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 305 NAQGNKTRLE--SSYLPS----IKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELH 378
Cdd:COG4942  130 DFLDAVRRLQylKYLAPArreqAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530396379 379 QKEITIATVTKKAALLEKQLKmELEIKEKMLAKQKVSD 416
Cdd:COG4942  210 ELAAELAELQQEAEELEALIA-RLEAEAAAAAERTPAA 246
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
11-280 4.72e-100

Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.


Pssm-ID: 465338 [Multi-domain]  Cd Length: 264  Bit Score: 304.82  E-value: 4.72e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   11 TSPCEAELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYE 90
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   91 GQLQSLKAQFSKLTNNFEKLRLHQMKQNKVPrkelPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQ 170
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREE----AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  171 QKLLSEKCNQFQKQAqsYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEIALSRNKLQDENQK 250
Cdd:pfam17045 157 RKALAEQSSLIQSAA--YQVQLEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQR 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 530396379  251 LLQELKMYQRQCQAMEAGLSEVKSELQSRD 280
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELKATLQSQD 264
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
50-385 1.90e-09

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: 60.84  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    50 RDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYEG---QLQSLKAQFSKLTNNFEKLRLHQMK---QNKVPRK 123
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkELEELSRQISALRKDLARLEAEVEQleeRIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   124 ELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSS 203
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   204 SEIPRLicdpdpnceinERDEFIIEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLL 283
Cdd:TIGR02168  835 ATERRL-----------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   284 RIIEMERLQLHRELLKIGEC------------QNAQGNKTRLESSYlpsIKEPERKIKELFSVMQDQPNHEKELNKIRSQ 351
Cdd:TIGR02168  904 RELESKRSELRRELEELREKlaqlelrlegleVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKRLENK 980
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 530396379   352 LQQ--------VEEYhNSEQER---MRNEISDLTEELHQKEITIA 385
Cdd:TIGR02168  981 IKElgpvnlaaIEEY-EELKERydfLTAQKEDLTEAKETLEEAIE 1024
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
37-381 1.55e-08

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: 57.77  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    37 ERKMRALEtRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCN--LAMTQNYEG-----QLQSLKAQFSKLTNNFEK 109
Cdd:TIGR02169  170 RKKEKALE-ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQalLKEKREYEGyellkEKEALERQKEAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   110 LRLHQMKqnkvprkeLPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEIL-YQTHLISLDAQQKLLS---EKCNQFQKQA 185
Cdd:TIGR02169  249 LEEELEK--------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLErsiAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   186 QS----YQTQLNGKKQCLEDSSSEIPRLicdpdpnceiNERDEFIIEKLKSAVNEIALSRNKLQD---ENQKLLQELKMY 258
Cdd:TIGR02169  321 EErlakLEAEIDKLLAEIEELEREIEEE----------RKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDY 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   259 QRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQgnKTRLESSYLpSIKEPERKIKELFSVMQDQ 338
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL--EEEKEDKAL-EIKKQEWKLEQLAADLSKY 467
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 530396379   339 pnhEKELNKIRSQLQQVEEyhnseqermrnEISDLTEELHQKE 381
Cdd:TIGR02169  468 ---EQELYDLKEEYDRVEK-----------ELSKLQRELAEAE 496
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1-474 1.92e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379     1 MENQAHNTMGTSPCE-AELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGllrqkldsle 79
Cdd:pfam15921  304 IQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG---------- 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    80 kcnlamtqNYEGQLQSLKAQFSKltnnfeklRLHQMKQNKVPRKELPHLKEEIPFELSNLNQKLEEfraksREWDKQEil 159
Cdd:pfam15921  374 --------NLDDQLQKLLADLHK--------REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNMEVQR-- 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   160 yqthlisLDAQQKLLSEKCnqfQKQAQSYQTQLNGKKQCLEDSSSEIPRLicdpdpnceinerdEFIIEKLKSAVNEIAL 239
Cdd:pfam15921  431 -------LEALLKAMKSEC---QGQMERQMAAIQGKNESLEKVSSLTAQL--------------ESTKEMLRKVVEELTA 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   240 SRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVkSELQSRDDlLRIIEMERLQLHRELLkigecQNAQGNKTRLESSYLP 319
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQEKERAIEATNAEI-TKLRSRVD-LKLQELQHLKNEGDHL-----RNVQTECEALKLQMAE 559
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   320 SIKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEqermRNEISDLTEELHQKEITIATVTKKAALLE-KQL 398
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR----RLELQEFKILKDKKDAKIRELEARVSDLElEKV 635
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   399 KMELEIKEKMLAKQKVS---DMKYKAVRTENTHLKGMMGDLdpgEYMSMDFTNREQSRHTSINKL-------QYENERLR 468
Cdd:pfam15921  636 KLVNAGSERLRAVKDIKqerDQLLNEVKTSRNELNSLSEDY---EVLKRNFRNKSEEMETTTNKLkmqlksaQSELEQTR 712

                   ....*.
gi 530396379   469 NDLAKL 474
Cdd:pfam15921  713 NTLKSM 718
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
16-288 4.56e-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: 46.60  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    16 AELQELMEQIDIMvSNKKMDWERKMRALETRLDLRDQELANAQTCL-----DQKGQEVGLLRQKLDSLEKcnlaMTQNYE 90
Cdd:TIGR02169  737 ERLEELEEDLSSL-EQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEE----EVSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    91 GQLQSLKAQFSKLTnnFEKLRLHQMKQNKVP-RKELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDA 169
Cdd:TIGR02169  812 ARLREIEQKLNRLT--LEKEYLEKEIQELQEqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   170 QQKLLSEKCNQFQK----------QAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEinerDEFIIEKLKSAVNEIAL 239
Cdd:TIGR02169  890 ERDELEAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEE 965
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 530396379   240 SRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSElqsRDDLLRIIEM 288
Cdd:TIGR02169  966 EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE---RKAILERIEE 1011
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
142-418 4.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 142 KLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINE 221
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 222 RDEfiiEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIG 301
Cdd:COG1196  313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 302 ECQNAQGNKTRLessylpsIKEPERKIKELfsvMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELHQKE 381
Cdd:COG1196  390 EALRAAAELAAQ-------LEELEEAEEAL---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 530396379 382 ITIATVTKKAALLEKQLKMELEIKEKMLAKQKVSDMK 418
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
242-413 6.07e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 242 NKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLESSYLPSI 321
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 322 KEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYhNSEQERMRNEISDLTEELHQKEITIATVTKKAALLEKQLKmE 401
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
                        170
                 ....*....|..
gi 530396379 402 LEIKEKMLAKQK 413
Cdd:PRK03918 333 LEEKEERLEELK 344
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
90-377 7.30e-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: 45.82  E-value: 7.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    90 EGQLQSLKAQ------FSKLTNNFEKLRLH-----------QMKQNKVPRKELPHLKEEIPFELSNLNQKLEEFRAKSRE 152
Cdd:TIGR02168  199 ERQLKSLERQaekaerYKELKAELRELELAllvlrleelreELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   153 WDKQEILYQTHLIS-------LDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLicdpdpnceiNERDEF 225
Cdd:TIGR02168  279 LEEEIEELQKELYAlaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----------EEKLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   226 IIEKLKSAVNEIALSRNKLQDENQKL--LQELKMYQRQCQA-MEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIG- 301
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESRLeeLEEQLETLRSKVAqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLk 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   302 ECQNAQGNKTRLESSYLpsIKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQ------ERMRNEISDLTE 375
Cdd:TIGR02168  429 KLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSE 506

                   ..
gi 530396379   376 EL 377
Cdd:TIGR02168  507 GV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
38-314 1.15e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  38 RKMRALETRLDLRDQELA-----NAQTCLDQKGQEVGLLRQKLDSLEkcnlAMTQNYEGQLQSLKAQFSKLTNNFE---- 108
Cdd:COG1196  213 ERYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELE----AELAELEAELEELRLELEELELELEeaqa 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 109 KLRLHQMKQNKVpRKELPHLKEEIpfelSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSY 188
Cdd:COG1196  289 EEYELLAELARL-EQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 189 QTQLNGKKQCLEDSSSEIprlicdpdpnceinERDEFIIEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAG 268
Cdd:COG1196  364 EEALLEAEAELAEAEEEL--------------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 530396379 269 LSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLE 314
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
227-474 1.21e-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: 45.43  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   227 IEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGEcqNA 306
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--EI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   307 QGNKTRLESSYlPSIKEPERKIKELFSVMQDQpnhEKELNKIRSQLQQVEEYHN----------SEQERMRNEISDLTEE 376
Cdd:TIGR02168  764 EELEERLEEAE-EELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELTllneeaanlrERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   377 LHQKEITIATVTKKAALLEKQL----KMELEIKEKMLAKQKVSDMKYKAVRTENTHLKGMMGDLDPGEYMSMDFTNREQS 452
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIeeleELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260
                   ....*....|....*....|..
gi 530396379   453 RHTSINKLQYENERLRNDLAKL 474
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNL 941
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
30-356 1.23e-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: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    30 SNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTqnyEGQLQSLKAQFSKLTNNFEK 109
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG---EEEQLRVKEKIGELEAEIAS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   110 LRlHQMKQNKVPRKELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQ 189
Cdd:TIGR02169  306 LE-RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   190 TQLNGKKQCLEDssseiprlicdpdpnceinerdefiiekLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGL 269
Cdd:TIGR02169  385 DELKDYREKLEK----------------------------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   270 SEVKSELQSRDDLLRIIEMERLQLHRELLKIGecqnaqgnktrlessylpsikeperkiKELFSVMQDQPNHEKELNKIR 349
Cdd:TIGR02169  437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYE---------------------------QELYDLKEEYDRVEKELSKLQ 489

                   ....*..
gi 530396379   350 SQLQQVE 356
Cdd:TIGR02169  490 RELAEAE 496
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
38-505 1.11e-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: 42.34  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    38 RKMRALETRLDLRDQELANAQTC------LDQKGQEVGLLRQKLDSLE---KCNLAMTQNYEGQLQSLKAQFSKLTNNFE 108
Cdd:TIGR00606  183 RYIKALETLRQVRQTQGQKVQEHqmelkyLKQYKEKACEIRDQITSKEaqlESSREIVKSYENELDPLKNRLKEIEHNLS 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   109 KL-----RLHQMKQNKVPR----KELPHLKEEIPFELSNLNQKLEEFRAKS-REWDKQEILYQTHLISLDAQQKLLSEKC 178
Cdd:TIGR00606  263 KImkldnEIKALKSRKKQMekdnSELELKMEKVFQGTDEQLNDLYHNHQRTvREKERELVDCQRELEKLNKERRLLNQEK 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   179 NQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDpnCEINERDEFIIEKLKsavNEIALSRNKLQDENQKLLQELKMY 258
Cdd:TIGR00606  343 TELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIK---NFHTLVIERQEDEAKTAAQLCADL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   259 QRQCQAMEAGLSEVKSELQSrddLLRIIEMERLQLHREL----LKIGECQNAQGNKTRLEssylpsikepeRKIKELFSV 334
Cdd:TIGR00606  418 QSKERLKQEQADEIRDEKKG---LGRTIELKKEILEKKQeelkFVIKELQQLEGSSDRIL-----------ELDQELRKA 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   335 MQDQPNHEKelNKIRSQLQQVEEYHNSEQERMRNEISDLTEELHQKEITIATVTKkaallekqlkMELEIKEKMLAKQKV 414
Cdd:TIGR00606  484 ERELSKAEK--NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ----------MEMLTKDKMDKDEQI 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   415 SDMKYKAvrteNTHLKGMMGDldpgeymsmdFTNREQSRHTsINKLQYENERLRNDLAKLHVNGKSTWTNQNTYEETGRY 494
Cdd:TIGR00606  552 RKIKSRH----SDELTSLLGY----------FPNKKQLEDW-LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
                          490
                   ....*....|.
gi 530396379   495 AYQSQIKVEQN 505
Cdd:TIGR00606  617 KEEQLSSYEDK 627
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
96-406 1.75e-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: 41.54  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   96 LKAQFSKLTNNFEKLRlHQMKQNKVPRKELPHLKEEIPFELSNLNQK---LEEFRAKSREWDKQEILYQTHLISLDAQQK 172
Cdd:TIGR04523 150 KEKELEKLNNKYNDLK-KQKEELENELNLLEKEKLNIQKNIDKIKNKllkLELLLSNLKKKIQKNKSLESQISELKKQNN 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  173 LLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEI-----ALSRNKLQDE 247
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLkseisDLNNQKEQDW 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  248 NQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLE----SSYLPSIKE 323
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIKN 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  324 PERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMR-------NEISDLTEELHQKEITIATVTKKAALLEK 396
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKetiiknnSEIKDLTNQDSVKELIIKNLDNTRESLET 468
                         330
                  ....*....|.
gi 530396379  397 QLK-MELEIKE 406
Cdd:TIGR04523 469 QLKvLSRSINK 479
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
95-506 5.61e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379    95 SLKAQFSKLTNNFEKLRLHQMKQNKVPRKELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLL 174
Cdd:pfam15921  289 SARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   175 SEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLiCDPDPNCEINerdefiIEKLKSAVNEialsRNKlqdENQKLLQE 254
Cdd:pfam15921  369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL-WDRDTGNSIT------IDHLRRELDD----RNM---EVQRLEAL 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   255 LKMYQRQCQA-MEAGLSEVKSELQSRDDLLRIieMERLQLHRELLKiGECQNAQGNKTRLESSylpsikepERKIKELFS 333
Cdd:pfam15921  435 LKAMKSECQGqMERQMAAIQGKNESLEKVSSL--TAQLESTKEMLR-KVVEELTAKKMTLESS--------ERTVSDLTA 503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   334 VMQDQPNH----EKELNKIRS----QLQQVEEYHNSEQ-----------------------ERMRNEISDLTEELHQKEI 382
Cdd:pfam15921  504 SLQEKERAieatNAEITKLRSrvdlKLQELQHLKNEGDhlrnvqtecealklqmaekdkviEILRQQIENMTQLVGQHGR 583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379   383 TIATVTKKAALLEKQLK-MELEIKE-KMLAKQKVSDMKYKAVRTENTHLKgMMGDLDPGEYMSMDFTNREQSRHTSINKL 460
Cdd:pfam15921  584 TAGAMQVEKAQLEKEINdRRLELQEfKILKDKKDAKIRELEARVSDLELE-KVKLVNAGSERLRAVKDIKQERDQLLNEV 662
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 530396379   461 QYENERLrNDLAKLHVNGKSTWTNQNTYEETGRYAYQSQIKVEQNE 506
Cdd:pfam15921  663 KTSRNEL-NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
224-406 6.73e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  224 EFIIEKLKSAVNEIAL-SRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLriiEMERLQLHRELLKIGE 302
Cdd:pfam09787  24 EKLIASLKEGSGVEGLdSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ---QEEAESSREQLQELEE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379  303 CQNAQGNKTRLESSYLPSIKEPERKIKE--------LFSVMQDQpnhEKELNKIRSQLQqVEEYHNSEQERMRNEISDLT 374
Cdd:pfam09787 101 QLATERSARREAEAELERLQEELRYLEEelrrskatLQSRIKDR---EAEIEKLRNQLT-SKSQSSSSQSELENRLHQLT 176
                         170       180       190
                  ....*....|....*....|....*....|...
gi 530396379  375 EELHQKEITIATVTKKAALLEKQLK-MELEIKE 406
Cdd:pfam09787 177 ETLIQKQTMLEALSTEKNSLVLQLErMEQQIKE 209
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
227-416 7.51e-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: 38.98  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 227 IEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLL--RIIEMERLQLHRELLKIGECQ 304
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaeLLRALYRLGRQPPLALLLSPE 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530396379 305 NAQGNKTRLE--SSYLPS----IKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELH 378
Cdd:COG4942  130 DFLDAVRRLQylKYLAPArreqAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530396379 379 QKEITIATVTKKAALLEKQLKmELEIKEKMLAKQKVSD 416
Cdd:COG4942  210 ELAAELAELQQEAEELEALIA-RLEAEAAAAAERTPAA 246
 
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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