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Conserved domains on  [gi|1212626334|ref|NP_001340053|]
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centrosomal protein of 63 kDa isoform d [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 ...
18-280 4.51e-92

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: 280.17  E-value: 4.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
                         250       260
                  ....*....|....*....|....*...
gi 1212626334 253 EKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-441 8.42e-11

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: 64.57  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 139 IERLTAKIEEFRQ--KSLdwEKQR------LIYQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:COG1196   188 LERLEDILGELERqlEPL--ERQAekaeryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAEL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 290 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKM 369
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1212626334 370 EISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
18-280 4.51e-92

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: 280.17  E-value: 4.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
                         250       260
                  ....*....|....*....|....*...
gi 1212626334 253 EKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-337 4.42e-12

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: 68.56  E-value: 4.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169  340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEEL 332
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQREL 492

                   ....*
gi 1212626334  333 KRMEA 337
Cdd:TIGR02169  493 AEAEA 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-441 8.42e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 139 IERLTAKIEEFRQ--KSLdwEKQR------LIYQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:COG1196   188 LERLEDILGELERqlEPL--ERQAekaeryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAEL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 290 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKM 369
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1212626334 370 EISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
95-365 8.94e-10

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: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 175 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG1196   312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1212626334 335 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 365
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-441 1.52e-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: 54.29  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  214 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  294 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 373
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626334  374 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-438 6.72e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 6.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224  192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224  347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 296 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 361
Cdd:PRK02224  427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 362 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 435
Cdd:PRK02224  507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586

                  ...
gi 1212626334 436 KLE 438
Cdd:PRK02224  587 RIE 589
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-444 6.63e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224  476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYKA 344
Cdd:PRK02224  548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 345 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVEHKEI---L 417
Cdd:PRK02224  628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALenrV 707
                         250       260
                  ....*....|....*....|....*..
gi 1212626334 418 DQLESLKLENRHLSEMVMKLELGLHER 444
Cdd:PRK02224  708 EALEALYDEAEELESMYGDLRAELRQR 734
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
165-430 4.66e-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: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  165 QQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTIcanELEIERLTMRvndLVGTSMTV 244
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQ---LVLANSEL 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  245 LQEQQQKEEKLRESEKLLEALQEekreLKAALQSQENLIHEARIQKEKLQEKVKATntqhaveaislesvSATCKQLSQE 324
Cdd:pfam15921  359 TEARTERDQFSQESGNLDDQLQK----LLADLHKREKELSLEKEQNKRLWDRDTGN--------------SITIDHLRRE 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ----------SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD 394
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1212626334  395 MEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHL 430
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHL 543
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
18-280 4.51e-92

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: 280.17  E-value: 4.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045   1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045  81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
                         250       260
                  ....*....|....*....|....*...
gi 1212626334 253 EKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-337 4.42e-12

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: 68.56  E-value: 4.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169  340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEEL 332
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQREL 492

                   ....*
gi 1212626334  333 KRMEA 337
Cdd:TIGR02169  493 AEAEA 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-441 8.42e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 139 IERLTAKIEEFRQ--KSLdwEKQR------LIYQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:COG1196   188 LERLEDILGELERqlEPL--ERQAekaeryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAEL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 290 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKM 369
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1212626334 370 EISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
95-365 8.94e-10

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: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 175 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG1196   312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1212626334 335 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 365
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-355 1.01e-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: 61.23  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEelcilkrsyeklqkkQMREFRGNTKNHREDR 136
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE---------------LSRQISALRKDLARLE 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  137 SEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERA 216
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLL 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  217 NDTICANELEIERLTMRVNDlvgtsmtvlqeqqqKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEK 296
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAA--------------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626334  297 VKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 355
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
136-418 1.15e-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: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 215
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  216 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL--------------QSQEN 281
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  282 LIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIlqgeQSYS 361
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL----RELE 907
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1212626334  362 SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 418
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-365 2.42e-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: 60.07  E-value: 2.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   37 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 116
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  117 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 196
Cdd:TIGR02168  304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  197 SVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL-----LEALQEEKRE 271
Cdd:TIGR02168  376 ELE----EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaiSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE 351
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
                          330
                   ....*....|....
gi 1212626334  352 QIlQGEQSYSSALE 365
Cdd:TIGR02168  528 LI-SVDEGYEAAIE 540
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
86-424 7.91e-09

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: 58.16  E-value: 7.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  166 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  245 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQE 324
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKE 890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEqsysSALEGMKMEISHLtQELHQRDITIASTKGSSSDMEKRLR---A 401
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQrveE 965
                          330       340
                   ....*....|....*....|....*..
gi 1212626334  402 EMQKAED---KAV-EHKEILDQLESLK 424
Cdd:TIGR02169  966 EIRALEPvnmLAIqEYEEVLKRLDELK 992
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-441 1.52e-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: 54.29  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  214 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  294 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 373
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626334  374 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
136-333 4.02e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206   188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENlihea 286
Cdd:COG3206   268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQA----- 334
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1212626334 287 riQKEKLQEKVKATNtQHAVEAISLESVSATCKQLSQELMEKYEELK 333
Cdd:COG3206   335 --QLAQLEARLAELP-ELEAELRRLEREVEVARELYESLLQRLEEAR 378
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-438 6.72e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 6.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224  192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224  347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 296 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 361
Cdd:PRK02224  427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 362 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 435
Cdd:PRK02224  507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586

                  ...
gi 1212626334 436 KLE 438
Cdd:PRK02224  587 RIE 589
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
157-439 3.96e-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: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  157 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 236
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  237 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAI---SLES 313
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  314 VSATCKQLSQELMEKY-----------EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA-LEGMKMEISHLTQELHQ- 380
Cdd:TIGR02168  373 RLEELEEQLETLRSKVaqlelqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEEl 452
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626334  381 --RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLEL 439
Cdd:TIGR02168  453 qeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-352 4.38e-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: 49.30  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   14 GGGFLTSCEAELQELMKQIDIM------VAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHE- 86
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEe 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   87 --KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgNTKNHREDRSEIERLTAKIEEfrqksldwekqrliyq 164
Cdd:TIGR02169  745 dlSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSK---------------- 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  165 qqvssLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169  803 -----LEEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL------- 866
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV------------------ 306
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleeelseiedpkgedeei 946
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1212626334  307 --EAISLESVSATCKQLSQEL-------MEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:TIGR02169  947 peEELSLEDVQAELQRVEEEIralepvnMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1-391 3.11e-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: 46.65  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334    1 MEALLEGIQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLH 79
Cdd:pfam15921  297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   80 QQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921  377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921  442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  226 EIERLTMRVNdlvgTSMTVLQEQQQKEEKLR--------------ESEKLLE---------------------ALQEEKR 270
Cdd:pfam15921  518 EITKLRSRVD----LKLQELQHLKNEGDHLRnvqtecealklqmaEKDKVIEilrqqienmtqlvgqhgrtagAMQVEKA 593
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:pfam15921  594 QLEKEINDRRLELQEFKILKDKKDAKIRELEAR--VSDLELEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNS 671
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1212626334  342 YKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGS 391
Cdd:pfam15921  672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
54-353 3.93e-05

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: 46.17  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNhR 133
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 134 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLVNRKQKLESVELSSQSE 205
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 206 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ------ 279
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikd 444
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1212626334 280 -ENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:TIGR04523 445 lTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
247-425 6.09e-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: 45.83  E-value: 6.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELM 326
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  327 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSAlegmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 406
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
                          170
                   ....*....|....*....
gi 1212626334  407 EDKAVEHKEILDQLESLKL 425
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKE 847
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-444 6.63e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224  476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYKA 344
Cdd:PRK02224  548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 345 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVEHKEI---L 417
Cdd:PRK02224  628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALenrV 707
                         250       260
                  ....*....|....*....|....*..
gi 1212626334 418 DQLESLKLENRHLSEMVMKLELGLHER 444
Cdd:PRK02224  708 EALEALYDEAEELESMYGDLRAELRQR 734
mukB PRK04863
chromosome partition protein MukB;
58-355 7.18e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 7.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   58 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 117
Cdd:PRK04863   389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 193
Cdd:PRK04863   466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 273
Cdd:PRK04863   544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  274 AALqsqenliheariqkEKLQEKVKATntqhaveaisLESvSATCKQLSQELMEKYEELKRmeaHNNEYKAEIKKLKEQI 353
Cdd:PRK04863   610 DAL--------------ARLREQSGEE----------FED-SQDVTEYMQQLLERERELTV---ERDELAARKQALDEEI 661

                   ..
gi 1212626334  354 LQ 355
Cdd:PRK04863   662 ER 663
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
95-353 1.49e-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: 43.98  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  95 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 175 KALAEQSEIIQAQLVNRKQKLESveLSSQSEIQHLSSKlerandticANELEIERLTMRVNDLVgtsmtvlQEQQQKEEK 254
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYLA-------PARREQAEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 255 LRESeklLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatckQLSQELMEKYEELKR 334
Cdd:COG4942   155 LRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAE 217
                         250
                  ....*....|....*....
gi 1212626334 335 MEAHNNEYKAEIKKLKEQI 353
Cdd:COG4942   218 LQQEAEELEALIARLEAEA 236
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
233-352 2.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 233 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKATnTQHAVEA 308
Cdd:PRK00409  517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1212626334 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:PRK00409  590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
136-346 2.86e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLVNRKQKLESVELSSqSEI 206
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALqsqenlihea 286
Cdd:COG4913    688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---------- 750
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626334  287 riqkekLQEKVKATNTQHAVEAISlESVSATCKQLSQELMEKYEEL-KRMEAHNNEYKAEI 346
Cdd:COG4913    751 ------LEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELeRAMRAFNREWPAET 804
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
58-325 3.70e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   58 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576  318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576  387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:pfam01576  467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1212626334  290 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQEL 325
Cdd:pfam01576  547 KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
246-377 4.04e-04

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: 41.83  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 246 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS--LESVSATCKQLSQ 323
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLED 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1212626334 324 ELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQE 377
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
46 PHA02562
endonuclease subunit; Provisional
203-436 4.45e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 203 QSEIQHLSSKLERANDTICANELEIERltmrvndlvgtsmtvlQEQQQKEEKLRESEKLLEALQEEKrELKAALQSQENL 282
Cdd:PHA02562  180 NQQIQTLDMKIDHIQQQIKTYNKNIEE----------------QRKKNGENIARKQNKYDELVEEAK-TIKAEIEELTDE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 283 IHEARIQKEKLQEKVKATNTQHAVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:PHA02562  243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 354 LQGEQSYSSALEgMKMEISHLTQELHQRDITIASTKGSSsdmeKRLRAEMQKAEDKAVEHKEILDQL-ESLKLENRHLSE 432
Cdd:PHA02562  323 DELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSE 397

                  ....
gi 1212626334 433 MVMK 436
Cdd:PHA02562  398 LVKE 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
164-358 8.53e-04

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: 8.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  244 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ-LS 322
Cdd:COG4913    670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLR 748
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1212626334  323 QELMEKYEELKRMEAHN---NEYKAEIKKLKEQILQGEQ 358
Cdd:COG4913    749 ALLEERFAAALGDAVERelrENLEERIDALRARLNRAEE 787
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
163-336 1.18e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 163 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSm 242
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 243 tvlqeqqqkEEKLRESEKLLEAlqeekrelKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS-LESVSATCKQL 321
Cdd:pfam00529 134 ---------PIGGISRESLVTA--------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEA 196
                         170
                  ....*....|....*
gi 1212626334 322 SQELMEKYEELKRME 336
Cdd:pfam00529 197 EAELKLAKLDLERTE 211
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-438 1.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918  343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 134 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 196
Cdd:PRK03918  416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 197 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 275
Cdd:PRK03918  496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 276 LQSQENLIHEARIQ-KEKLQEKVKATNtqhavEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 354
Cdd:PRK03918  576 LKELEELGFESVEElEERLKELEPFYN-----EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 355 QGEQSYS-SALEGMKMEISHLTQELhqrditiastkgsssdmeKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEM 433
Cdd:PRK03918  651 ELEKKYSeEEYEELREEYLELSREL------------------AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712

                  ....*
gi 1212626334 434 VMKLE 438
Cdd:PRK03918  713 LEKLE 717
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-353 1.78e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   98 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLiyqqqvSSLEAQRKA 176
Cdd:COG4913    235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAEL------EELRAELAR 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  177 LAEQSEIIQAQLVNRKQKLESVELssqseiQHLSSKLERandticaneleIERLTmrvndlvgtsmtvlQEQQQKEEKLR 256
Cdd:COG4913    307 LEAELERLEARLDALREELDELEA------QIRGNGGDR-----------LEQLE--------------REIERLERELE 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  257 ESEKLLEALQEEKRELKAALQSQE----NLIHEARIQKEKLQEKVKATNTQHAvEAISLESvsatckQLSQELMEKYEEL 332
Cdd:COG4913    356 ERERRRARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALA-EAEAALR------DLRRELRELEAEI 428
                          250       260
                   ....*....|....*....|.
gi 1212626334  333 KRMEAHNNEYKAEIKKLKEQI 353
Cdd:COG4913    429 ASLERRKSNIPARLLALRDAL 449
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
164-363 1.85e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSKLERANDTICANELEIERLTMRVNDLV----- 238
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAELEELNEEYNEL----QAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 239 -GTSMTVLQ------------EQQQKEEKLRESEK-LLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQH 304
Cdd:COG3883    98 sGGSVSYLDvllgsesfsdflDRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626334 305 AVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA 363
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
253-430 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: 40.52  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQELMEKYEEL 332
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 333 KRMEAHNNEYKAEIKK-LKEQILQGEQSY---------SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAE 402
Cdd:COG4942    93 AELRAELEAQKEELAElLRALYRLGRQPPlalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                         170       180
                  ....*....|....*....|....*...
gi 1212626334 403 MQKAEDKAVEHKEILDQLESLKLENRHL 430
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKL 200
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-220 1.96e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   20 SCEAELQELMKQIDIMVAhKKSEWEgrthALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYK 97
Cdd:COG4913    665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAA 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 175
Cdd:COG4913    740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1212626334  176 ALAEQSEIIQAQLVNRKQKL-ESVELSSQSEIQHLSSKLERANDTI 220
Cdd:COG4913    817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI 862
PRK09039 PRK09039
peptidoglycan -binding protein;
193-334 2.40e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039   41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1212626334 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ--------HAVEAISLES---VSATCKQLSQELMEKYEELKR 334
Cdd:PRK09039  121 LAQELDSEKQVSARALAQVELLNQQIAALRRQlaaleaalDASEKRDRESqakIADLGRRLNVALAQRVQELNR 194
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
61-353 2.93e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   61 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 136
Cdd:pfam12128  253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  137 SEIERLTAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKlesVELSSQSEIQHLSSK 212
Cdd:pfam12128  322 SELEALEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDK 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  213 LERANDTICANELEIErltmrvNDLVGTSMTVLQEQQQKEEKLRESEKLLE-ALQEEKRELKAALQSQENLIHEAriQKE 291
Cdd:pfam12128  399 LAKIREARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLE--NFD 470
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1212626334  292 KLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKyeeLKRMEAHNNEYKAEIKKLKEQI 353
Cdd:pfam12128  471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEA---LRQASRRLEERQSALDELELQL 529
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
133-316 3.13e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSK 212
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 213 LER---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG3883   105 LDVllgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
                         170       180
                  ....*....|....*....|....*..
gi 1212626334 290 KEKLQEKVKATNTQHAVEAISLESVSA 316
Cdd:COG3883   180 QEALLAQLSAEEAAAEAQLAELEAELA 206
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
81-409 3.39e-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: 40.09  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgntKNHREDRSEIERLTAKIEEFRQKSLD-WEKQ 159
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDLQIATKTICQLTEEKEAQMEeLNKA 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 160 RLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELssqsEIQHLSSKLERANDTICANELEIERLTmrvndlvg 239
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEELK-------- 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 240 tsmTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ-------KEKLQEKVKATNTQHAVEAISLE 312
Cdd:pfam05483 412 ---KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiktsEEHYLKEVEDLKTELEKEKLKNI 488
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 313 SVSATCKQLSQELMEKYEELKRMEAHNNEYKAEI---KKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTK 389
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
                         330       340
                  ....*....|....*....|
gi 1212626334 390 GSSSDMEKRLRAEMQKAEDK 409
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQ 588
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
81-425 3.98e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 160
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  161 liyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 240
Cdd:pfam02463  260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  241 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ 320
Cdd:pfam02463  337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  321 LSQELMEKYEELKR------MEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD 394
Cdd:pfam02463  414 ARQLEDLLKEEKKEeleileEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1212626334  395 MEKRLRAEMQKAEDKAVEHKEILDQLESLKL 425
Cdd:pfam02463  494 KLEERSQKESKARSGLKVLLALIKDGVGGRI 524
COG5022 COG5022
Myosin heavy chain [General function prediction only];
87-438 4.29e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   87 KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhREDRSEIerltakIEEFRQKSLDWEKQRLIYQQQ 166
Cdd:COG5022    825 TIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS--------LLKKETI------YLQSAQRVELAERQLQELKID 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  167 VSSLEAqrkaLAEQSEIIQAQLVNRKQKLESVELSsQSEIQ-HLSSKLERANDTIcanELEIERLTMrvndlvgtsmtvl 245
Cdd:COG5022    891 VKSISS----LKLVNLELESEIIELKKSLSSDLIE-NLEFKtELIARLKKLLNNI---DLEEGPSIE------------- 949
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  246 QEQQQKEEKLRESEKlleALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaislesvsatcKQLSQEL 325
Cdd:COG5022    950 YVKLPELNKLHEVES---KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAEL---------------SKQYGAL 1011
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  326 MEKYEELKRMEAHNNEYKAEIKKLKEqilqgEQSYSSALEGMKMEISHLTQELHQrdiTIASTKGSSSDMEKRLRAEMQK 405
Cdd:COG5022   1012 QESTKQLKELPVEVAELQSASKIISS-----ESTELSILKPLQKLKGLLLLENNQ---LQARYKALKLRRENSLLDDKQL 1083
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1212626334  406 AEDKAVEHKEILDQLESLKLENRHLSEMVMKLE 438
Cdd:COG5022   1084 YQLESTENLLKTINVKDLEVTNRNLVKPANVLQ 1116
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
165-430 4.66e-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: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  165 QQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTIcanELEIERLTMRvndLVGTSMTV 244
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQ---LVLANSEL 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  245 LQEQQQKEEKLRESEKLLEALQEekreLKAALQSQENLIHEARIQKEKLQEKVKATntqhaveaislesvSATCKQLSQE 324
Cdd:pfam15921  359 TEARTERDQFSQESGNLDDQLQK----LLADLHKREKELSLEKEQNKRLWDRDTGN--------------SITIDHLRRE 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ----------SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD 394
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1212626334  395 MEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHL 430
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHL 543
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
22-438 4.66e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   22 EAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQ 98
Cdd:pfam01576   52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   99 ELKKLHEELCILKRSYEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 178
Cdd:pfam01576  132 KIKKLEEDILLLEDQNSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  179 eQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREs 258
Cdd:pfam01576  198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE- 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  259 ekLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAH 338
Cdd:pfam01576  276 --LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  339 NNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHqrdiTIASTKGSSSDMEKRLRAEMQ----KAEDKAVEHK 414
Cdd:pfam01576  354 HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDSEHKRKKLEGQLQelqaRLSESERQRA 429
                          410       420
                   ....*....|....*....|....
gi 1212626334  415 EILDQLESLKLENRHLSEMVMKLE 438
Cdd:pfam01576  430 ELAEKLSKLQSELESVSSLLNEAE 453
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
245-414 5.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKAtnTQHAVEAISLESVSATCKQLSQE 324
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLEE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS----SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR 400
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
                         170
                  ....*....|....
gi 1212626334 401 AEMQKAEDKAVEHK 414
Cdd:COG4717   231 QLENELEAAALEER 244
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
97-299 7.66e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 38.90  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  97 KQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQ--------KSLDWEKQRLIYQQQV- 167
Cdd:COG0497   157 LEEYREAYRAWRALKKELEELRADE-----------AERARELDLLRFQLEELEAaalqpgeeEELEEERRRLSNAEKLr 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVE-------------LSSQSEIQHLSSKLERANDTICANELEIERLTMRV 234
Cdd:COG0497   226 EALQEALEALSGGEGGALDLLGQALRALERLAeydpslaelaerlESALIELEEAASELRRYLDSLEFDPERLEEVEERL 305
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212626334 235 NDLVGTS----------MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK-EKLQEKVKA 299
Cdd:COG0497   306 ALLRRLArkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
86-293 7.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQ--KKQMREFRGNTKNHREDRSEIERLTAKIEEFRQK--SLDWEKQRL 161
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 162 IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElSSQSEIQHLSSKLERANDTIC-ANELEIERLTMRVNDLvgt 240
Cdd:COG4717   129 PLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL--- 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1212626334 241 smtvlqeQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:COG4717   205 -------QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-286 8.28e-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: 38.90  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334   41 SEWEGRTHALETCLKIREQELKSLRSQLdvthkevgmlhqqveEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKK 120
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEI---------------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  121 QMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLvnRKQKLESVEL 200
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK--GEDEEIPEEE 950
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  201 SSQSEIQhlssklerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQE 280
Cdd:TIGR02169  951 LSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013

                   ....*.
gi 1212626334  281 NLIHEA 286
Cdd:TIGR02169 1014 KKKREV 1019
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
159-436 8.77e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 8.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  159 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLvNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 237
Cdd:pfam12128  588 KRIDVPEWAASEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  238 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELKAALQSQENLIHEARIQK-EKLQEKVKATNTQHA--VEAISLESV 314
Cdd:pfam12128  667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  315 SATCKQ-----------------------LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEI 371
Cdd:pfam12128  744 GAKAELkaletwykrdlaslgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI 823
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334  372 SHLTQELHQ-------RDITIASTKGSSSDMEKR-------LRAEMQK---------AEDKAVEHKEILDQLESLKLENR 428
Cdd:pfam12128  824 SELQQQLARliadtklRRAKLEMERKASEKQQVRlsenlrgLRCEMSKlatlkedanSEQAQGSIGERLAQLEDLKLKRD 903

                   ....*...
gi 1212626334  429 HLSEMVMK 436
Cdd:pfam12128  904 YLSESVKK 911
PRK12704 PRK12704
phosphodiesterase; Provisional
160-354 9.46e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 160 RLIYQQQVSSLEAQRKALAEQSEIiQAQLVNRKQKLESvelssQSEIQHLSSKLERandticanELEIERltmrvndlvg 239
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRILEEAKK-EAEAIKKEALLEA-----KEEIHKLRNEFEK--------ELRERR---------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626334 240 tsmtvlQEQQQKEEKLRESEKLL----EALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVS 315
Cdd:PRK12704   82 ------NELQKLEKRLLQKEENLdrklELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE-------LERIS 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1212626334 316 A-TCKQLSQELMEKYEELKRMEA------HNNEYKAEIKKLKEQIL 354
Cdd:PRK12704  149 GlTAEEAKEILLEKVEEEARHEAavlikeIEEEAKEEADKKAKEIL 194
 
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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