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Conserved domains on  [gi|1212626336|ref|NP_001340054|]
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centrosomal protein of 63 kDa isoform h [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 ...
 1-252 1.29e-82

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: 255.90  E-value: 1.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   1 MKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELC 80
Cdd:pfam17045  12 MKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  81 ILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQA-- 158
Cdd:pfam17045  92 KLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQSSLIQSaa 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 159 ---QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLE 235
Cdd:pfam17045 172 yqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247

                         250
                  ....*....|....*..
gi 1212626336 236 ALQEEKRELKAALQSQE 252
Cdd:pfam17045 248 VLQNELMELKATLQSQD 264
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-413 2.74e-10

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: 62.65  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 135 YQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 213
Cdd:COG1196   218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 214 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQL 293
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 294 SQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRA 373
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1212626336 374 EMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 413
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
 1-252 1.29e-82

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: 255.90  E-value: 1.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   1 MKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELC 80
Cdd:pfam17045  12 MKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  81 ILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQA-- 158
Cdd:pfam17045  92 KLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQSSLIQSaa 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 159 ---QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLE 235
Cdd:pfam17045 172 yqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247

                         250
                  ....*....|....*..
gi 1212626336 236 ALQEEKRELKAALQSQE 252
Cdd:pfam17045 248 VLQNELMELKATLQSQD 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-309 2.74e-11

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: 65.86  E-value: 2.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   27 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRE 106
Cdd:TIGR02169  219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  107 DRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSS 183
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  184 KLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKE 263
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1212626336  264 KLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEELKRMEA 309
Cdd:TIGR02169  459 QLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQRELAEAEA 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-413 2.74e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 135 YQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 213
Cdd:COG1196   218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 214 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQL 293
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 294 SQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRA 373
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1212626336 374 EMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 413
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-337 2.42e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  67 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 147 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 226
Cdd:COG1196   312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 227 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 306
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1212626336 307 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 337
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-413 4.12e-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: 52.75  E-value: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  186 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 265
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  266 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 345
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626336  346 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 413
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
50-410 8.79e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  50 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 124
Cdd:PRK02224  192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 125 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 194
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 195 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 267
Cdd:PRK02224  347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 268 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 333
Cdd:PRK02224  427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 334 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 407
Cdd:PRK02224  507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586


                  ...
gi 1212626336 408 KLE 410
Cdd:PRK02224  587 RIE 589
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 205-324 4.30e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 205 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKATnTQHAVEA 280
Cdd:PRK00409  517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1212626336 281 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 324
Cdd:PRK00409  590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
 
Name Accession Description Interval E-value
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
 1-252 1.29e-82

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: 255.90  E-value: 1.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   1 MKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELC 80
Cdd:pfam17045  12 MKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  81 ILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQA-- 158
Cdd:pfam17045  92 KLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQSSLIQSaa 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 159 ---QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLE 235
Cdd:pfam17045 172 yqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247

                         250
                  ....*....|....*..
gi 1212626336 236 ALQEEKRELKAALQSQE 252
Cdd:pfam17045 248 VLQNELMELKATLQSQD 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-309 2.74e-11

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: 65.86  E-value: 2.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   27 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRE 106
Cdd:TIGR02169  219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  107 DRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSS 183
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  184 KLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKE 263
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1212626336  264 KLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEELKRMEA 309
Cdd:TIGR02169  459 QLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQRELAEAEA 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-413 2.74e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 135 YQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 213
Cdd:COG1196   218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 214 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQL 293
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 294 SQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRA 373
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1212626336 374 EMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 413
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-337 2.42e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  67 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 147 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 226
Cdd:COG1196   312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 227 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 306
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1212626336 307 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 337
Cdd:COG1196   468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-390 3.74e-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: 59.30  E-value: 3.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  108 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 187
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  188 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL--------------QSQEN 253
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  254 LIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIlqgeQSYS 333
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL----RELE 907

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1212626336  334 SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 390
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-337 7.73e-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: 58.14  E-value: 7.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336    9 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 88
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   89 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 168
Cdd:TIGR02168  304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  169 SVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL-----LEALQEEKRE 243
Cdd:TIGR02168  376 ELE----EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEE 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  244 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaiSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE 323
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527

                          330
                   ....*....|....
gi 1212626336  324 QIlQGEQSYSSALE 337
Cdd:TIGR02168  528 LI-SVDEGYEAAIE 540
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-327 4.58e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 4.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   58 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 137
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  138 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 216
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  217 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQE 296
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKE 890

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1212626336  297 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 327
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSE 921
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-413 4.12e-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: 52.75  E-value: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  186 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 265
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  266 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 345
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626336  346 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 413
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-305 5.56e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 108 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 180
Cdd:COG3206   188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 181 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENlihea 258
Cdd:COG3206   268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQA----- 334

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1212626336 259 riQKEKLQEKVKATNtQHAVEAISLESVSATCKQLSQELMEKYEELK 305
Cdd:COG3206   335 --QLAQLEARLAELP-ELEAELRRLEREVEVARELYESLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-271 3.67e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   70 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLI-YQQQVSSLEAQRK 147
Cdd:COG4913    235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEeLRAELARLEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  148 ALAEQSEIIQAQLVNRKQKLESvelSSQSEIQHLSSKLERANDTIcaneLEIERLTMRVNDLVGT-SMTVLQEQQQKEEK 226
Cdd:COG4913    313 RLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLEREL----EERERRRARLEALLAAlGLPLPASAEEFAAL 385

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1212626336  227 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKA 271
Cdd:COG4913    386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 129-426 4.93e-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: 49.28  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  129 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 208
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  209 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAI---SLES 285
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  286 VSATCKQLSQELMEKY-----------EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA-LEGMKMEISHLTQELHQ- 352
Cdd:TIGR02168  373 RLEELEEQLETLRSKVaqlelqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEEl 452

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212626336  353 --RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECSLPVSPLGSI 426
Cdd:TIGR02168  453 qeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
50-410 8.79e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  50 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 124
Cdd:PRK02224  192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 125 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 194
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 195 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 267
Cdd:PRK02224  347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 268 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 333
Cdd:PRK02224  427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 334 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 407
Cdd:PRK02224  507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586


                  ...
gi 1212626336 408 KLE 410
Cdd:PRK02224  587 RIE 589
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-324 1.04e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336    7 MVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVE----EHEKIKQEMT-------------MEYK 69
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLEeleedlssleqeiENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   70 QELKKLHEELCILKRSYEKLQKkqmrefrgntknhredrsEIERLTAKIEEFRQKSLdwekqrliyQQQVSSLEAQRKAL 149
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEE------------------ALNDLEARLSHSRIPEI---------QAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  150 AEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRE 229
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLE----KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEELEAALRD 879

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  230 SEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV--------------------EAISLESVSAT 289
Cdd:TIGR02169  880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleeelseiedpkgedeeipeEELSLEDVQAE 959

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1212626336  290 CKQLSQEL-------MEKYEELKRMEAHNNEYKAEIKKLKEQ 324
Cdd:TIGR02169  960 LQRVEEEIralepvnMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 219-458 1.09e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  219 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELM 298
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  299 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSAlegmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 378
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  379 EDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECslpvspLGSIATRFLEEEELRSHHI-----LERLDAHIEELK 453
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL------EEELEELEAALRDLESRLGdlkkeRDELEAQLRELE 902


                   ....*
gi 1212626336  454 RESEK 458
Cdd:TIGR02169  903 RKIEE 907
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-318 1.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  115 TAKIEEFRQksldwEKQRLiyQQQVSSLEAQRKALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERAndticA 194
Cdd:COG4913    609 RAKLAALEA-----ELAEL--EEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVASAEREIA-----E 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  195 NELEIERLTMRVNDLvgtsmTVLQEQ-QQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATN 273
Cdd:COG4913    673 LEAELERLDASSDDL-----AALEEQlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1212626336  274 TQHAVEAISLESVSATCKQLSQELMEKYEELKR------------MEAHNNEYKAEI 318
Cdd:COG4913    748 RALLEERFAAALGDAVERELRENLEERIDALRArlnraeeeleraMRAFNREWPAET 804
mukB PRK04863
chromosome partition protein MukB;
30-327 1.57e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   30 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 89
Cdd:PRK04863   389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   90 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 165
Cdd:PRK04863   466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  166 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 245
Cdd:PRK04863   544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  246 AALqsqenliheariqkEKLQEKVKATntqhaveaisLESvSATCKQLSQELMEKYEELKRmeaHNNEYKAEIKKLKEQI 325
Cdd:PRK04863   610 DAL--------------ARLREQSGEE----------FED-SQDVTEYMQQLLERERELTV---ERDELAARKQALDEEI 661


                   ..
gi 1212626336  326 LQ 327
Cdd:PRK04863   662 ER 663
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-325 2.01e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  67 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 146
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 147 KALAEQSEIIQAQLVNRKQKLESveLSSQSEIQHLSSKlerandticANELEIERLTMRVNDLVgtsmtvlQEQQQKEEK 226
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYLA-------PARREQAEE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 227 LRESeklLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatckQLSQELMEKYEELKR 306
Cdd:COG4942   155 LRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAE 217

                         250
                  ....*....|....*....
gi 1212626336 307 MEAHNNEYKAEIKKLKEQI 325
Cdd:COG4942   218 LQQEAEELEALIARLEAEA 236
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-325 3.84e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  26 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNhR 105
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 106 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLVNRKQKLESVELSSQSE 177
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 178 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ------ 251
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikd 444

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1212626336 252 -ENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 325
Cdd:TIGR04523 445 lTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 205-324 4.30e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 205 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKATnTQHAVEA 280
Cdd:PRK00409  517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1212626336 281 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 324
Cdd:PRK00409  590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
163-409 6.28e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 163 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 242
Cdd:PRK02224  476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 243 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYKA 316
Cdd:PRK02224  548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 317 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVEHKEI---L 389
Cdd:PRK02224  628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALenrV 707

                         250       260
                  ....*....|....*....|
gi 1212626336 390 DQLESLKLENRHLSEMVMKL 409
Cdd:PRK02224  708 EALEALYDEAEELESMYGDL 727
46 PHA02562
endonuclease subunit; Provisional
 175-408 7.97e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 175 QSEIQHLSSKLERANDTICANELEIERltmrvndlvgtsmtvlQEQQQKEEKLRESEKLLEALQEEKrELKAALQSQENL 254
Cdd:PHA02562  180 NQQIQTLDMKIDHIQQQIKTYNKNIEE----------------QRKKNGENIARKQNKYDELVEEAK-TIKAEIEELTDE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 255 IHEARIQKEKLQEKVKATNTQHAVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 325
Cdd:PHA02562  243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 326 LQGEQSYSSALEgMKMEISHLTQELHQRDITIASTKGSSsdmeKRLRAEMQKAEDKAVEHKEILDQL-ESLKLENRHLSE 404
Cdd:PHA02562  323 DELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSE 397


                  ....
gi 1212626336 405 MVMK 408
Cdd:PHA02562  398 LVKE 401
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 135-308 9.96e-04

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: 41.25  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 135 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSm 214
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 215 tvlqeqqqkEEKLRESEKLLEAlqeekrelKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS-LESVSATCKQL 293
Cdd:pfam00529 134 ---------PIGGISRESLVTA--------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEA 196

                         170
                  ....*....|....*
gi 1212626336 294 SQELMEKYEELKRME 308
Cdd:pfam00529 197 EAELKLAKLDLERTE 211
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 218-349 1.50e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 218 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS--LESVSATCKQLSQ 295
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLED 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1212626336 296 ELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQE 349
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 136-335 1.81e-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: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 136 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSKLERANDTICANELEIERLTMRVNDLV----- 210
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAELEELNEEYNEL----QAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 211 -GTSMTVLQ------------EQQQKEEKLRESEK-LLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQH 276
Cdd:COG3883    98 sGGSVSYLDvllgsesfsdflDRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626336 277 AVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA 335
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 30-297 1.81e-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: 40.93  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   30 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 104
Cdd:pfam01576  318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  105 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 181
Cdd:pfam01576  387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  182 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 261
Cdd:pfam01576  467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1212626336  262 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQEL 297
Cdd:pfam01576  547 KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 12-443 1.91e-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: 40.87  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   12 KSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQK 91
Cdd:pfam15921  337 KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK-----------LLADLHKREKELSLEKEQNKRLWD 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   92 KQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQKSLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQ 157
Cdd:pfam15921  406 RDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSECQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVV 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  158 AQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANELEIERLTMRVNdlvgTSMTVLQEQQQKEEKLR--------- 228
Cdd:pfam15921  482 EELTAKKMTLES----SERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKLQELQHLKNEGDHLRnvqteceal 553

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  229 -----ESEKLLE---------------------ALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAIS 282
Cdd:pfam15921  554 klqmaEKDKVIEilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR--VSDLE 631

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  283 LESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQR 353
Cdd:pfam15921  632 LEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  354 DITIASTKGSSSD-------MEKRLRAEM-----------------------------------QKAEDKAVEHKEILDQ 391
Cdd:pfam15921  712 RNTLKSMEGSDGHamkvamgMQKQITAKRgqidalqskiqfleeamtnankekhflkeeknklsQELSTVATEKNKMAGE 791

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1212626336  392 LESLKLENRHLSEMVMKLELGLHECSLPVSPLGSIATRFLEEE-ELRSHHILE 443
Cdd:pfam15921  792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESvRLKLQHTLD 844
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
136-330 1.91e-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: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  136 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 215
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  216 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ-LS 294
Cdd:COG4913    670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLR 748

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1212626336  295 QELMEKYEELKRMEAHN---NEYKAEIKKLKEQILQGEQ 330
Cdd:COG4913    749 ALLEERFAAALGDAVERelrENLEERIDALRARLNRAEE 787
PRK09039 PRK09039
peptidoglycan -binding protein;
165-306 2.35e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 165 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 243
Cdd:PRK09039   41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1212626336 244 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ--------HAVEAISLES---VSATCKQLSQELMEKYEELKR 306
Cdd:PRK09039  121 LAQELDSEKQVSARALAQVELLNQQIAALRRQlaaleaalDASEKRDRESqakIADLGRRLNVALAQRVQELNR 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 225-402 2.55e-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: 40.13  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 225 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQELMEKYEEL 304
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 305 KRMEAHNNEYKAEIKK-LKEQILQGEQSY---------SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAE 374
Cdd:COG4942    93 AELRAELEAQKEELAElLRALYRLGRQPPlalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180
                  ....*....|....*....|....*...
gi 1212626336 375 MQKAEDKAVEHKEILDQLESLKLENRHL 402
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKL 200
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 105-288 3.08e-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: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 105 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSK 184
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 185 LER---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 261
Cdd:COG3883   105 LDVllgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179

                         170       180
                  ....*....|....*....|....*..
gi 1212626336 262 KEKLQEKVKATNTQHAVEAISLESVSA 288
Cdd:COG3883   180 QEALLAQLSAEEAAAEAQLAELEAELA 206
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-255 3.37e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  50 LHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQK--SLD 127
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEEL--------KEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 128 WEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElSSQSEIQHLSSKLERANDTIC-ANELEIERLTMRV 206
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSlATEEELQDLAEEL 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1212626336 207 NDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLI 255
Cdd:COG4717   202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-192 5.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   21 ALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYKQELKKLHEELCILKRSYEKLQKKQMREFR 98
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   99 GNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKL-ESVELSSQ 175
Cdd:COG4913    769 ENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPEYLALLDRLEEDGLPEYEERFkELLNENSI 845

                          170
                   ....*....|....*..
gi 1212626336  176 SEIQHLSSKLERANDTI 192
Cdd:COG4913    846 EFVADLLSKLRRAIREI 862
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 205-466 8.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  205 RVNDL---VGTSMTVLQEQQQKEEKLREseklleaLQEEKRELKAALQSQEnlIHEARIQKEKLQEKVKATNTQHAVEAI 281
Cdd:TIGR02168  190 RLEDIlneLERQLKSLERQAEKAERYKE-------LKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  282 SLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSyssalegmkmeISHLTQELHQRDITIASTK 361
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-----------LANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  362 GSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECSlpvsplGSIATRFLEEEELRSHhi 441
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR------SKVAQLELQIASLNNE-- 401

                          250       260
                   ....*....|....*....|....*
gi 1212626336  442 LERLDAHIEELKRESEKTVRQFTAL 466
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEEL 426
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 33-325 8.94e-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: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336   33 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 108
Cdd:pfam12128  253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  109 SEIERLTAKIEEFRQKSLDwekqrlIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERA 188
Cdd:pfam12128  322 SELEALEDQHGAFLDADIE------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  189 NDTICANELEIERLTMRVNDLVGTSMTVLQEQ--QQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEAriQKEKLQ 266
Cdd:pfam12128  396 KDKLAKIREARDRQLAVAEDDLQALESELREQleAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE--NFDERI 473

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626336  267 EKVKATNTQHAVEAISLESVSATCKQLSQELMEKyeeLKRMEAHNNEYKAEIKKLKEQI 325
Cdd:pfam12128  474 ERAREEQEAANAEVERLQSELRQARKRRDQASEA---LRQASRRLEERQSALDELELQL 529
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
87-281 9.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336  87 EKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDW---EKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNR 163
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626336 164 KQKLESVELssQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 243
Cdd:COG4717   129 PLYQELEAL--EAELAELPERLEELEERLEELRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAEELEE 203

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1212626336 244 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAI 281
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
 
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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