|
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 |
6.97e-99 |
|
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: 303.67 E-value: 6.97e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1034635722 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 |
1.91e-13 |
|
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: 73.95 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169 340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEEL 332
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQREL 492
|
....*
gi 1034635722 333 KRMEA 337
Cdd:TIGR02169 493 AEAEA 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-454 |
1.49e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 139 IERLTAKIEEFRQ--KSLdwEKQR------LIYQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:COG1196 188 LERLEDILGELERqlEPL--ERQAekaeryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 290 KEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQsyssalegmkm 369
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 370 EISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISL 449
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
....*
gi 1034635722 450 ADLQE 454
Cdd:COG1196 495 LLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-463 |
2.21e-11 |
|
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: 67.39 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 215
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 216 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQE 295
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 296 KVKATntqhaveAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLT 375
Cdd:TIGR02168 832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 376 QELHQRditiastkgsssdmeKRLRAEMQKAEDKAVEHKEildQLESLKLENRHLSEMVM---KLELGLHEAKEISLADL 452
Cdd:TIGR02168 905 ELESKR---------------SELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSeeySLTLEEAEALENKIEDD 966
|
330
....*....|.
gi 1034635722 453 QENYIEALNKL 463
Cdd:TIGR02168 967 EEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-355 |
5.39e-11 |
|
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: 66.23 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 57 REQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEelcilkrsyeklqkkQMREFRGNTKNHREDR 136
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE---------------LSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 137 SEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERA 216
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 217 NDTICANELEIERLTMRVNDlvgtsmtvlqeqqqKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEK 296
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAA--------------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635722 297 VKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 355
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-365 |
5.96e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 175 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG1196 312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270
....*....|....*....|....*....|.
gi 1034635722 335 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 365
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-365 |
9.00e-11 |
|
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: 65.46 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 37 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 116
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 117 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 196
Cdd:TIGR02168 304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 197 SVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL-----LEALQEEKRE 271
Cdd:TIGR02168 376 ELE----EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaiSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE 351
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330
....*....|....
gi 1034635722 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 |
1.06e-10 |
|
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: 65.09 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 166 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKatNTQHAVeaislesvsatcKQLSQE 324
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELE--ELEAAL------------RDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS---SALEGMKMEISHLtQELHQRDITIASTKGSSSDMEKRLR- 400
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQr 962
|
330 340 350
....*....|....*....|....*....|
gi 1034635722 401 --AEMQKAED---KAV-EHKEILDQLESLK 424
Cdd:TIGR02169 963 veEEIRALEPvnmLAIqEYEEVLKRLDELK 992
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-482 |
4.73e-10 |
|
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: 63.15 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 214 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 294 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 373
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 374 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI------ 447
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNEraslee 887
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034635722 448 ---SLADLQENYIEALNKLVSENQQLQKDLMNTKSQLE 482
Cdd:TIGR02168 888 alaLLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-487 |
4.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 170 LEAQRKALAEQSEI------IQAQLVNRKQKLesvelsSQSEIQHLSSKLERANDTICANELEIERLTmrvndlvgtsmt 243
Cdd:COG1196 198 LERQLEPLERQAEKaeryreLKEELKELEAEL------LLLKLRELEAELEELEAELEELEAELEELE------------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 244 vlQEQQQKEEKLRES-------EKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSA 316
Cdd:COG1196 260 --AELAELEAELEELrleleelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 317 TCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEgmkmEISHLTQELHQRDITIASTKGSSSDME 396
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 397 KRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELgLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMN 476
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330
....*....|.
gi 1034635722 477 TKSQLEISTQM 487
Cdd:COG1196 493 LLLLLEAEADY 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-471 |
1.50e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 296 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 361
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 362 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 435
Cdd:PRK02224 507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430
....*....|....*....|....*....|....*.
gi 1034635722 436 KLElglHEAKEISLADLQENYIEALNKLVSENQQLQ 471
Cdd:PRK02224 587 RIE---SLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-333 |
2.34e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENlihea 286
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQA----- 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034635722 287 riQKEKLQEKVKATNtQHAVEAISLESVSATCKQLSQELMEKYEELK 333
Cdd:COG3206 335 --QLAQLEARLAELP-ELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-352 |
6.54e-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: 56.23 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 14 GGGFLTSCEAELQELMKQIDIM------VAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHE- 86
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEe 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 87 --KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKkqmrefrgntknhredrsEIERLTAKIEEFRQKSLdwekqrliyQ 164
Cdd:TIGR02169 745 dlSSLEQEIENVKSELKELEARIEELEEDLHKLEE------------------ALNDLEARLSHSRIPEI---------Q 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 165 QQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV------------------ 306
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleeelseiedpkgedeei 946
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034635722 307 --EAISLESVSATCKQLSQEL-------MEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:TIGR02169 947 peEELSLEDVQAELQRVEEEIralepvnMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-439 |
2.26e-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: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 157 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 236
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 237 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAI---SLES 313
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 314 VSATCKQLSQELMEKY-----------EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA-LEGMKMEISHLTQELHQ- 380
Cdd:TIGR02168 373 RLEELEEQLETLRSKVaqlelqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEEl 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635722 381 --RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLEL 439
Cdd:TIGR02168 453 qeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-482 |
2.99e-07 |
|
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: 53.92 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELM 326
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 327 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSAlegmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 406
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034635722 407 EDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEIsladlQENYIEALNKLVSENQQLQKDLMNTKSQLE 482
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
245-495 |
1.01e-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: 52.38 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS-LESVSATCKQLSQ 323
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 324 ELMEKYEELKRMEAHNNEYKAEIKKLKEQI--LQGEQ--------SYSSALEGMKMEISHLTQELHQRDITIASTKGSSS 393
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIeeLEREIeeerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 394 DMEKRLraemqkaEDKAVEHKEILDQLESLKLENRHLSEMV--MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQ 471
Cdd:TIGR02169 389 DYREKL-------EKLKREINELKRELDRLQEELQRLSEELadLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
250 260
....*....|....*....|....
gi 1034635722 472 KDLMNTKSQLEISTQMCKKQNDRI 495
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-479 |
1.80e-06 |
|
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: 51.17 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNhR 133
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 134 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLVNRKQKLESVELSSQSE 205
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 206 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ------ 279
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikd 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 280 -ENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI---LQ 355
Cdd:TIGR04523 445 lTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslKE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 356 GEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEK-----RLRAEMQKAEDKAVEHKEILDQLESLKLENRHL 430
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1034635722 431 SEMVMKL------ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKS 479
Cdd:TIGR04523 605 IEEKEKKisslekELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-353 |
2.53e-06 |
|
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: 50.15 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 175 KALAEQSEIIQAQLVNRKQKLESveLSSQSEIQHLSSKlerandticANELEIERLTMRVNDLVgtsmtvlQEQQQKEEK 254
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYLA-------PARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 255 LRESeklLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatckQLSQELMEKYEELKR 334
Cdd:COG4942 155 LRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAE 217
|
250
....*....|....*....
gi 1034635722 335 MEAHNNEYKAEIKKLKEQI 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEA 236
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-466 |
2.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYKA 344
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 345 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLraemqkaedKAVEHKeiLDQLESL 423
Cdd:PRK02224 628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI---------GAVENE--LEELEEL 696
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034635722 424 KLENRHLSEMVMKLELGLHEAKEIS------LADLQENYIEALNKLVSE 466
Cdd:PRK02224 697 RERREALENRVEALEALYDEAEELEsmygdlRAELRQRNVETLERMLNE 745
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-355 |
3.61e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 58 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 117
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 193
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 273
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 274 AALqsqenliheariqkEKLQEKVKATntqhaveaisLESvSATCKQLSQELMEKYEELKRmeaHNNEYKAEIKKLKEQI 353
Cdd:PRK04863 610 DAL--------------ARLREQSGEE----------FED-SQDVTEYMQQLLERERELTV---ERDELAARKQALDEEI 661
|
..
gi 1034635722 354 LQ 355
Cdd:PRK04863 662 ER 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-391 |
4.57e-06 |
|
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: 50.12 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 1 MEALLEGIQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLH 79
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 80 QQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921 377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921 442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 226 EIERLTMRVNdlvgTSMTVLQEQQQKEEKLR--------------ESEKLLE---------------------ALQEEKR 270
Cdd:pfam15921 518 EITKLRSRVD----LKLQELQHLKNEGDHLRnvqtecealklqmaEKDKVIEilrqqienmtqlvgqhgrtagAMQVEKA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEAR--VSDLELEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNS 671
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1034635722 342 YKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGS 391
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS 721
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-494 |
4.98e-06 |
|
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: 50.12 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 165 QQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTIcanELEIERLTMRvndLVGTSMTV 244
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQ---LVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 245 LQEQQQKEEKLRESEKLLEALQEekreLKAALQSQENLIHEARIQKEKLQEKVKATntqhaveaislesvSATCKQLSQE 324
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQK----LLADLHKREKELSLEKEQNKRLWDRDTGN--------------SITIDHLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQ----------SYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD 394
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 395 MEKRLRAEMQKAEDKAVEHKEI-------LDQLESLKLENRHLSEMVMKLE-LGLHEAKEISLADLQENYIEALNKLVSE 466
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHLRNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
330 340
....*....|....*....|....*...
gi 1034635722 467 NQQLQKDLMNTKSQLEistqmcKKQNDR 494
Cdd:pfam15921 581 HGRTAGAMQVEKAQLE------KEINDR 602
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-447 |
5.11e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 134 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 196
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 197 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 275
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 276 LQSQENLIHEARIQ-KEKLQEKVKATNtqhavEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 354
Cdd:PRK03918 576 LKELEELGFESVEElEERLKELEPFYN-----EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 355 QGEQSYS-SALEGMKMEISHLTQELhqrditiastkgsssdmeKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEM 433
Cdd:PRK03918 651 ELEKKYSeEEYEELREEYLELSREL------------------AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
410
....*....|....
gi 1034635722 434 VMKLELGLHEAKEI 447
Cdd:PRK03918 713 LEKLEKALERVEEL 726
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-495 |
1.55e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 89 KQEMTMEYKQELKKLHEELCILKRSYEKLqKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQrliYQQQVS 168
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF---ISEILK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 169 SLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERAND-------TICANELEIERLTMRVNDLVgts 241
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcPVCGTTLGEEKSNHIINHYN--- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 242 mtvlQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlihEARIQKEKLQEKVKATNtqhaveaiSLESVSATCKql 321
Cdd:PRK01156 476 ----EKKSRLEEKIREIEIEVKDIDEKIVDLKKR---------KEYLESEEINKSINEYN--------KIESARADLE-- 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 322 sqELMEKYEELKRMEAHNNEYKAEIKKLKEQILqgEQSYSSALEGM------------------KMEISHLTQELHQRDI 383
Cdd:PRK01156 533 --DIKIKINELKDKHDKYEEIKNRYKSLKLEDL--DSKRTSWLNALavislidietnrsrsneiKKQLNDLESRLQEIEI 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 384 TIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENyiEALNKL 463
Cdd:PRK01156 609 GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE--DNLKKS 686
|
410 420 430
....*....|....*....|....*....|..
gi 1034635722 464 VSENQQLQKDLMNTKSQLEISTQMCKKQNDRI 495
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-325 |
1.55e-05 |
|
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: 48.25 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 58 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034635722 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 |
3.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 246 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS--LESVSATCKQLSQ 323
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034635722 324 ELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQE 377
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-346 |
4.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLVNRKQKLESVELSSqSEI 206
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALqsqenlihea 286
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---------- 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635722 287 riqkekLQEKVKATNTQHAVEAISlESVSATCKQLSQELMEKYEEL-KRMEAHNNEYKAEI 346
Cdd:COG4913 751 ------LEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELeRAMRAFNREWPAET 804
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-466 |
6.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 39 KKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT------MEYKQELKKLHEELCILKR 112
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 113 SYEKLQK--KQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS--------- 181
Cdd:PRK03918 267 RIEELKKeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerleelkkk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 182 -EIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEK 260
Cdd:PRK03918 347 lKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 261 LLEALQEEK-------------------RELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEA--ISLESVSATCK 319
Cdd:PRK03918 427 AIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 320 QLS--------QELMEKYEELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISHLTQELHQRdITIASTKGS 391
Cdd:PRK03918 507 ELEeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEEELAEL-LKELEELGF 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 392 SS--DMEKRLRaEMQKAEDKAVE----HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEIsladlqENYIEALNKLVS 465
Cdd:PRK03918 585 ESveELEERLK-ELEPFYNEYLElkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEEL------RKELEELEKKYS 657
|
.
gi 1034635722 466 E 466
Cdd:PRK03918 658 E 658
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-425 |
7.62e-05 |
|
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: 46.12 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 160
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 161 liyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 240
Cdd:pfam02463 260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 241 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ 320
Cdd:pfam02463 337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 321 LSQELMEKYEELKR------MEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD 394
Cdd:pfam02463 414 ARQLEDLLKEEKKEeleileEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350
....*....|....*....|....*....|.
gi 1034635722 395 MEKRLRAEMQKAEDKAVEHKEILDQLESLKL 425
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-473 |
1.04e-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: 45.14 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQELMEKYEEL 332
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 333 KRMEAHNNEYKAEIKK-LKEQILQGEQSY---------SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAE 402
Cdd:COG4942 93 AELRAELEAQKEELAElLRALYRLGRQPPlalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635722 403 MQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLElglhEAKEISLADLQENYiEALNKLVSENQQLQKD 473
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKEL----AELAAELAELQQEA-EELEALIARLEAEAAA 238
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
233-352 |
1.19e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 233 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKATnTQHAVEA 308
Cdd:PRK00409 517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034635722 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:PRK00409 590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-453 |
1.19e-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: 45.55 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 22 EAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQ 98
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 99 ELKKLHEELCILKRSYEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 178
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 179 eQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREs 258
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 259 ekLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAH 338
Cdd:pfam01576 276 --LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 339 NNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHqrdiTIASTKGSSSDMEKRLRAEMQ----KAEDKAVEHK 414
Cdd:pfam01576 354 HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDSEHKRKKLEGQLQelqaRLSESERQRA 429
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034635722 415 EILDQLESLKLENRHLSEMVMKLELGLHE-AKEISLADLQ 453
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIKlSKDVSSLESQ 469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
164-363 |
1.29e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSKLERANDTICANELEIERLTMRVNDLV----- 238
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNEL----QAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 239 -GTSMTVLQ------------EQQQKEEKLRESEK-LLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQH 304
Cdd:COG3883 98 sGGSVSYLDvllgsesfsdflDRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635722 305 AVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA 363
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
81-483 |
1.31e-04 |
|
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: 45.10 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 81 QVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgntKNHREDRSEIERLTAKIEEFRQKSLD-WEKQ 159
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDLQIATKTICQLTEEKEAQMEeLNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 160 RLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELssqsEIQHLSSKLERANDTICANELEIERLTmrvndlvg 239
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEELK-------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 240 tsmTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ-------KEKLQEKVKATNTQHAVEAISLE 312
Cdd:pfam05483 412 ---KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiktsEEHYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 313 SVSATCKQLSQELMEKYEELKRMEAHNNEYKAEI---KKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTK 389
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 390 GSSSDMEKRLRAEMQKAEDKAVEHKEILDQL-ESLKLENRHLSEMVMK----LELGLHEAKEISLADLQENYIEAlnKLV 464
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLkKQIENKNKNIEELHQEnkalKKKGSAENKQLNAYEIKVNKLEL--ELA 646
|
410
....*....|....*....
gi 1034635722 465 SENQQLQKDLMNTKSQLEI 483
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIED 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-293 |
1.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQ--KKQMREFRGNTKNHREDRSEIERLTAKIEEFRQK--SLDWEKQRL 161
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 162 IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElSSQSEIQHLSSKLERANDTIC-ANELEIERLTMRVNDLvgt 240
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL--- 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034635722 241 smtvlqeQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:COG4717 205 -------QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
163-336 |
1.50e-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: 44.34 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 163 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSm 242
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 243 tvlqeqqqkEEKLRESEKLLEAlqeekrelKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS-LESVSATCKQL 321
Cdd:pfam00529 134 ---------PIGGISRESLVTA--------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEA 196
|
170
....*....|....*
gi 1034635722 322 SQELMEKYEELKRME 336
Cdd:pfam00529 197 EAELKLAKLDLERTE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-353 |
1.72e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 98 QELKKLHEELCILKRsyeklQKKQMREFRGNTKNHREDRSEIERLtakiEEFRQKSLDWEKQRLI--YQQQVSSLEAQRK 175
Cdd:COG4913 235 DDLERAHEALEDARE-----QIELLEPIRELAERYAAARERLAEL----EYLRAALRLWFAQRRLelLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 176 ALAEQSEIIQAQLVNRKQKLESVELssqseiQHLSSKLERandticaneleIERLTmrvndlvgtsmtvlQEQQQKEEKL 255
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEA------QIRGNGGDR-----------LEQLE--------------REIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 256 RESEKLLEALQEEKRELKAALQSQE----NLIHEARIQKEKLQEKVKATNTQHAvEAISLESvsatckQLSQELMEKYEE 331
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALA-EAEAALR------DLRRELRELEAE 427
|
250 260
....*....|....*....|..
gi 1034635722 332 LKRMEAHNNEYKAEIKKLKEQI 353
Cdd:COG4913 428 IASLERRKSNIPARLLALRDAL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-358 |
1.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 244 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ-LS 322
Cdd:COG4913 670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLR 748
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034635722 323 QELMEKYEELKRMEAHN---NEYKAEIKKLKEQILQGEQ 358
Cdd:COG4913 749 ALLEERFAAALGDAVERelrENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-493 |
2.25e-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: 44.24 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMT---MEYKQELKKLHEELCILKrSYEKLQKKQM-------- 122
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNdklKKNKDKINKLNSDLSKIN-SEIKNDKEQKnkleveln 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 123 ---REFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE 199
Cdd:TIGR04523 128 kleKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 200 LSSQ------SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQ-------QQKEEKLRESEKLLEALQ 266
Cdd:TIGR04523 208 KKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQnkikkqlSEKQKELEQNNKKIKELE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 267 EEKRELKAAL-----QSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:TIGR04523 288 KQLNQLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 342 YKAEIKKLKEQIlqgeQSYSSALEGMKMEISHLTQELHQRditiastKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLE 421
Cdd:TIGR04523 368 KQNEIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034635722 422 SLKLENRHLSEMVMKLELGLHEAKeiSLADLQENYIEALNKLVSENQQlqkDLMNTKSQLEISTQMCKKQND 493
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLD--NTRESLETQLKVLSRSINKIKQ---NLEQKQKELKSKEKELKKLNE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-316 |
2.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 136 RSEIERLTAKIEEFRQksldwEKQRLiyQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSKLER 215
Cdd:COG3883 36 QAELDALQAELEELNE-----EYNEL--QAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 216 ---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 292
Cdd:COG3883 108 llgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180
....*....|....*....|....
gi 1034635722 293 LQEKVKATNTQHAVEAISLESVSA 316
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELA 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-414 |
2.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKAtnTQHAVEAISLESVSATCKQLSQE 324
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS----SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR 400
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|....
gi 1034635722 401 AEMQKAEDKAVEHK 414
Cdd:COG4717 231 QLENELEAAALEER 244
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
203-436 |
3.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 203 QSEIQHLSSKLERANDTICANELEIERltmrvndlvgtsmtvlQEQQQKEEKLRESEKLLEALQEEKrELKAALQSQENL 282
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYNKNIEE----------------QRKKNGENIARKQNKYDELVEEAK-TIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 283 IHEARIQKEKLQEKVKATNTQHAVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 354 LQGEQSYSSALEgMKMEISHLTQELHQRDITIASTKGSSsdmeKRLRAEMQKAEDKAVEHKEILDQL-ESLKLENRHLSE 432
Cdd:PHA02562 323 DELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSE 397
|
....
gi 1034635722 433 MVMK 436
Cdd:PHA02562 398 LVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-220 |
3.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 20 SCEAELQELMKQIDIMVAhKKSEWEgrthALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYK 97
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 175
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034635722 176 ALAEQSEIIQAQLVNRKQKL-ESVELSSQSEIQHLSSKLERANDTI 220
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI 862
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-482 |
3.45e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 44 EGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVE--EHEKIKQEMTMEYKQELKKLHEELCILKRSYEKL-QKK 120
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 121 QMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAE-QSEIIQAQLVNRKQKLESVE 199
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 200 LSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ 279
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 280 ENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE------QI 353
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 354 LQGEQSYSSALEGMKMEISHLTQELHQRDITiastkgssSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEM 433
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASL--------KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034635722 434 VMKLELGLHEAKEISLADLQENyiEALNKLVSENQQLQKDLMNTKSQLE 482
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPE--QDLQDVRLHLQQCSQELALKLTALH 649
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
58-511 |
4.16e-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: 43.47 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 58 EQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYkQELKKLHEELcilkRSYEKLQKKQMREFRGNTKNHREDRS 137
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY-NDLKKQKEEL----ENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 138 EIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSK---LE 214
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 215 RANDTICANELEIERLTMRVNDLvgtsmtvlqEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQ 294
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDL---------NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 295 EKVKATNTQHaveaislesvsatcKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQsyssalegmkmEISHL 374
Cdd:TIGR04523 349 KELTNSESEN--------------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES-----------KIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 375 TQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLE----NRHLSEMVMKLELGLHEAKEISLA 450
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQN 483
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635722 451 --------DLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQNDRIFKPTHSRTTEFKNTEF 511
Cdd:TIGR04523 484 leqkqkelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
61-353 |
4.94e-04 |
|
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: 43.29 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 61 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 136
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 137 SEIERLTAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKlesVELSSQSEIQHLSSK 212
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 213 LERANDTICANELEIErltmrvNDLVGTSMTVLQEQQQKEEKLRESEKLLE-ALQEEKRELKAALQSQENLIHEAriQKE 291
Cdd:pfam12128 399 LAKIREARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLE--NFD 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034635722 292 KLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKyeeLKRMEAHNNEYKAEIKKLKEQI 353
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEA---LRQASRRLEERQSALDELELQL 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-286 |
8.99e-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: 42.75 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 22 EAELQELMKQIdimvahkkSEWEGRTHALETCLKIREQELKSLRSQLdvthkevgmlhqqveEHEKIKQEMTMEYKQELK 101
Cdd:TIGR02169 797 QAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEI---------------QELQEQRIDLKEQIKSIE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 102 KLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQS 181
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 182 EIIQAQLvnRKQKLESVELSSQSEIQhlssklerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL 261
Cdd:TIGR02169 934 SEIEDPK--GEDEEIPEEELSLEDVQ-----------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
250 260
....*....|....*....|....*
gi 1034635722 262 LEALQEEKRELKAALQSQENLIHEA 286
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-436 |
9.60e-04 |
|
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: 42.52 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 159 QRLIYQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 237
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSA-REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 238 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELKAALQSQENLIHEARIQK-EKLQEKVKATNTQHA--VEAISLESV 314
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 315 SATCKQ-----------------------LSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEI 371
Cdd:pfam12128 744 GAKAELkaletwykrdlaslgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 372 SHLTQELHQ-------RDITIASTKGSSSDMEKR-------LRAEMQK---------AEDKAVEHKEILDQLESLKLENR 428
Cdd:pfam12128 824 SELQQQLARliadtklRRAKLEMERKASEKQQVRlsenlrgLRCEMSKlatlkedanSEQAQGSIGERLAQLEDLKLKRD 903
|
....*...
gi 1034635722 429 HLSEMVMK 436
Cdd:pfam12128 904 YLSESVKK 911
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
193-334 |
1.07e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034635722 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ--------HAVEAISLES---VSATCKQLSQELMEKYEELKR 334
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQlaaleaalDASEKRDRESqakIADLGRRLNVALAQRVQELNR 194
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
160-354 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 160 RLIYQQQVSSLEAQRKALAEQSEIiQAQLVNRKQKLESvelssQSEIQHLSSKLERandticanELEIERltmrvndlvg 239
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKK-EAEAIKKEALLEA-----KEEIHKLRNEFEK--------ELRERR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 240 tsmtvlQEQQQKEEKLRESEKLL----EALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVS 315
Cdd:PRK12704 82 ------NELQKLEKRLLQKEENLdrklELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE-------LERIS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034635722 316 A-TCKQLSQELMEKYEELKRMEA------HNNEYKAEIKKLKEQIL 354
Cdd:PRK12704 149 GlTAEEAKEILLEKVEEEARHEAavlikeIEEEAKEEADKKAKEIL 194
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
27-359 |
1.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 27 ELMKQIDIMVAHKKSEWEGRTHAletclKIREQELKSLRSQLDVTHKEVGMlHQQVEEHEKIKQEmTMEYKQELKKLHEE 106
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQE-----KFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQA-EMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 107 LCILK-RSYEKLQKKQMREfrgntKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ 185
Cdd:pfam17380 342 MAMEReRELERIRQEERKR-----ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 186 AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELE----IERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL 261
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQErqqqVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 262 LEALQEEKRE-----------LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatcKQLSQELMEKYE 330
Cdd:pfam17380 497 LEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEER-------------RRIQEQMRKATE 563
|
330 340
....*....|....*....|....*....
gi 1034635722 331 ELKRMEAHNNEykaeiKKLKEQILQGEQS 359
Cdd:pfam17380 564 ERSRLEAMERE-----REMMRQIVESEKA 587
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
58-209 |
2.01e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 58 EQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMtMEYKQELKKLHEELCILKRSYEKLQKKqmrefrgNTKNHREDRS 137
Cdd:pfam13851 53 QQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSL-KNLKARLKVLEKELKDLKWEHEVLEQR-------FEKVERERDE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635722 138 EIERLTAKIEEFRQKSldwEKQRLIYQQQVSSL-------EAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHL 209
Cdd:pfam13851 125 LYDKFEAAIQDVQQKT---GLKNLLLEKKLQALgetlekkEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
95-445 |
2.07e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 95 EYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 175 KALAEQSEiiqaqlvnrkqklesvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGtsmtvlqEQQQKEEK 254
Cdd:pfam07888 118 DALLAQRA------------------AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGA-------QRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVkatntqhaveaislesvsatckqlsQELMEKYEELKR 334
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------------------------TTLTQKLTTAHR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 335 MEAHNNEYKAEIKKLKEQILQGEQSYS---SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRaemqkaEDKAV 411
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEglgEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR------EGRAR 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034635722 412 EHKEILDQLESLKLENRH---LSEMVMKLELGLHEAK 445
Cdd:pfam07888 302 WAQERETLQQSAEADKDRiekLSAELQRLEERLQEER 338
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
97-299 |
2.15e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 97 KQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQ--------KSLDWEKQRLIYQQQV- 167
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADE-----------AERARELDLLRFQLEELEAaalqpgeeEELEEERRRLSNAEKLr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 168 SSLEAQRKALAEQSEIIQAQLVNRKQKLESVE-------------LSSQSEIQHLSSKLERANDTICANELEIERLTMRV 234
Cdd:COG0497 226 EALQEALEALSGGEGGALDLLGQALRALERLAeydpslaelaerlESALIELEEAASELRRYLDSLEFDPERLEEVEERL 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034635722 235 NDLVGTS----------MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK-EKLQEKVKA 299
Cdd:COG0497 306 ALLRRLArkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVTA 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-300 |
2.49e-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: 39.91 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelSSQSEIQHLSSK 212
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 213 LERANDTICANELEIERLTMRVndlvgtsmtvlqeqQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEK 292
Cdd:COG1579 98 IESLKRRISDLEDEILELMERI--------------EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1034635722 293 LQEKVKAT 300
Cdd:COG1579 164 EREELAAK 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
80-508 |
2.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 80 QQVEEHEKIKQEMTMEYKQELKKLHEELcilKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQ 159
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 160 RLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLER-ANDTICANELEIERLTMRVNDLV 238
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 239 GTSMTVLQEQQQKEEKLRESEKLLEALQ--EEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSA 316
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 317 TCKQLSQELMEKYEELKRMEAHNNE---YKAEIKKLKEQILQGEQSYSSALEgmKMEISHLTQELHQRDITIASTKGSSS 393
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 394 DMEKRLRAEMQ--KAED--KAVEHKEILDQLESLKLENRHLSEMVMKLE--LGLHEAKEISLADLQENYIEALNKLVSEN 467
Cdd:PTZ00121 1608 KAEEAKKAEEAkiKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1034635722 468 QQLQKDLMNTKSQLEISTQMCKKQNDRIFKPTHSRTTEFKN 508
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-446 |
2.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 95 EYKQELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELR--EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 175 KALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTsmtvlQEQQQKEEK 254
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE-----LEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 255 LRESEKLLEA--------------------------------------LQEEKRELKAALQSQENLIHEARIQKEKLQEK 296
Cdd:COG4717 245 LKEARLLLLIaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 297 VKATNTQHAVEAISLESVSATCKQLsQELMEKYEELKRmEAHNNEYKAEIKKL-KEQILQGEQSYSSALE------GMKM 369
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEE-ELQLEELEQEIAALlAEAGVEDEEELRAALEqaeeyqELKE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 370 EISHLTQELHQR--DITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHL--SEMVMKLELGLHEAK 445
Cdd:COG4717 403 ELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELK 482
|
.
gi 1034635722 446 E 446
Cdd:COG4717 483 A 483
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
87-438 |
3.00e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 87 KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhREDRSEIerltakIEEFRQKSLDWEKQRLIYQQQ 166
Cdd:COG5022 825 TIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS--------LLKKETI------YLQSAQRVELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 167 VSSLEAqrkaLAEQSEIIQAQLVNRKQKLESVELSsQSEIQ-HLSSKLERANDTIcanELEIERLTMrvndlvgtsmtvl 245
Cdd:COG5022 891 VKSISS----LKLVNLELESEIIELKKSLSSDLIE-NLEFKtELIARLKKLLNNI---DLEEGPSIE------------- 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 246 QEQQQKEEKLRESEKlleALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaislesvsatcKQLSQEL 325
Cdd:COG5022 950 YVKLPELNKLHEVES---KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAEL---------------SKQYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 326 MEKYEELKRMEAHNNEYKAEIKKLKEqilqgEQSYSSALEGMKMEISHLTQELHQrdiTIASTKGSSSDMEKRLRAEMQK 405
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISS-----ESTELSILKPLQKLKGLLLLENNQ---LQARYKALKLRRENSLLDDKQL 1083
|
330 340 350
....*....|....*....|....*....|...
gi 1034635722 406 AEDKAVEHKEILDQLESLKLENRHLSEMVMKLE 438
Cdd:COG5022 1084 YQLESTENLLKTINVKDLEVTNRNLVKPANVLQ 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-495 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 274 AALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 354 LQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEM 433
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034635722 434 VMKLELGLHEakeisladlQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQNDRI 495
Cdd:COG4942 173 RAELEALLAE---------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
97-475 |
3.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 97 KQELKKLHEELcilkRSYEKLQKKQMREFRGNTKNHREDRSEIERltaKIEEFRQKsldwEKQRLiyQQQVSSLEAQRKA 176
Cdd:PTZ00121 1541 KAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALR---KAEEAKKA----EEARI--EEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 177 LAEQSEIIQAQlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNdlvgtsmtVLQEQQQKEEKLR 256
Cdd:PTZ00121 1608 KAEEAKKAEEA----KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--------AAEEAKKAEEDKK 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 257 ESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSAtcKQLSQELMEKYEELKRME 336
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--KKEAEEDKKKAEEAKKDE 1753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 337 AHNNEYkAEIKKLKEQILQGEQSYSSAL--EGMKMEISHLTQELhqrDITIASTKGSSSDMEK---------RLRAEMQK 405
Cdd:PTZ00121 1754 EEKKKI-AHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEV---DKKIKDIFDNFANIIEggkegnlviNDSKEMED 1829
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 406 AEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYIEALNKlVSENQQLQKDLM 475
Cdd:PTZ00121 1830 SAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE-ADEIEKIDKDDI 1898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-482 |
3.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 22 EAELQELMKQIDIMVAhKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIK---QEMTMEYKQ 98
Cdd:COG1196 238 EAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 99 ELKKLHEELCILKRSYEKLQKKQMR---EFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLiyQQQVSSLEAQRK 175
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEEleeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE--ELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 176 ALAEQSEIIQAQ-----LVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQ 250
Cdd:COG1196 395 AAELAAQLEELEeaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 251 KEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQ--------------EKVKATNTQHAVEAISLESVSA 316
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavligvEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 317 TCKQLSQ------------------ELMEKYEELKRME------------AHNNEYKAEIKKLKEQILQGEQSYSSALEG 366
Cdd:COG1196 555 DDEVAAAaieylkaakagratflplDKIRARAALAAALargaigaavdlvASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 367 MKMEISHLTQELHQ--RDITIASTKGSSS--------------DMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHL 430
Cdd:COG1196 635 ALRRAVTLAGRLREvtLEGEGGSAGGSLTggsrrellaalleaEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034635722 431 SEMVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLE 482
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-491 |
4.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 179 EQSEIIQAQLVNRKQKLESVEL--SSQSEIQHLSSKLERANDTICANELEIERLTMRVNdLVGTSMtvlqEQQQKEEKLR 256
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQlaAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN-LVQTAL----RQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 257 ESeklLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHA--VEAISLESVSATCKQLSQELMEKYEEL-- 332
Cdd:PRK04863 355 AD---LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyQQALDVQQTRAIQYQQAVQALERAKQLcg 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 333 ------KRMEAHNNEYKAEIKKLKEQILQGEQSYSSAlEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 406
Cdd:PRK04863 432 lpdltaDNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 407 EDKAVE-----HKEILDQLESLKLENRHLSEMVMKLELGLHEAKEI-SLADLQENYIEALNKLVSENQQLQKDLMNTKSQ 480
Cdd:PRK04863 511 LAEQLQqlrmrLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELeQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330
....*....|.
gi 1034635722 481 LEISTQMCKKQ 491
Cdd:PRK04863 591 LQARIQRLAAR 601
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-494 |
4.23e-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: 40.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 24 ELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKL 103
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 104 HEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAE 179
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 180 QSEIIQAQLVNRKQKLESVELSSQ--SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSmtvlqeqQQKEEKLRE 257
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPEllLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR-------DQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 258 SEKLLEALQEEKRELKAALQSQE-NLIHEARIQKEKLQE---KVKATNTQHAVE---AISLESVSATCKQLSQELMEKYE 330
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQsigKVISPELLHRTDldpEVWDGSVGGELNLYGVKLDLKRI 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 331 ELKRMEAHNNEYKAEIKKLKEQiLQGEQSYSSALEGMKMEISHLTQELhQRDITIASTKGSSSDME-KRLRAEMQKAEDK 409
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEA-LQSAREKQAAAEEQLVQANGELEKA-SREETFARTALKNARLDlRRLFDEKQSEKDK 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 410 AveHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYIEALNKL--VSENQQLQKDLMNT-----KSQLE 482
Cdd:pfam12128 669 K--NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWqvVEGALDAQLALLKAaiaarRSGAK 746
|
490
....*....|..
gi 1034635722 483 ISTQMCKKQNDR 494
Cdd:pfam12128 747 AELKALETWYKR 758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
247-480 |
4.60e-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: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatckQLSQELM 326
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 327 EKYEELKRMEAHNNEYKAEIKKLkeQILQGEQSYSSALEGMKMeISHLTQelHQRDI--TIASTKGSSSDMEKRLRAEMQ 404
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYL--DVLLGSESFSDFLDRLSA-LSKIAD--ADADLleELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034635722 405 KAEDKAVEHKEILDQLESLKLENrhlsemvmklelglhEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQ 480
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQ---------------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-493 |
4.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 55 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQ---ELKKLHEelcilKRSYEKLQKK--QMREFRGNT 129
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkadEAKKAEE-----KKKADEAKKKaeEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 130 KNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLEsvELSSQSEIQHL 209
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 210 SSKLERANDTICANELEIERltmrvndlvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENliHEARIQ 289
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKK---------------ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 290 KEKLQEKVKATNTQHAVE----AISLESVSATCKQLSQELMEKYEELKRMEAHNneyKAEIKKLKEQILQGEQSySSALE 365
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEA-KKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 366 GMKMEISHLTQELHQ-RDITIASTKGSSSDM---EKRLRAEMQKAED-KAVEHKEILDQLESLKLENRHLSEMVMKLELG 440
Cdd:PTZ00121 1539 AKKAEEKKKADELKKaEELKKAEEKKKAEEAkkaEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034635722 441 LHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQND 493
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-424 |
5.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 249 QQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKatntQHAVEAIslesvsatcKQLSQELMEK 328
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR----GNGGDRL---------EQLEREIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 329 YEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQrditiastkgsssdMEKRLRAEMQKAED 408
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA--------------LEEALAEAEAALRD 416
|
170
....*....|....*.
gi 1034635722 409 KAVEHKEILDQLESLK 424
Cdd:COG4913 417 LRRELRELEAEIASLE 432
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-487 |
7.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 248 QQQKEEKLRESEKLLEALQEEKRELKAALqsqenliheariqkEKLQEKVKATNTQHAVEAISLESvsatcKQLSQELME 327
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 328 KYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEgmkmeishltqelhqrDITIASTKGSSSDMEKRLRAEMQKAE 407
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELAELSARYT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 408 DKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENyIEALNKLVSENQQLQKDLMNTKSQLEISTQM 487
Cdd:COG3206 288 PNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-LAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
55-472 |
8.53e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 55 KIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEmtmeYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhre 134
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH----INNELESKEEQLSSYEDKLFDVCGSQDEE---------- 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 135 drSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSeiiqaqlvnrkQKLESVELSSQSEIQHLSSKLE 214
Cdd:TIGR00606 639 --SDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC-----------QRVFQTEAELQEFISDLQSKLR 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 215 RANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQK---- 290
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEesak 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 291 ---------EKLQEKVKATNTQHAVEAISLESVSA--TCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIlQGEQS 359
Cdd:TIGR00606 786 vcltdvtimERFQMELKDVERKIAQQAAKLQGSDLdrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI-QHLKS 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635722 360 YSSALEGMKMEIS--------------HLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAED----KAVEHKEILDQLE 421
Cdd:TIGR00606 865 KTNELKSEKLQIGtnlqrrqqfeeqlvELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEElissKETSNKKAQDKVN 944
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1034635722 422 SLKLENRHLSEMVMKLELGLHEAKEISLADlQENYIEALNKLVSENQQLQK 472
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQ-KETELNTVNAQLEECEKHQE 994
|
|
| |
