|
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 |
8.54e-91 |
|
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: 277.86 E-value: 8.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 178 AEQSEIIQA-----QLVNRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1212626330 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 |
1.23e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 96 YKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 176 ALAEQSEIIQ---AQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169 340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHaveaislESVSATCKQLSQELMEKYEEL 332
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQREL 492
|
....*
gi 1212626330 333 KRMEA 337
Cdd:TIGR02169 493 AEAEA 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-441 |
2.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 163 YQQQVSSLEAQRKALA-EQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTS 241
Cdd:COG1196 218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 242 MTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQL 321
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 322 SQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRA 401
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1212626330 402 EMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-365 |
1.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 175 KALAEQseiiQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG1196 312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270
....*....|....*....|....*....|.
gi 1212626330 335 MEAHNNEYKAEIKKLKEQILQGEQSYSSALE 365
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-418 |
2.23e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLER 215
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 216 ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAAL--------------QSQEN 281
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 282 LIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 361
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1212626330 362 SALEgmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILD 418
Cdd:TIGR02168 912 ELRR----ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-365 |
4.54e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 37 AHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEK 116
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 117 LQKKQMREfrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE 196
Cdd:TIGR02168 304 KQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 197 SVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL-----LEALQEEKRE 271
Cdd:TIGR02168 376 ELE----EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaiSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKE 351
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330
....*....|....
gi 1212626330 352 QIlQGEQSYSSALE 365
Cdd:TIGR02168 528 LI-SVDEGYEAAIE 540
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-355 |
2.39e-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: 56.61 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 86 EKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 166 QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAAlqsqenlIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQE 324
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKE 890
|
250 260 270
....*....|....*....|....*....|.
gi 1212626330 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQ 355
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-441 |
2.82e-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: 53.52 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 214 ERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKL 293
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 294 QEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSalegmkmeish 373
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE----------- 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626330 374 LTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGL 441
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-333 |
3.27e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELKAALQSQENlihea 286
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQA----- 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1212626330 287 riQKEKLQEKVKATNtQHAVEAISLESVSATCKQLSQELMEKYEELK 333
Cdd:COG3206 335 --QLAQLEARLAELP-ELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-454 |
2.69e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 157 EKQRLIYQQQVSSLEAQRKALAEQseiiqaqlvnrKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVND 236
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEE-----------LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 237 LVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAI---SLES 313
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 314 VSATCKQLSQELMEKY-----------EELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA-LEGMKMEISHLTQELHQ- 380
Cdd:TIGR02168 373 RLEELEEQLETLRSKVaqlelqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEEl 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212626330 381 --RDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECSLPVSPLGSI 454
Cdd:TIGR02168 453 qeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-299 |
2.77e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 98 QELKKLHEELCILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIE-EFRQKSLDWEKQRLI-YQQQVSSLEAQRK 175
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE--PIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEeLRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 176 ALAEQSEIIQAQLVNRKQKLESvelSSQSEIQHLSSKLERANDTIcaneLEIERLTMRVNDLVGT-SMTVLQEQQQKEEK 254
Cdd:COG4913 313 RLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLEREL----EERERRRARLEALLAAlGLPLPASAEEFAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1212626330 255 LRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKA 299
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-438 |
4.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELcilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LVNRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA-------LQSQENLIHEARIQKEKLQE 295
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 296 KVKATNTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS 361
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 362 SA--LEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVE-HKEILDQLESLKLENRHLSEMVM 435
Cdd:PRK02224 507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAELKE 586
|
...
gi 1212626330 436 KLE 438
Cdd:PRK02224 587 RIE 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-352 |
1.63e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 14 GGGFLTSCEAELQELMKQIDIM------VAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHE- 86
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEe 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 87 --KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQmrefrgNTKNHREDRSEIERLTAKIEEfrqksldwekqrliyq 164
Cdd:TIGR02169 745 dlSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSK---------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 165 qqvssLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 803 -----LEEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAV------------------ 306
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleeelseiedpkgedeei 946
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1212626330 307 --EAISLESVSATCKQLSQEL-------MEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:TIGR02169 947 peEELSLEDVQAELQRVEEEIralepvnMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-471 |
2.75e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 1 MEALLEGIQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLH 79
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 80 QQVEEhekikqemtmeYKQELKKLHEELCILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921 377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLVNRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921 442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 226 EIERLTMRVNdlvgTSMTVLQEQQQKEEKLR--------------ESEKLLE---------------------ALQEEKR 270
Cdd:pfam15921 518 EITKLRSRVD----LKLQELQHLKNEGDHLRnvqtecealklqmaEKDKVIEilrqqienmtqlvgqhgrtagAMQVEKA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEAR--VSDLELEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 342 YKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSD-------MEKRLRAEM----------- 403
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRgqidalqskiq 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 404 ------------------------QKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECSLPVSPLGSIATRFL 459
Cdd:pfam15921 752 fleeamtnankekhflkeeknklsQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQE 831
|
570
....*....|...
gi 1212626330 460 EEE-ELRSHHILE 471
Cdd:pfam15921 832 QESvRLKLQHTLD 844
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-353 |
6.13e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNhR 133
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 134 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLVNRKQKLESVELSSQSE 205
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 206 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQ------ 279
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikd 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1212626330 280 -ENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:TIGR04523 445 lTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-486 |
6.67e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 247 EQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELM 326
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 327 EKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSAlegmkmEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKA 406
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 407 EDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECslpvspLGSIATRFLEEEELRSHHI-----LERLDAHIEELK 481
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL------EEELEELEAALRDLESRLGdlkkeRDELEAQLRELE 902
|
....*
gi 1212626330 482 RESEK 486
Cdd:TIGR02169 903 RKIEE 907
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-355 |
1.09e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 58 EQELKSLRSQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELCILKRsyeKL 117
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLVNRKQ 193
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELK 273
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 274 AALqsqenliheariqkEKLQEKVKATntqhaveaisLESvSATCKQLSQELMEKYEELKRmeaHNNEYKAEIKKLKEQI 353
Cdd:PRK04863 610 DAL--------------ARLREQSGEE----------FED-SQDVTEYMQQLLERERELTV---ERDELAARKQALDEEI 661
|
..
gi 1212626330 354 LQ 355
Cdd:PRK04863 662 ER 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-353 |
1.09e-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: 44.37 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 95 EYKQELKKLHEELCILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 175 KALAEQSEIIQAQLVNRKQKLESveLSSQSEIQHLSSKlerandticANELEIERLTMRVNDLVgtsmtvlQEQQQKEEK 254
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYLA-------PARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 255 LRESeklLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAveaislesvsatckQLSQELMEKYEELKR 334
Cdd:COG4942 155 LRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAE 217
|
250
....*....|....*....
gi 1212626330 335 MEAHNNEYKAEIKKLKEQI 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEA 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
233-352 |
3.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 233 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELKAAlqsQENLIHEariQKEKLQEKVKATnTQHAVEA 308
Cdd:PRK00409 517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1212626330 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQ 352
Cdd:PRK00409 590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-437 |
4.27e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 271 ELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYKA 344
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 345 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKR---LRAEMQKAEDKAVEHKEI---L 417
Cdd:PRK02224 628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALenrV 707
|
250 260
....*....|....*....|
gi 1212626330 418 DQLESLKLENRHLSEMVMKL 437
Cdd:PRK02224 708 EALEALYDEAEELESMYGDL 727
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
203-436 |
5.21e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 203 QSEIQHLSSKLERANDTICANELEIERltmrvndlvgtsmtvlQEQQQKEEKLRESEKLLEALQEEKrELKAALQSQENL 282
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYNKNIEE----------------QRKKNGENIARKQNKYDELVEEAK-TIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 283 IHEARIQKEKLQEKVKATNTQHAVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQI 353
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 354 LQGEQSYSSALEgMKMEISHLTQELHQRDITIASTKGSSsdmeKRLRAEMQKAEDKAVEHKEILDQL-ESLKLENRHLSE 432
Cdd:PHA02562 323 DELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSE 397
|
....
gi 1212626330 433 MVMK 436
Cdd:PHA02562 398 LVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-346 |
5.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLVNRKQKLESVELSSqSEI 206
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALqsqenlihea 286
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---------- 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1212626330 287 riqkekLQEKVKATNTQHAVEAISlESVSATCKQLSQELMEKYEEL-KRMEAHNNEYKAEI 346
Cdd:COG4913 751 ------LEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELeRAMRAFNREWPAET 804
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
163-336 |
7.13e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 163 YQQQVSSLEAQRKALAEQSEIIQAQlVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSm 242
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 243 tvlqeqqqkEEKLRESEKLLEAlqeekrelKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS-LESVSATCKQL 321
Cdd:pfam00529 134 ---------PIGGISRESLVTA--------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEA 196
|
170
....*....|....*
gi 1212626330 322 SQELMEKYEELKRME 336
Cdd:pfam00529 197 EAELKLAKLDLERTE 211
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-325 |
7.63e-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: 42.08 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 58 EQELKSLRSQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 1212626330 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 |
8.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 246 QEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIS--LESVSATCKQLSQ 323
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1212626330 324 ELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQE 377
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
164-363 |
1.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVelssQSEIQHLSSKLERANDTICANELEIERLTMRVNDLV----- 238
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNEL----QAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 239 -GTSMTVLQ------------EQQQKEEKLRESEK-LLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQH 304
Cdd:COG3883 98 sGGSVSYLDvllgsesfsdflDRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1212626330 305 AVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSA 363
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-358 |
1.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 164 QQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 244 vLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQ-LS 322
Cdd:COG4913 670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLR 748
|
170 180 190
....*....|....*....|....*....|....*....
gi 1212626330 323 QELMEKYEELKRMEAHN---NEYKAEIKKLKEQILQGEQ 358
Cdd:COG4913 749 ALLEERFAAALGDAVERelrENLEERIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-430 |
1.61e-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: 40.90 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 253 EKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaisLESVSATCKQLSQELMEKYEEL 332
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 333 KRMEAHNNEYKAEIKK-LKEQILQGEQSY---------SSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAE 402
Cdd:COG4942 93 AELRAELEAQKEELAElLRALYRLGRQPPlalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180
....*....|....*....|....*...
gi 1212626330 403 MQKAEDKAVEHKEILDQLESLKLENRHL 430
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
133-316 |
2.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVeLSSQSEIQHLSSK 212
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 213 LER---ANDTicaNELeIERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ 289
Cdd:COG3883 105 LDVllgSESF---SDF-LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180
....*....|....*....|....*..
gi 1212626330 290 KEKLQEKVKATNTQHAVEAISLESVSA 316
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-453 |
2.35e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 22 EAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQ 98
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 99 ELKKLHEELCILKRSYEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 178
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 179 eQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREs 258
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 259 ekLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAH 338
Cdd:pfam01576 276 --LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 339 NNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHqrdiTIASTKGSSSDMEKRLRAEMQ----KAEDKAVEHK 414
Cdd:pfam01576 354 HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDSEHKRKKLEGQLQelqaRLSESERQRA 429
|
410 420 430
....*....|....*....|....*....|....*....
gi 1212626330 415 EILDQLESLKLENRHLSEMVMKLELGLHECSLPVSPLGS 453
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
193-334 |
2.55e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1212626330 272 LKAALQSQENLIHEARIQKEKLQEKVKATNTQ--------HAVEAISLES---VSATCKQLSQELMEKYEELKR 334
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQlaaleaalDASEKRDRESqakIADLGRRLNVALAQRVQELNR 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-220 |
3.23e-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: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 20 SCEAELQELMKQIDIMVAhKKSEWEgrthALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQE--MTMEYK 97
Cdd:COG4913 665 SAEREIAELEAELERLDA-SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 98 QELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHRED-RSEIERLTAKIEE-FRQKSLDWekqRLIYQQQVSSLEAQRK 175
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDAlRARLNRAEEELERaMRAFNREW---PAETADLDADLESLPE 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1212626330 176 ALAEQSEIIQAQLVNRKQKL-ESVELSSQSEIQHLSSKLERANDTI 220
Cdd:COG4913 817 YLALLDRLEEDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREI 862
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-494 |
4.54e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 233 RVNDL---VGTSMTVLQEQQQKEEKLREseklleaLQEEKRELKAALQSQEnlIHEARIQKEKLQEKVKATNTQhaveai 309
Cdd:TIGR02168 190 RLEDIlneLERQLKSLERQAEKAERYKE-------LKAELRELELALLVLR--LEELREELEELQEELKEAEEE------ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 310 slesvsatCKQLSQELMEKYEELKRMEAHNNEYKAEIkklkeQILQGE-QSYSSALEGMKMEISHLTQELHQRDITIAST 388
Cdd:TIGR02168 255 --------LEELTAELQELEEKLEELRLEVSELEEEI-----EELQKElYALANEISRLEQQKQILRERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 389 KGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHECSLPVSPLGS-IATRFLEEEELRSH 467
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNE 401
|
250 260
....*....|....*....|....*..
gi 1212626330 468 hiLERLDAHIEELKRESEKTVRQFTAL 494
Cdd:TIGR02168 402 --IERLEARLERLEDRRERLQQEIEEL 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-361 |
5.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 54 LKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 134 EDRSEIERLTAKIEEFRQKSL----------DWEKQRLI--YQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLE----- 196
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGkcpvcgreltEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesel 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 197 SVELSSQSEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAA 275
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 276 LQSQENLIHEARIQ-KEKLQEKVKATNtqhavEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQIL 354
Cdd:PRK03918 576 LKELEELGFESVEElEERLKELEPFYN-----EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
....*..
gi 1212626330 355 QGEQSYS 361
Cdd:PRK03918 651 ELEKKYS 657
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
61-353 |
5.42e-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: 39.44 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 61 LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELcilkrsyeklqKKQMREFRGNTKNHRED----R 136
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW-----------KEKRDELNGELSAADAAvakdR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 137 SEIERLTAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKlesVELSSQSEIQHLSSK 212
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 213 LERANDTICANELEIErltmrvNDLVGTSMTVLQEQQQKEEKLRESEKLLE-ALQEEKRELKAALQSQENLIHEAriQKE 291
Cdd:pfam12128 399 LAKIREARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLE--NFD 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1212626330 292 KLQEKVKATNTQHAVEAISLESVSATCKQLSQELMEKyeeLKRMEAHNNEYKAEIKKLKEQI 353
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEA---LRQASRRLEERQSALDELELQL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-495 |
6.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 39 KKSEWEGRTHALETCLKIREQELKSLRSQLDVTH---KEVGMLHQQVEEHEKIKQEMTmEYKQELKKLHEELCILKRSYE 115
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 116 KLQKKqmrefrgnTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKL 195
Cdd:PRK03918 325 GIEER--------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 196 ESVELSSQSEIQHLSSKLERANDTICANELEIERL--TMRVNDLVGTSMTVLQEQQQKEE---KLRESEKLLEALQEEKR 270
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkAKGKCPVCGRELTEEHRKELLEEytaELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 271 ELKAALQSQENLIHEAR--IQKEKLQEKVKatNTQHAVEAISLEsvsatckqlsqELMEKYEELKRMEAHNNEYKAEIKK 348
Cdd:PRK03918 477 KLRKELRELEKVLKKESelIKLKELAEQLK--ELEEKLKKYNLE-----------ELEKKAEEYEKLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 349 LKEQiLQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHK-------EILDQLE 421
Cdd:PRK03918 544 LKKE-LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKdaekeleREEKELK 622
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1212626330 422 SLKLENRHLSEMVMKLELGLHECSLPVSPLGSIAT----RFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALK 495
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
87-438 |
7.11e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.29 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 87 KIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREfrgntknhREDRSEIerltakIEEFRQKSLDWEKQRLIYQQQ 166
Cdd:COG5022 825 TIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS--------LLKKETI------YLQSAQRVELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 167 VSSLEAqrkaLAEQSEIIQAQLVNRKQKLESVELSsQSEIQ-HLSSKLERANDTIcanELEIERLTMrvndlvgtsmtvl 245
Cdd:COG5022 891 VKSISS----LKLVNLELESEIIELKKSLSSDLIE-NLEFKtELIARLKKLLNNI---DLEEGPSIE------------- 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 246 QEQQQKEEKLRESEKlleALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQhaveaislesvsatcKQLSQEL 325
Cdd:COG5022 950 YVKLPELNKLHEVES---KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAEL---------------SKQYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 326 MEKYEELKRMEAHNNEYKAEIKKLKEqilqgEQSYSSALEGMKMEISHLTQELHQrdiTIASTKGSSSDMEKRLRAEMQK 405
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISS-----ESTELSILKPLQKLKGLLLLENNQ---LQARYKALKLRRENSLLDDKQL 1083
|
330 340 350
....*....|....*....|....*....|...
gi 1212626330 406 AEDKAVEHKEILDQLESLKLENRHLSEMVMKLE 438
Cdd:COG5022 1084 YQLESTENLLKTINVKDLEVTNRNLVKPANVLQ 1116
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
73-409 |
7.33e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 38.93 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 73 KEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQK 152
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELssqsEIQHLSSKLERANDTICANELEIERLTm 232
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEELK- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 233 rvndlvgtsmTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQ-------KEKLQEKVKATNTQHA 305
Cdd:pfam05483 412 ----------KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiktsEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 306 VEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEI---KKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRD 382
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
330 340
....*....|....*....|....*..
gi 1212626330 383 ITIASTKGSSSDMEKRLRAEMQKAEDK 409
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-414 |
8.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 245 LQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKAtnTQHAVEAISLESVSATCKQLSQE 324
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212626330 325 LMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYS----SALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLR 400
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|....
gi 1212626330 401 AEMQKAEDKAVEHK 414
Cdd:COG4717 231 QLENELEAAALEER 244
|
|
| |
