|
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 |
3.34e-98 |
|
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: 301.74 E-value: 3.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 18 LTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYK 97
Cdd:pfam17045 1 LSSCEAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 98 QELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKAL 177
Cdd:pfam17045 81 QQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 178 AEQSEIIQA-----QLANRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:pfam17045 161 AEQSSLIQSaayqvQLEGRKQCLE----ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLL 236
|
250 260
....*....|....*....|....*...
gi 1622903738 253 EKLRESEKLLEALQEEKRELRAALQSQE 280
Cdd:pfam17045 237 EELRMSQRQLQVLQNELMELKATLQSQD 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-337 |
4.31e-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: 72.79 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 23 AELQELMKQIDIMVAHKKSEWEG----RTHAL---ETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTME 95
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERlrreREKAEryqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 96 YKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 176 ALAEQSEIIQ---AQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKE 252
Cdd:TIGR02169 340 ELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 253 EKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHaveaislESVSATCKQLSQELMEKYEEL 332
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQREL 492
|
....*
gi 1622903738 333 KRMEA 337
Cdd:TIGR02169 493 AEAEA 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-453 |
1.53e-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: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 139 IERLTAKIEEFRQ--KSLdwEKQR------LIYQQQVSSLEAQRKALA-EQSEIIQAQLANRKQKLESVELSSQSEIQHL 209
Cdd:COG1196 188 LERLEDILGELERqlEPL--ERQAekaeryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQ 289
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 290 KEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQI----------LQGEQS 359
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallerlerlEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 360 YSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFEL 439
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330
....*....|....
gi 1622903738 440 GLHEAKEISLADLQ 453
Cdd:COG1196 506 FLEGVKAALLLAGL 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-438 |
1.58e-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: 67.79 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 86 EKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQ 165
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 166 QVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELS-SQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtv 244
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 245 LQEQQQKEEKLRESEKLLEALQEEKRELRAAlqsqenlIHEGRMQKEKLQEKVKatDTQHAVeaislesvsatcKQLSQE 324
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-------IENLNGKKEELEEELE--ELEAAL------------RDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 325 LMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYS---SALEGMKMEISHLtQELHQRDISIASTKGSSSDMEKRLKA 401
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQR 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622903738 402 --------------EIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFE 438
Cdd:TIGR02169 963 veeeiralepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-365 |
1.65e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKKQmrefRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQseiiQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEK 254
Cdd:COG1196 312 RELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 255 LRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270
....*....|....*....|....*....|.
gi 1622903738 335 MEAHNNEYRAEIKKLKEQILQGEQSYSSALE 365
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-446 |
3.24e-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: 66.63 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKKqMREFRGNTKNHREDRSEIER---LTAKIEEFRQKSLDWEKQRLiyQQQVSSLE 171
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLI-IDEKRQQLERLRREREKAERyqaLLKEKREYEGYELLKEKEAL--ERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 172 AQRKALAEQSEIIQAQLANRKQKLESVElssqSEIQHLSSKLER-ANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQ 250
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIE----QLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 251 KEEKLRESEKLLEALQEEKRELRAALQSQenlihegRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYE 330
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEE-------RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 331 ELKRMEAHNNEYRAEIKKLKEQIlqgeQSYSSALEGMKMEISHLTQELHQRDisiastkgsssDMEKRLKAEIQKAEEKA 410
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEEL----QRLSEELADLNAAIAGIEAKINELE-----------EEKEDKALEIKKQEWKL 457
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622903738 411 vehKEILDQLESLKLENRHLSEMVMKFELGLHEAKE 446
Cdd:TIGR02169 458 ---EQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-355 |
4.10e-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: 66.62 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 57 REQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEelgilkrsyeklqkkQMREFRGNTKNHREDR 136
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE---------------LSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 137 SEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqSEIQHLSSKLERA 216
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 217 NDTICANELEIERLTMRVNDLvGTSMTVLQEQ-QQKEEKLRESEKLLEALQEEKRELRAALQSQENlihegrmQKEKLQE 295
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAAT-ERRLEDLEEQiEELSEDIESLAAEIEELEELIEELESELEALLN-------ERASLEE 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 296 KVKATDTQhaveaisLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQILQ 355
Cdd:TIGR02168 888 ALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-365 |
6.95e-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: 62.38 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 23 AELQELmkQIDIMVAHKKSEWEGRtHALETCLKIREQELKTLRGQLDvthkevgMLHQQVEEHEKIKQEMTMEYKQELKK 102
Cdd:TIGR02168 220 AELREL--ELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 103 LHEELGILKRSYEKLQKKQMREfrgntknhREDRSEIERLTAKIEEfrqksldWEKQRLIYQQQVSSLEAQRKALAEQSE 182
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERL--------ANLERQLEELEAQLEE-------LESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 183 IIQAQLANRKQKLESVELSSQS---EIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESE 259
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEEleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 260 KL-----LEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAveaiSLESVSATCKQLSQELMEKYEELKR 334
Cdd:TIGR02168 435 LKelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350
....*....|....*....|....*....|.
gi 1622903738 335 MEAHNNEYRAEIKKLKEQIlQGEQSYSSALE 365
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-482 |
1.51e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 249 QQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEK 328
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 329 YEELKRMEAHNNEYRAEIKKLKEQILQGE----------QSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKR 398
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEaeieeleaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 399 LKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEI---------SLADLQENYIEALNKLVSENQQ 469
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealaLLRSELEELSEELRELESKRSE 912
|
250
....*....|...
gi 1622903738 470 LQKDLMNTKSQLE 482
Cdd:TIGR02168 913 LRRELEELREKLA 925
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-333 |
1.55e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 136 RSEIERLTAKIEEFRQKS--LDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESV-----ELSSQSEIQH 208
Cdd:COG3206 188 RKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 209 LSSKLERAndticanELEIERLTMRVNDLvGTSMTVLQEQQQ--KEEKLRESEKLLEALQEEKRELRAALQSQENliheg 286
Cdd:COG3206 268 LRAQLAEL-------EAELAELSARYTPN-HPDVIALRAQIAalRAQLQQEAQRILASLEAELEALQAREASLQA----- 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622903738 287 rmQKEKLQEKVKATdTQHAVEAISLESVSATCKQLSQELMEKYEELK 333
Cdd:COG3206 335 --QLAQLEARLAEL-PELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-356 |
1.64e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 22 EAELQELMKQIDimvahkksEWEGRTHALETCLKIREQELKTLRGQLDvthkevgmlhqqveehekikqemtmEYKQELK 101
Cdd:COG1196 238 EAELEELEAELE--------ELEAELEELEAELAELEAELEELRLELE-------------------------ELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 102 KLHEELGILKRSYEKLQKKQMREfrgnTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQs 181
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 182 eiiQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL 261
Cdd:COG1196 360 ---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 262 LEALQEEKRELRAALQSQENLIHEGRMQKEKLQEkvkatdtqhavEAISLESVSATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLE-----------EAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330
....*....|....*
gi 1622903738 342 YRAEIKKLKEQILQG 356
Cdd:COG1196 506 FLEGVKAALLLAGLR 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-456 |
1.76e-08 |
|
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: 57.76 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 100 LKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAE 179
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 180 QSEIIQAQLANRKQKLESVelssQSEIQHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESE 259
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEEL----QKELYALANEISRL-------EQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 260 KLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHaveaislesvsatckqlsQELMEKYEELKRMEAHN 339
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL------------------ETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 340 NeyrAEIKKLKEQIlqgeQSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEkrlKAEIQKAEEKAVEhkeildQ 419
Cdd:TIGR02168 399 N---NEIERLEARL----ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE---LEELQEELERLEE------A 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622903738 420 LESLKLENRHLSEMVMKFELGLHE--AKEISLADLQENY 456
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQlqARLDSLERLQENL 501
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-471 |
6.28e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 78 LHQQVEEHE-KIKQEMTMEYKQELKKLHEELgilkRSYEKlQKKQMREFRGNTK----NHREDRSEIERLTAKIEEFRQK 152
Cdd:PRK02224 192 LKAQIEEKEeKDLHERLNGLESELAELDEEI----ERYEE-QREQARETRDEADevleEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 153 SLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQ----------LANRKQKLESVELSSQSEIQHLSSKLERANDTICA 222
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 223 NELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAA-------LQSQENLIHEGRMQKEKLQE 295
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 296 KVKATDTQHAVEAISLESVSA--------TCKQLSQE------LMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYS 361
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpECGQPVEGsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 362 SA--LEGMKMEISHLTQELHQRDISIASTKGSSSDMEKR---LKAEIQKAEEKAVE-HKEILDQLESLKLENRHLSEmvM 435
Cdd:PRK02224 507 AEdrIERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAEEKREAAAEaEEEAEEAREEVAELNSKLAE--L 584
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622903738 436 KFELGLHEAKEISLADLqENYIEALNKLVSENQQLQ 471
Cdd:PRK02224 585 KERIESLERIRTLLAAI-ADAEDEIERLREKREALA 619
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-334 |
4.78e-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: 53.15 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 14 GGGFLTSCEAELQELMKQIDIM------VAHKKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHE- 86
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLkrelssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEe 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 87 --KIKQEMTMEYKQELKKLHEELGILKRSYEKLQKK-----------QMREFRGNTKNHREDRSEIERLTAKIE------ 147
Cdd:TIGR02169 745 dlSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEqklnrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 148 EFRQKSLDWEKQRLiyQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSS----------QSEIQHLSSKLERAN 217
Cdd:TIGR02169 825 TLEKEYLEKEIQEL--QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdlesrlgdlKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 218 DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRE------SEKLLEALQEEKRELRAALQSQENLIHEGRMQKE 291
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622903738 292 KLQEKVKATDTQHAVEAISLESVsatckqlsQELMEKYEELKR 334
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAI--------LERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-501 |
1.09e-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: 51.99 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 247 EQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELM 326
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 327 EKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYSSAlegmkmEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQKA 406
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 407 EEKAVEHKEILDQLESLKLENRHLSEmvmkfELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQ 486
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEK-----EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250
....*....|....*
gi 1622903738 487 MCKKQNDRIFKPTHR 501
Cdd:TIGR02169 904 KIEELEAQIEKKRKR 918
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-353 |
1.46e-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: 50.92 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKKQmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEE-----------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQSEIIQAQLANRKQKLESveLSSQSEIQHLSSKlerandticANELEIERLTMRVNDLVgtsmtvlQEQQQKEEK 254
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP---------EDFLDAVRRLQYLKYLA-------PARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 255 LRESeklLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAveaislesvsatckQLSQELMEKYEELKR 334
Cdd:COG4942 155 LRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA--------------RLEKELAELAAELAE 217
|
250
....*....|....*....
gi 1622903738 335 MEAHNNEYRAEIKKLKEQI 353
Cdd:COG4942 218 LQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-354 |
7.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 136 RSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEI---------IQAQLANRKQKLESVELSSqSEI 206
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDASS-DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 207 QHLSSKLERAndticanELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKR-ELRAALQSQ-ENLIH 284
Cdd:COG4913 688 AALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERfAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 285 EGRMQK--EKLQEKVKATDTQHAVEAISLEsvsatckqlsqELMEKYEELKRMEAHN--------NEYRAEIKKLKEQIL 354
Cdd:COG4913 761 DAVERElrENLEERIDALRARLNRAEEELE-----------RAMRAFNREWPAETADldadleslPEYLALLDRLEEDGL 829
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-355 |
8.33e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 58 EQELKTLRGQL-------DVTHKEVGMLHQQVEEHEKIKQ-------------EMTMEYKQELKKLHEELGILKRsyeKL 117
Cdd:PRK04863 389 EEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQ---KL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 118 QKKQM--REFRGNTKNHREDRSEIERLTAKiEEFRQKSLDWEKQRlIYQQQVSSLEAQRKALAEQSEIIQA--QLANRKQ 193
Cdd:PRK04863 466 SVAQAahSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRRLREQR-HLAEQLQQLRMRLSELEQRLRQQQRaeRLLAEFC 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 194 KLESVELSSQSEIQHLSSKLERandticanelEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREseklLEALQEEKRELR 273
Cdd:PRK04863 544 KRLGKNLDDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQR----LAARAPAWLAAQ 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 274 AALqsqenlihegrmqkEKLQEKVKATDTQhaveaislesvSATCKQLSQELMEKYEELKRmeaHNNEYRAEIKKLKEQI 353
Cdd:PRK04863 610 DAL--------------ARLREQSGEEFED-----------SQDVTEYMQQLLERERELTV---ERDELAARKQALDEEI 661
|
..
gi 1622903738 354 LQ 355
Cdd:PRK04863 662 ER 663
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
95-353 |
1.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKKqmrefrgntknhREDRSEIERLTAKIEEFRQKSLDWEKqrliYQQQVSSLEAQR 174
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAE------------LDALQERREALQRLAEYSWDEIDVAS----AEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KAL-AEQSEI--IQAQLANRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQ---EQ 248
Cdd:COG4913 678 ERLdASSDDLaaLEEQLEELEAELEELE----EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 249 QQKEEKLRESEK-LLEALQEEKRELRAALQSQENLIhEGRMQKEKLQEKVKATDtqHAVEAISLESVSATCKQLSQE-LM 326
Cdd:COG4913 754 RFAAALGDAVEReLRENLEERIDALRARLNRAEEEL-ERAMRAFNREWPAETAD--LDADLESLPEYLALLDRLEEDgLP 830
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622903738 327 EKYEELKRMEAHNN---------EYRAEIKKLKEQI 353
Cdd:COG4913 831 EYEERFKELLNENSiefvadllsKLRRAIREIKERI 866
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-494 |
1.41e-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: 48.58 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 165 QQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTIcanELEIERLTMRvndLVGTSMTV 244
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY---EDKIEELEKQ---LVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 245 LQEQQQKEEKLRESEKLLEALQEekreLRAALQSQENLIHEGRMQKEKLQEKvkatDTQHAVeaislesvsaTCKQLSQE 324
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQK----LLADLHKREKELSLEKEQNKRLWDR----DTGNSI----------TIDHLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 325 LMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQ----------SYSSALEGMKMEISHLTQELHQRDISIASTKGSSSD 394
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 395 MEKRLKAEIQKAEEKAVEHKEI-------LDQLESLKLENRHLSEMVMKFE-LGLHEAKEISLADLQENYIEALNKLVSE 466
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKNEGDHLRNVQTECEaLKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
330 340
....*....|....*....|....*...
gi 1622903738 467 NQQLQKDLMNTKSQLEistqmcKKQNDR 494
Cdd:pfam15921 581 HGRTAGAMQVEKAQLE------KEINDR 602
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-424 |
2.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 54 LKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELgilkrsyEKLQKKQMREFRGNTKNHR 133
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL-------EKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 134 EDRSEIERLTAKIEEFRQ---------KSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQaQLANRKQKLESV-----E 199
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKVlkkesE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 200 LSSQ----SEIQHLSSKLERAN-DTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRA 274
Cdd:PRK03918 495 LIKLkelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 275 ALQSQENLiheGRMQKEKLQEKVKATDTQHAvEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQIL 354
Cdd:PRK03918 575 LLKELEEL---GFESVEELEERLKELEPFYN-EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622903738 355 QGEQSYS--------SALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKaEIQKAEEKAVEHKEILDQLESLK 424
Cdd:PRK03918 651 ELEKKYSeeeyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELR 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-229 |
2.69e-05 |
|
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: 47.07 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 22 EAELQELMKQIDIMVAHKKSEwEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMtmeyKQELK 101
Cdd:COG4942 26 EAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 102 KLHEELGILKRSYEKLQKKQMREFRGNTKN--------------HREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQV 167
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622903738 168 SSLEAQRKALAEQSEIIQAQLANRKQKLEsvelSSQSEIQHLSSKLERANDTICANELEIER 229
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELA----ELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-437 |
2.97e-05 |
|
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: 47.53 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 159 QRLIYQQQVSSLEAQRKALAEQSEIIQAQLAnRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDL- 237
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEk 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 238 VGTSMTVLQEQQQKEEKLRESEKLLEALqeeKRELRAALQSQENLIHEGRMQK-EKLQEKVKATDTQHA--VEAISLESV 314
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLAllKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 315 SATCKQ-----------------------LSQELMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYSSALEGMKMEI 371
Cdd:pfam12128 744 GAKAELkaletwykrdlaslgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 372 SHLTQELHQ-------RDISIASTKGSSSDMEKRLK----------------AEIQKAEEKAVEHKEILDQLESLKLENR 428
Cdd:pfam12128 824 SELQQQLARliadtklRRAKLEMERKASEKQQVRLSenlrglrcemsklatlKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
....*....
gi 1622903738 429 HLSEMVMKF 437
Cdd:pfam12128 904 YLSESVKKY 912
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-447 |
3.30e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 54 LKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNhR 133
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 134 EDRSEIERLTAKIEEFR-QKSLDWEKQ-RLIYQQQVSSLEAQRKALAEQSEIIQ------AQLANRKQKLESVELSSQSE 205
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 206 IQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQ------ 279
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikd 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 280 -ENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQI----- 353
Cdd:TIGR04523 445 lTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsslke 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 354 ---------LQGEQSYSS------------ALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAE-------IQK 405
Cdd:TIGR04523 525 kieklesekKEKESKISDledelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKekekkdlIKE 604
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622903738 406 AEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEI 447
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-444 |
5.38e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 1 MEALLERMQNRGHGGGFLTSCE-AELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLH 79
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 80 QQVEEhekikqemtmeYKQELKKLHEELGILKRSYEKLQKKQMrefrGNT------KNHREDRS-EIERLTAKIEEFRQK 152
Cdd:pfam15921 377 DQLQK-----------LLADLHKREKELSLEKEQNKRLWDRDT----GNSitidhlRRELDDRNmEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 153 SLDWEKQRLIYQQ-------QVSSLEAQRKALAEQSEIIQAQLANRKQKLESvelsSQSEIQHLSSKLERANDTICANEL 225
Cdd:pfam15921 442 CQGQMERQMAAIQgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 226 EIERLTMRVNdlvgTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE-------LRAALQSQENLIHE-----GRMQKEKL 293
Cdd:pfam15921 518 EITKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQhgrtaGAMQVEKA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 294 Q---------------------EKVKATDTQHAVEAISLESVS---------ATCKQLSQELMEKYEELKRMEAHNNEYR 343
Cdd:pfam15921 594 QlekeindrrlelqefkilkdkKDAKIRELEARVSDLELEKVKlvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 344 AEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSD-------MEKR----------LKAEIQKA 406
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQitakrgqidaLQSKIQFL 753
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622903738 407 EEK-------------------------AVEHKEILDQLESLKLENRHLSEMVMKFELGLHEA 444
Cdd:pfam15921 754 EEAmtnankekhflkeeknklsqelstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
191-466 |
5.41e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 191 RKQKLESVELSSQSEIQHLSSKLERANDTICAnELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLE-------ELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 271 ELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLS------QELMEKYEELKRMEAHNNEYRA 344
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaeDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 345 EIKKLKEQILQGEQSY-SSALEGMKMEISHLTQELHQRDISIASTKgsssDMEKRLKAEIQKAEEKavehkeiLDQLESL 423
Cdd:PRK02224 628 RLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELR----EERDDLQAEIGAVENE-------LEELEEL 696
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622903738 424 KLENRHLSEMVMKFELGLHEAKEIS------LADLQENYIEALNKLVSE 466
Cdd:PRK02224 697 RERREALENRVEALEALYDEAEELEsmygdlRAELRQRNVETLERMLNE 745
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-325 |
7.90e-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: 45.94 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 58 EQELKTLRGQldvthkEVGMLHQQVEE----HEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQK-KQMREfrgntKNH 132
Cdd:pfam01576 318 QQELRSKREQ------EVTELKKALEEetrsHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKaKQALE-----SEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVE---LSSQSEIQHL 209
Cdd:pfam01576 387 AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgknIKLSKDVSSL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 210 SSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQ 289
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622903738 290 KEKLQEKVKATDTQHAVEAISLESVSATCKQLSQEL 325
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
81-483 |
9.19e-05 |
|
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: 45.87 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 81 QVEEHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQmrefrgntKNHREDRSEIERLTAKIEEFRQKSLD-WEKQ 159
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ--------KALEEDLQIATKTICQLTEEKEAQMEeLNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 160 RLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELssqsEIQHLSSKLERANDTICANELEIERLTmrvndlvg 239
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM----ELQKKSSELEEMTKFKNNKEVELEELK-------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 240 tsmTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQ-------KEKLQEKVKATDTQHAVEAISLE 312
Cdd:pfam05483 412 ---KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQltaiktsEEHYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 313 SVSATCKQLSQELMEKYEELKRMEAHNNEYRAEI---KKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDISIASTK 389
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 390 GSSSDMEKRLKAEIQKAEEKAVEHKEILDQL-ESLKLENRHLSEMVMKFEL----GLHEAKEISLADLQENYIEAlnKLV 464
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLkKQIENKNKNIEELHQENKAlkkkGSAENKQLNAYEIKVNKLEL--ELA 646
|
410
....*....|....*....
gi 1622903738 465 SENQQLQKDLMNTKSQLEI 483
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIED 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
39-426 |
1.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 39 KKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMT------MEYKQELKKLHEELGILKR 112
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelekelESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 113 SYEKLQK--KQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEiiqaqlan 190
Cdd:PRK03918 267 RIEELKKeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE-------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 191 RKQKLESVELSSQSEIQHLSSKlERANDTICANELEIERLTMRVNDLvgtsmtvlqEQQQKEEKLRESEKLLEALQEEKR 270
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGL---------TPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 271 ELRAALQSQENLIHEGRMQKEKLqEKVKAT--------DTQHAVEAIS-----LESVSATCKQLSQELMEKYEELKRMEA 337
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEEL-KKAKGKcpvcgrelTEEHRKELLEeytaeLKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 338 HNNEYRAEIK--KLKEQILQGEQSYSS----ALEGMKMEISHLTQE---LHQRDISIASTKGSSSDMEKRLKAEIQKAEE 408
Cdd:PRK03918 488 VLKKESELIKlkELAEQLKELEEKLKKynleELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
410
....*....|....*...
gi 1622903738 409 KAVEHKEILDQLESLKLE 426
Cdd:PRK03918 568 LEEELAELLKELEELGFE 585
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-493 |
1.13e-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: 45.40 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 54 LKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMT---MEYKQELKKLHEELGILKrSYEKLQKKQM-------- 122
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNdklKKNKDKINKLNSDLSKIN-SEIKNDKEQKnkleveln 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 123 ---REFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVE 199
Cdd:TIGR04523 128 kleKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 200 LSSQ------SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQ-------QQKEEKLRESEKLLEALQ 266
Cdd:TIGR04523 208 KKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQnkikkqlSEKQKELEQNNKKIKELE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 267 EEKRELRAAL-----QSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNE 341
Cdd:TIGR04523 288 KQLNQLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 342 YRAEIKKLKEQIlqgeQSYSSALEGMKMEISHLTQELHQRdisiastKGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLE 421
Cdd:TIGR04523 368 KQNEIEKLKKEN----QSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622903738 422 SLKLENRHLSEMVMKFELGLHEAKeiSLADLQENYIEALNKLVSENQQlqkDLMNTKSQLEISTQMCKKQND 493
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLD--NTRESLETQLKVLSRSINKIKQ---NLEQKQKELKSKEKELKKLNE 503
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-486 |
1.34e-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: 45.34 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 57 REQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQmrefrgnTKNHREDR 136
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-------QIHLQETR 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 137 SEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQ-RKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLER 215
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 216 ANDTICANELEIERLTmrvNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQE 295
Cdd:TIGR00618 568 IQQSFSILTQCDNRSK---EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 296 KVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYSSALEGMKMEISHLT 375
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 376 QELHQRDISIASTKGSSSDMEKRLKAEI-----------QKAEEKAVEHKEILDQLESLKlenRHLSEMVMKFELGLHEA 444
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQArtvlkarteahFNNNEEVTAALQTGAELSHLA---AEIQFFNRLREEDTHLL 801
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622903738 445 KEIsLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQ 486
Cdd:TIGR00618 802 KTL-EAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-482 |
1.69e-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: 45.01 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKkqmrEFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKD----NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQSEIIQAQLAN-RKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEE 253
Cdd:TIGR04523 284 KELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 254 KLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQhaveaislesvsatCKQLSQELMEKYEELK 333
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ--------------IKKLQQEKELLEKEIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 334 RMEAHNNEYRAEIKKLKEQILQGEQSYSSalegMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQ-----KAEE 408
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKN----LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkklNEEK 505
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622903738 409 KAVEH--KEILDQLESLKLENRHLSEMVMKFELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLE 482
Cdd:TIGR04523 506 KELEEkvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-399 |
3.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 163 YQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAndticanELEIERLTmrvndlvgtsm 242
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL-------EAELEELR----------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 243 tvlQEQQQKEEKLRESEKLLEALQEEKRELRAALQSqenliHEGRmQKEKLQEKVKATDTQHAVEAISLESVSATCKQLS 322
Cdd:COG4913 302 ---AELARLEAELERLEARLDALREELDELEAQIRG-----NGGD-RLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622903738 323 QELMEKYEELKRMeahnneyRAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRL 399
Cdd:COG4913 373 LPLPASAEEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
203-436 |
3.67e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 203 QSEIQHLSSKLERANDTICANELEIERLTMRVNDlvgtsmtVLQEQQQKEEKLRESEK----LLEALQEEKRELRAALQS 278
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGE-------NIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 279 QENLIHEGRMQKEKLQEKVKatdtQHAVEAISLES--VSATCKQLSQELMEKYEELKrmeAHNNEYRAEIKKLKEQILQG 356
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIE----QFQKVIKMYEKggVCPTCTQQISEGPDRITKIK---DKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 357 EQSYSSALEgMKMEISHLTQELHQRDISIASTKGSSsdmeKRLKAEIQKAEEKAVEHKEILDQL-ESLKLENRHLSEMVM 435
Cdd:PHA02562 326 EEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLqDELDKIVKTKSELVK 400
|
.
gi 1622903738 436 K 436
Cdd:PHA02562 401 E 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-316 |
4.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 145 KIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLSSKLERANDTI---- 220
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 221 --------CANELE-----------IERLTMrVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQEN 281
Cdd:COG3883 93 ralyrsggSVSYLDvllgsesfsdfLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1622903738 282 LIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSA 316
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
246-377 |
5.16e-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: 42.22 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 246 QEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAIS--LESVSATCKQLSQ 323
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622903738 324 ELMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQE 377
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-466 |
5.48e-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: 42.83 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 253 EKLRESEKLLEALQEEKRELRAALQSQENlihegrmQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEEL 332
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 333 KRMEAHNNEYRAEIKK-LKEQILQGEQSY---------SSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAE 402
Cdd:COG4942 93 AELRAELEAQKEELAElLRALYRLGRQPPlalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622903738 403 IQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKfELGLHEAKEISLADLQENYIEALNKLVSE 466
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEK-ELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-416 |
5.58e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 105 EELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEF--RQKSLDWEKQRLIYQQqvsslEAQRKALAEQsE 182
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSlkAKKRFSLLKKETIYLQ-----SAQRVELAER-Q 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 183 IIQAQLANRK-QKLESVELSSQSEIQHLSSKLEraNDTICANELEIERLTmRVNDLVGTSMTVLQ-----EQQQKEEKLR 256
Cdd:COG5022 884 LQELKIDVKSiSSLKLVNLELESEIIELKKSLS--SDLIENLEFKTELIA-RLKKLLNNIDLEEGpsieyVKLPELNKLH 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 257 ESEKlleALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKatdtqhaveaisleSVSATCKQLSqELMEKYEELKRME 336
Cdd:COG5022 961 EVES---KLKETSEEYEDLLKKSTILVREGNKANSELKNFKK--------------ELAELSKQYG-ALQESTKQLKELP 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 337 AHNNEYRAEIKKLKE-----QILQGEQSYSSALEGMKMEISHLTQELHQRdisiastKGSSSDMEKRLK-AEIQKAEEKA 410
Cdd:COG5022 1023 VEVAELQSASKIISSestelSILKPLQKLKGLLLLENNQLQARYKALKLR-------RENSLLDDKQLYqLESTENLLKT 1095
|
....*.
gi 1622903738 411 VEHKEI 416
Cdd:COG5022 1096 INVKDL 1101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-446 |
6.25e-04 |
|
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: 43.04 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 81 QVEEHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQR 160
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 161 liyQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT 240
Cdd:pfam02463 260 ---IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 241 SmtvLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQ 320
Cdd:pfam02463 337 I---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 321 LSQELMEKYEELKRMEAHNNE--YRAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKR 398
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622903738 399 LKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKE 446
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
163-336 |
6.46e-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: 42.41 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 163 YQQQVSSLEAQRKALAEQSEIIQAQLaNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSm 242
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 243 tvlqeqqqkEEKLRESEKLLEAlqeekrelRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAIS-LESVSATCKQL 321
Cdd:pfam00529 134 ---------PIGGISRESLVTA--------GALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEA 196
|
170
....*....|....*
gi 1622903738 322 SQELMEKYEELKRME 336
Cdd:pfam00529 197 EAELKLAKLDLERTE 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
245-414 |
7.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 245 LQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDtqHAVEAISLESVSATCKQLSQE 324
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 325 LMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQSYS----SALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLK 400
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|....
gi 1622903738 401 AEIQKAEEKAVEHK 414
Cdd:COG4717 231 QLENELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-299 |
7.89e-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: 41.45 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelSSQSEIQHLSSK 212
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 213 LERANDTICANELEIERLTMRVNDLVgtsmtvlQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEgrmQKEK 292
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELE-------EELAELEAELAELEAELEEKKAELDEELAELEAELEELEA---EREE 167
|
....*..
gi 1622903738 293 LQEKVKA 299
Cdd:COG1579 168 LAAKIPP 174
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
233-352 |
9.64e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 233 RVNDLVGTSMTVLQEQQQK----EEKLRESEKLLEALQEEKRELRAAlqsQENLIHEgrmQKEKLQEKVKATdTQHAVEA 308
Cdd:PRK00409 517 KLNELIASLEELERELEQKaeeaEALLKEAEKLKEELEEKKEKLQEE---EDKLLEE---AEKEAQQAIKEA-KKEADEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622903738 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQ 352
Cdd:PRK00409 590 IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-358 |
1.01e-03 |
|
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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 164 QQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVElssqsEIQHLSSKLERANDTicanELEIERLTMRvndlvgtsmt 243
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-----ERREALQRLAEYSWD----EIDVASAERE---------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 244 vLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVK-ATDTQHAVEAISLESVSATCKQLS 322
Cdd:COG4913 670 -IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622903738 323 QELMEKYEELKRMEAHN---NEYRAEIKKLKEQILQGEQ 358
Cdd:COG4913 749 ALLEERFAAALGDAVERelrENLEERIDALRARLNRAEE 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-289 |
1.30e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 58 EQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEM------TMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKN 131
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELqeqridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 132 HREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQklESVELSSQSEIQhlss 211
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE--IPEEELSLEDVQ---- 957
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622903738 212 klerandticaneLEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENLIHEGRMQ 289
Cdd:TIGR02169 958 -------------AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
67-353 |
1.68e-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: 41.75 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 67 QLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELgilkRSYEKLQKKQMREFRGNTKNHRED----RSEIERL 142
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL----RTLDDQWKEKRDELNGELSAADAAvakdRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 143 TAKIEEFRQKSLDWEKQRL----IYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKlesVELSSQSEIQHLSSKLERAND 218
Cdd:pfam12128 328 EDQHGAFLDADIETAAADQeqlpSWQSELENLEERLKALTGKHQDVTAKYNRRRSK---IKEQNNRDIAGIKDKLAKIRE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 219 TICANELEIErltmrvNDLVGTSMTVLQEQQQKEEKLRESEKLLE-ALQEEKRELRAALQSQENLihegrMQKEKLQEKV 297
Cdd:pfam12128 405 ARDRQLAVAE------DDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELL-----LQLENFDERI 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622903738 298 KATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQI 353
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
22-495 |
1.83e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 22 EAELQELMKQIDIMVAHKKsewegRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQE---MTMEYKQ 98
Cdd:PRK01156 224 SIEYNNAMDDYNNLKSALN-----ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyKNRNYIN 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 99 ELKKLHEELGILKRSYEKLqKKQMREFRGNTKNHRE---DRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRK 175
Cdd:PRK01156 299 DYFKYKNDIENKKQILSNI-DAEINKYHAIIKKLSVlqkDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 176 ALAEQSEIIQAQLANRKQKLESVELSSQ----------SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVL 245
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEILKIQEIDPDaikkelneinVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 246 QEQQQKEEKlreSEKLLEALQEEKRELRAALQSQEN---LIHEGRMQKEKLQEKVKATDTQHAV-EAISLESVSATCKql 321
Cdd:PRK01156 458 CGTTLGEEK---SNHIINHYNEKKSRLEEKIREIEIevkDIDEKIVDLKKRKEYLESEEINKSInEYNKIESARADLE-- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 322 sqELMEKYEELKRMEAHNNEYRAEIKKLKEQILqgEQSYSSALEGM------------------KMEISHLTQELHQRDI 383
Cdd:PRK01156 533 --DIKIKINELKDKHDKYEEIKNRYKSLKLEDL--DSKRTSWLNALavislidietnrsrsneiKKQLNDLESRLQEIEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 384 SIASTKGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEISLADLQENyiEALNKL 463
Cdd:PRK01156 609 GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE--DNLKKS 686
|
490 500 510
....*....|....*....|....*....|..
gi 1622903738 464 VSENQQLQKDLMNTKSQLEISTQMCKKQNDRI 495
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
84-508 |
2.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 84 EHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSldwEKQRLIY 163
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA---EEKKKAD 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 164 QQQVSSLEAQRKAlaeqSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERANDticANELEIERLTMRVndlvgtsmt 243
Cdd:PTZ00121 1395 EAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKK--------- 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 244 vLQEQQQKEEKLRESEKLLEAlQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQ 323
Cdd:PTZ00121 1459 -AEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 324 ELMEKYEELKRMEAHNNE---YRAEIKKLKEQILQGEQSYSSALEgmKMEISHLTQELHQRDISIASTKGSSSDMEKRLK 400
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 401 AEIQ--KAEE--KAVEHKEILDQLESLKLENRHLSEMVMKFE--LGLHEAKEISLADLQENYIEALNKLVSENQQLQKDL 474
Cdd:PTZ00121 1615 AEEAkiKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430
....*....|....*....|....*....|....
gi 1622903738 475 MNTKSQLEISTQMCKKQNDRIFKPTHRRTTEFKN 508
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-353 |
2.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 54 LKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEmtmeYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNhr 133
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN----QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 134 edRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVEL------------- 200
Cdd:TIGR04523 439 --NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekkeleekvkdlt 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 201 ----SSQSEIQHLSSKLERANDTIcaNELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELRAAL 276
Cdd:TIGR04523 517 kkisSLKEKIEKLESEKKEKESKI--SDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 277 QSQENLIHEGRMQKEKLQEKV--KATDTQHAVEAISLE--SVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQ 352
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLekELEKAKKENEKLSSIikNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
.
gi 1622903738 353 I 353
Cdd:TIGR04523 675 I 675
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
27-345 |
2.66e-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: 40.88 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 27 ELMKQIDIMVAHKKSEWEGRTHAletclKIREQELKTLRGQLDVTHKEVGMlHQQVEEHEKIKQEmTMEYKQELKKLHEE 106
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQE-----KFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQA-EMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 107 LGILK-RSYEKLQKKQMREfrgntKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQ 185
Cdd:pfam17380 342 MAMEReRELERIRQEERKR-----ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 186 AQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELE----IERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKL 261
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQErqqqVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 262 LEALQEEKRE-----------LRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAvEAISLESVSATCKQLSQELMEKYE 330
Cdd:pfam17380 497 LEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEER-RRIQEQMRKATEERSRLEAMERER 575
|
330
....*....|....*
gi 1622903738 331 ELKRMEAHNNEYRAE 345
Cdd:pfam17380 576 EMMRQIVESEKARAE 590
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
24-476 |
2.76e-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: 40.98 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 24 ELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKL 103
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 104 HEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLdwEKQRLIYQQQVSSL----EAQRKALAE 179
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQL--AVAEDDLQALESELreqlEAGKLEFNE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 180 QSEIIQAQLANRKQKLESVELS---------SQSEIQHLSSKLERANDTICANELEIERLTMR---VNDLVGTSMTVLQE 247
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATpelllqlenFDERIERAREEQEAANAEVERLQSELRQARKRrdqASEALRQASRRLEE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 248 QQQKEEKLRE-----SEKLLEALQEEK---RELRAALQSQEnLIHEGRMQKEKLQEKVKATDT-----------QHAVEA 308
Cdd:pfam12128 518 RQSALDELELqlfpqAGTLLHFLRKEApdwEQSIGKVISPE-LLHRTDLDPEVWDGSVGGELNlygvkldlkriDVPEWA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKeqilQGEQSYSSALEGMKMEISHLTQElhQRDISIAST 388
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS----REETFARTALKNARLDLRRLFDE--KQSEKDKKN 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 389 KGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEISLADLQENYIEALNKLVSENQ 468
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
....*...
gi 1622903738 469 QLQKDLMN 476
Cdd:pfam12128 751 ALETWYKR 758
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-432 |
2.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQkkQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQR 174
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELR--EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTsmtvlQEQQQKEEK 254
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE-----LEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 255 LRESEKLLEA--------------------------------------LQEEKRELRAALQSQENLIHEGRMQKEKLQEK 296
Cdd:COG4717 245 LKEARLLLLIaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 297 VKATDTQHAVEAISLESVSATCKQLsQELMEKYEELKRmEAHNNEYRAEIKKL-KEQILQGEQSYSSALE------GMKM 369
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEE-ELQLEELEQEIAALlAEAGVEDEEELRAALEqaeeyqELKE 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622903738 370 EISHLTQELHQR--DISIASTKGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLESLKLENRHLSE 432
Cdd:COG4717 403 ELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-487 |
3.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 248 QQQKEEKLRESEKLLEALQEEKRELRAALQSQENlihegRMQKEKLQEKVKATDTQHAVEAISLEsvsatckQLSQELME 327
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEA-----ALEEFRQKNGLVDLSEEAKLLLQQLS-------ELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 328 KYEELKRMEAHNNEYRAEIKKLKEQIlqGEQSYSSALEGMKMEISHLTQELhqrdISIASTKGSSSDMEKRLKAEIQKAE 407
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAELEAEL----AELSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 408 EK-AVEHKEILDQLESLKLENRHLSEMVMKfELGLHEAKEISLADLQENYIEaLNKLVSENQQLQKDLMNTKSQLEISTQ 486
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQA-QLAQLEARLAELPELEAELRR-LEREVEVARELYESLLQRLEEARLAEA 382
|
.
gi 1622903738 487 M 487
Cdd:COG3206 383 L 383
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
58-209 |
3.07e-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: 39.50 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 58 EQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMtMEYKQELKKLHEELGILKRSYEKLQKKqmrefrgNTKNHREDRS 137
Cdd:pfam13851 53 QQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSL-KNLKARLKVLEKELKDLKWEHEVLEQR-------FEKVERERDE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622903738 138 EIERLTAKIEEFRQKSldwEKQRLIYQQQVSSL-------EAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHL 209
Cdd:pfam13851 125 LYDKFEAAIQDVQQKT---GLKNLLLEKKLQALgetlekkEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
133-414 |
3.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 133 REDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVelssQSEIQHLSSK 212
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDEL----NEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 213 LERANDTI--CANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLleaLQEEKRELRAALQSQENLIHEgRMQK 290
Cdd:COG1340 80 RDELNEKLneLREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVL---SPEEEKELVEKIKELEKELEK-AKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 291 EKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQILQgeqsYSSALEGMKME 370
Cdd:COG1340 156 LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE----AQEKADELHEE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622903738 371 ISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQKAEEKAVEHK 414
Cdd:COG1340 232 IIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-410 |
3.73e-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: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 201 SSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQE 280
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 281 NLIHEGRMQKEKLQEKVKATDTQHAVEAIS-LESVSATCKQLSQELMEKYEELKRMEAHNNEYRAEIKKLKEQILQGEQS 359
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622903738 360 YSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQKAEEKA 410
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
95-422 |
4.59e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 95 EYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIyqqqvssleaqR 174
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-----------K 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQSEIIQAQLANrkQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVgtsmtvlqEQQQKEEK 254
Cdd:COG5185 309 KATESLEEQLAAAEAE--QELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV--------ELSKSSEE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 255 LRESEKLLEALQEEKRELRAALQSQENLIHEG-----RMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKY 329
Cdd:COG5185 379 LDSFKDTIESTKESLDEIPQNQRGYAQEILATledtlKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 330 EELK-----RMEAHNNEYRAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQ 404
Cdd:COG5185 459 EESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHI 538
|
330
....*....|....*...
gi 1622903738 405 KAEEKAVEHKEILDQLES 422
Cdd:COG5185 539 LALENLIPASELIQASNA 556
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-434 |
4.65e-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: 40.16 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 22 EAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTME---YKQ 98
Cdd:pfam01576 52 ETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtTEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 99 ELKKLHEELGILKRSYEKLQKkqmrefrgnTKNHREDRseIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKala 178
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSK---------ERKLLEER--ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 179 eQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLREs 258
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 259 ekLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKATDTQHAVEAISLESVSATCKQLSQELMEKYEELKRMEAH 338
Cdd:pfam01576 276 --LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 339 NNEYRAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHqrdiSIASTKGSSSDMEKRLKAEIQ----KAEEKAVEHK 414
Cdd:pfam01576 354 HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDSEHKRKKLEGQLQelqaRLSESERQRA 429
|
410 420
....*....|....*....|
gi 1622903738 415 EILDQLESLKLENRHLSEMV 434
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-230 |
7.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 59 QELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTME-YKQELKKLHEELGILKRSYEKLQKKQmREFRGNTKNHreDRS 137
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEeLRAELARLEAELERLEARLDALREEL-DELEAQIRGN--GGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 138 EIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAN 217
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170
....*....|...
gi 1622903738 218 DTICANELEIERL 230
Cdd:COG4913 419 RELRELEAEIASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-493 |
7.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 55 KIREQELKTLRGQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQ---ELKKLHEelgilKRSYEKLQKK--QMREFRGNT 129
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkadEAKKAEE-----KKKADEAKKKaeEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 130 KNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLEsvELSSQSEIQHL 209
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 210 SSKLERANDTICANELEIERltmrvndlvgtsmtvLQEQQQKEEKLRESEKLLEALQEEKRELRAALQSQENliHEGRMQ 289
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKK---------------ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 290 KEKLQEKVKATDTQHAVE----AISLESVSATCKQLSQELMEKYEELKRMEAHNneyRAEIKKLKEQILQGEQSySSALE 365
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEA-KKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 366 GMKMEISHLTQELHQ-RDISIASTKGSSSDM---EKRLKAEIQKAEE-KAVEHKEILDQLESLKLENRHLSEMVMKFELG 440
Cdd:PTZ00121 1539 AKKAEEKKKADELKKaEELKKAEEKKKAEEAkkaEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622903738 441 LHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQND 493
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
80-469 |
7.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 80 QQVEEHEKIKQEMTMEYKQELKKLHEELGILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQ 159
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 160 RLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLE---------RANDTICANELEIERL 230
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEdarkaeearKAEDAKKAEAARKAEE 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 231 TMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEK-RELRAALQSQENLIHEGRMQKEKLQEKV-KATDTQHAVEA 308
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIrKFEEARMAHFA 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 309 ISLESVSATCKQLSQELMEKYEELKRMEAHNNEYRA---EIKKLKEQILQGEQSYSSALEGMKM--EISHLTQELHQRDI 383
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKkadEAKKKAEEAKKADEAKKKAEEAKKKadAAKKKAEEAKKAAE 1346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 384 SIASTKGSSSDMEKRLKAEIQKAEEKAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEISLADLQENYIEALNKL 463
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
....*.
gi 1622903738 464 VSENQQ 469
Cdd:PTZ00121 1427 AEEKKK 1432
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
97-474 |
8.61e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.05 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 97 KQELKKLHEELgilkRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQksldwekqrliyqqqvsSLEAQRKA 176
Cdd:PRK04778 104 KHEINEIESLL----DLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRK-----------------SLLANRFS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 177 LAEQSEIIQAQLANRKQKLES-VELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKL 255
Cdd:PRK04778 163 FGPALDELEKQLENLEEEFSQfVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYREL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 256 RESEKLLEALQEEKR--ELRAALQSQENLIHEGRMqkEKLQEKVKATDTQ--HAVEAISLEsVSAtcKQLSQELMEKYEE 331
Cdd:PRK04778 243 VEEGYHLDHLDIEKEiqDLKEQIDENLALLEELDL--DEAEEKNEEIQERidQLYDILERE-VKA--RKYVEKNSDTLPD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 332 -LKRMEAHNNEYRAEIKKLKE--QILQGEQSYSSALEgmkMEISHLTQELHQRDISIASTKGSSSDMEKRLKAEIQKAEE 408
Cdd:PRK04778 318 fLEHAKEQNKELKEEIDRVKQsyTLNESELESVRQLE---KQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 409 KAVEHKEILDQLESLKLENRHLSEMVMKFELGLHEAKEI----SLADLQENYIEALNKLVSENQQLQKDL 474
Cdd:PRK04778 395 IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYleksNLPGLPEDYLEMFFEVSDEIEALAEEL 464
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
193-345 |
8.77e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 193 QKLESVELSSQ-SEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRE 271
Cdd:PRK09039 41 QFFLSREISGKdSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 272 LRAALQSQENLIHEGRMQKEKLQEKVKATDTQ--------HAVEAISLES---VSATCKQLSQELMEKYEELKRmeahnn 340
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQlaaleaalDASEKRDRESqakIADLGRRLNVALAQRVQELNR------ 194
|
....*
gi 1622903738 341 eYRAE 345
Cdd:PRK09039 195 -YRSE 198
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-479 |
9.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 175 KALAEQSEIIQAQLANRKQKLESVElssqSEIQHLSSKLERANDTICANELEIERLtmrvndlvgtsmtvlqeqQQKEEK 254
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEVKEL------------------EELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 255 LRESEKLLEALQEEKRELRAALQSQENLIHEGRMQKEKLQEKVKatdtqhavEAISLESVSATCKQLSQELMEKYEELKR 334
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK--------ELKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622903738 335 MEAHNNEYRAEIKKLKEQIlqgeqsysSALEGMKMEISHLTQELhqrdisiastkgssSDMEKRLkAEIQKAEEKAVEHK 414
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERI--------KELEEKEERLEELKKKL--------------KELEKRL-EELEERHELYEEAK 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622903738 415 EILDQLESLKLENRHLSEMVMKFELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKS 479
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| |
