|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-338 |
3.83e-12 |
|
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: 69.32 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQvkvEE 331
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ---ER 944
|
....*..
gi 578824467 332 LTEERSL 338
Cdd:TIGR02168 945 LSEEYSL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-351 |
8.78e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELE 182
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 183 RQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQhIIRLESLQAEQVLEIKML 262
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 263 SDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSA 342
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
....*....
gi 578824467 343 ATSTSLLSE 351
Cdd:COG1196 500 EADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-358 |
4.43e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 99 LLSVIRQKEKDLVLAarlgKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELEsdvkqlq 178
Cdd:COG1196 230 LLLKLRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 179 dELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLE 258
Cdd:COG1196 299 -RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 259 IKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK-DLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260
....*....|....*....|.
gi 578824467 338 LQSSAATSTSLLSEIEQSMEA 358
Cdd:COG1196 458 EEALLELLAELLEEAALLEAA 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-337 |
1.12e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 195 KSRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALREDFREKNSSTNQHIIR-LESLQAEQVLEIKMLSDRKRELEHRL 273
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824467 274 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-354 |
1.17e-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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 135 HKELTDKLEHLEQEkhELRRRFENREGEWEgrvsELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLS 214
Cdd:COG1196 215 YRELKEELKELEAE--LLLLKLRELEAELE----ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 215 RASEVERQLSMQVHALREDfREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRV 294
Cdd:COG1196 289 EEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 295 LILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELteERSLQSSAATSTSLLSEIEQ 354
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-335 |
3.11e-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: 56.99 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 120 LLERNQDMSRQYEQMhKELTDKLEHLEQEKHELRRRFEnregewegrvsELESDVKQLQDELERQQIHLREADREKSRAV 199
Cdd:TIGR02168 672 ILERRREIEELEEKI-EELEEKIAELEKALAELRKELE-----------ELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 200 QElSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEE 279
Cdd:TIGR02168 740 AE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578824467 280 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 335
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-348 |
3.17e-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: 56.60 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 103 IRQKEKDLvLAARLG--KALLERNQDMSRQYEQMHKELTD-------KLEHLEQEKHELRRRFENREGEWE---GRVSEL 170
Cdd:TIGR02168 222 LRELELAL-LVLRLEelREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYalaNEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 171 ESDVKQLQ-----------------DELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALRED 233
Cdd:TIGR02168 301 EQQKQILRerlanlerqleeleaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 234 FREKNSSTNQHIIRLESLQAeqvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK---DLQLHQ 310
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNN----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeleELQEEL 456
|
250 260 270
....*....|....*....|....*....|....*...
gi 578824467 311 SQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 348
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-332 |
1.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 129 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 208 RLLDQLSRaseverqlsmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG4913 338 DRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824467 288 EELQDRVLILERQGHD-----KDLQLHQSQL--ELQEVRLS-CRQLQVKVEEL 332
Cdd:COG4913 408 AEAEAALRDLRRELREleaeiASLERRKSNIpaRLLALRDAlAEALGLDEAEL 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-303 |
9.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELESDVKQLQDELERQQIHLREADREKSR 197
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----TLRSKVAQLELQIASLNNEIERLEARLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 198 AVQELSEQNQRLLDQLSRASEVERQ-LSMQVHALREDFREKNSSTNQHIIRLESLQaEQVLEIKMLSDRKRELEHRLSAT 276
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQAR 490
|
170 180
....*....|....*....|....*..
gi 578824467 277 LEENDLLQGTVEELQDRVLILERQGHD 303
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-358 |
1.30e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 179 DELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQV-- 256
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTel 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 257 -LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKV------ 329
Cdd:TIGR02168 760 eAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterr 839
|
170 180 190
....*....|....*....|....*....|....*...
gi 578824467 330 --------EELTEER-SLQSSAATSTSLLSEIEQSMEA 358
Cdd:TIGR02168 840 ledleeqiEELSEDIeSLAAEIEELEELIEELESELEA 877
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
105-319 |
1.38e-06 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 50.41 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849 77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEverqlsmQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQ-------QMAELSEELARK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 238 NSSTNQHIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLE 314
Cdd:pfam04849 230 MEENLRQQEEITSLLAQIVdlqHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEE 302
|
....*
gi 578824467 315 LQEVR 319
Cdd:pfam04849 303 LKELR 307
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
118-352 |
3.59e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQE-KHELRRRFENREgewegRVSELESDV-----KQLQDELERQQIHLREA 191
Cdd:COG5022 816 LACIIKLQKTIKREKKLRETEEVEFSLKAEVlIQKFGRSLKAKK-----RFSLLKKETiylqsAQRVELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 192 DREksraVQELSEQNQRLLdqlSRASEVERQLSmqvhalrEDFREKNSSTNQHIIRLESLQAEqvLEIKMLSDRKRELEH 271
Cdd:COG5022 891 VKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIARLKKLLNN--IDLEEGPSIEYVKLP 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 272 RLSATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 348
Cdd:COG5022 955 ELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKI 1034
|
....
gi 578824467 349 LSEI 352
Cdd:COG5022 1035 ISSE 1038
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-535 |
7.40e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 338 LQSSA-ATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY----------CQVRYLCSHLRGNDSADSAVSTDSSMDESS 406
Cdd:TIGR02168 765 ELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltlLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 407 ETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSED-KEPKEQLQKAIRDRDEAIAKK 485
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKL 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578824467 486 NAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 535
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
95-355 |
1.08e-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: 48.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 333
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
250 260
....*....|....*....|....
gi 578824467 334 E--ERSLQSSAATSTSLLSEIEQS 355
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKA 680
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
118-357 |
1.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELTD----------KLEHLEQEKHELRRRFENREGEWEGRVSELESdvkqLQDELERqqIH 187
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEareavedrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERDE--LR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 188 LREADREKS-RAVQELSEQNQRLLDQ---------------LSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESL 251
Cdd:PRK02224 426 EREAELEATlRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 252 qAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
250 260
....*....|....*....|....*.
gi 578824467 332 LTEERSLQSSAATSTSLLSEIEQSME 357
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIE 609
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-319 |
1.81e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 98 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 178 QDE----LERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhALREDFREKNSSTNQHIIRLESLQA 253
Cdd:COG1196 368 LEAeaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824467 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVR 319
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-337 |
2.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 139 TDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELER-QQIHLREADREKSRAVQELSEQNQRLLDQLSRAS 217
Cdd:COG4913 609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 218 EVERQLSMQVHALREDFREknsstnqhiirleslqAEQvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 297
Cdd:COG4913 685 DDLAALEEQLEELEAELEE----------------LEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578824467 298 ERQGHDKDLQLHQSQLELQEVRlscRQLQVKVEELTEERS 337
Cdd:COG4913 747 LRALLEERFAAALGDAVERELR---ENLEERIDALRARLN 783
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-335 |
1.23e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 125 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAvqelsE 204
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 205 QNQRLLDQLSRASEVERQLSMQV---HALREDFREKNSSTNQHIIRLESLQAEqvLEIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR00606 769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGSDLD--RTVQQVNQEKQEKQHELDTVVSKIE 846
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578824467 282 LLQGTVEELQDRVLILErqghDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 335
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLK----SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-522 |
1.23e-04 |
|
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: 45.05 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 155 RFENREGEWEGRVSELESDVKQLQD---ELERQQIHLrEADREKSRAVQELSEQnqrlldqlsrasevERQLSMQVHALR 231
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDilnELERQLKSL-ERQAEKAERYKELKAE--------------LRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 232 -EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQ 310
Cdd:TIGR02168 234 lEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 311 SQLELQEVRLSCRQLQVKVEELTEErsLQSSAATSTSLLSEIEqSMEAEELEQEREQLrlqlweaycqvrylcshlrgnd 390
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELE-SLEAELEELEAELE---------------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 391 sadsavstdssmdESSETSSAKDVPAGSLRTALNELKRLIQSIvdgmEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQ 470
Cdd:TIGR02168 369 -------------ELESRLEELEEQLETLRSKVAQLELQIASL----NNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578824467 471 LQKaIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEA 522
Cdd:TIGR02168 432 EAE-LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
153-522 |
1.54e-04 |
|
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: 44.72 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 153 RRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASE----VERQLSMQVH 228
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsqedLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 229 ------ALREDFREkNSSTNQHIIRLESLQAEQVL-EIKML------SDRKRELEHRLSATLEENDL---LQGTVEELQD 292
Cdd:pfam15921 153 eleaakCLKEDMLE-DSNTQIEQLRKMMLSHEGVLqEIRSIlvdfeeASGKKIYEHDSMSTMHFRSLgsaISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 293 RVLILERQGHDKDLQLHQSQLELQ-EVRLSCRQLQVKVEELTEERS-----LQSSAATSTSLLSEIEQSMEAEELEQERE 366
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQnKIELLLQQHQDRIEQLISEHEveitgLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 367 QLRlqlweaycqvrylcsHLRGNDSADSAVStdssmdessetssakdvpagSLRTALNELKRLIQSIVDGMEPTVTLLSV 446
Cdd:pfam15921 312 NSM---------------YMRQLSDLESTVS--------------------QLRSELREAKRMYEDKIEELEKQLVLANS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 447 EMTALKEERDRLrvTSEDKEPKEQLQKAIRDRDEAiAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLS----QQLEA 522
Cdd:pfam15921 357 ELTEARTERDQF--SQESGNLDDQLQKLLADLHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevQRLEA 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-335 |
1.54e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 136 KELTDKLEHLEQEKH------ELRRRFENREG-EWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQR 208
Cdd:TIGR02169 194 DEKRQQLERLRREREkaeryqALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 209 LldqlsraseveRQLSMQVHALRED----FREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQ 284
Cdd:TIGR02169 274 L-----------EELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578824467 285 GTVEELQdrvlilerqghdkdLQLHQSQLELQEVRLSCRQLQVKVEELTEE 335
Cdd:TIGR02169 343 REIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-300 |
2.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---FENREGEWEGRVSELESDVKQLQDELERQQIHLRE------- 190
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 191 ---ADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKR 267
Cdd:COG4942 116 lgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578824467 268 E-------LEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:COG4942 196 ErqkllarLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-315 |
2.89e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELER--QQIHLREADREKSRAVQELSEQNQRLlDQL 213
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 214 SRASEVERQLSMQVHALREDFREKNSSTNQHiirLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|..
gi 578824467 294 VLILERQGHDKDLQLHQSQLEL 315
Cdd:COG4717 229 LEQLENELEAAALEERLKEARL 250
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-282 |
4.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 136 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELES------DVKQLQDELERQQIHLREADREKSRAVQELSEQ 205
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824467 206 NQRLLDQLSRASEVERQLSMQVHA-LREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDL 282
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-254 |
4.91e-04 |
|
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: 43.18 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 127 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELEsdvkqlqdeleRQQIHLREADREKSRAVQELSEQN 206
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLE-----------LEKVKLVNAGSERLRAVKDIKQER 655
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578824467 207 QRLLDQLSRASEVERQLSMQVHALREDFREKN----SSTNQHIIRLESLQAE 254
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSE 707
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-291 |
5.08e-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: 42.44 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 178 QDELERQQIHLREADReKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVL 257
Cdd:COG4942 121 PLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190
....*....|....*....|....*....|....
gi 578824467 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQ 291
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-300 |
5.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQihLREADREKSRAVQ 200
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELE----ELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 201 ELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLeslqaeqVLEIKMLSDRKRELEHRLSATLEEN 280
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|
gi 578824467 281 DLLQGTVEELQDRVLILERQ 300
Cdd:COG4717 223 EELEEELEQLENELEAAALE 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
98-300 |
7.26e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 167
Cdd:pfam05557 52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 168 SELESDVKQLQDELERQQIHLREAdrekSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalrEDFREKNSSTNQHIIR 247
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824467 248 LESLQAEQvleikmlsDRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 300
Cdd:pfam05557 199 IPELEKEL--------ERLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
121-497 |
7.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 201 ELSE-QNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEE 279
Cdd:COG4717 228 ELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 280 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRlSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAE 359
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 360 ELEQEREQLRLQLWEAycQVRYLCSHLRGNDSADSAVSTDSSMDEssetssakdvpagsLRTALNELKRLIQSIVDgmep 439
Cdd:COG4717 387 LRAALEQAEEYQELKE--ELEELEEQLEELLGELEELLEALDEEE--------------LEEELEELEEELEELEE---- 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578824467 440 tvtllsvEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRM 497
Cdd:COG4717 447 -------ELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
129-289 |
8.50e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 129 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 208 RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLE-SLQAEQVLEIKMLSDRKRELEHRLSatlEENDLLQGT 286
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQLA---EEQKRLMEM 471
|
...
gi 578824467 287 VEE 289
Cdd:pfam15709 472 AEE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-304 |
8.51e-04 |
|
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: 42.35 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 104 RQKEKDLVLAARLGKALLERNQDMSRQYEQmHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQDELER 183
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 184 QQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLS 263
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578824467 264 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK 304
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQ 1040
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
108-345 |
9.36e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 108 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELER---Q 184
Cdd:pfam07888 28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 185 QIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNqhiiRLESLQAEQVLEIKMLSD 264
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE----RMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 265 RKRELEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAA 343
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLN 247
|
..
gi 578824467 344 TS 345
Cdd:pfam07888 248 AS 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-358 |
1.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 168 SELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQ----------LSMQVHALREDFREK 237
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaleaelaeLEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 238 NSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLsatleenDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQE 317
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRAD--LAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578824467 318 VRLScrqlQVKVEELTEERSLQSSAATSTSLLSEIEQSMEA 358
Cdd:COG4942 174 AELE----ALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
118-337 |
1.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELTDKLEH---LEQEKHELRRRFENREGEWEgRVSELESDVKQLQDELERQQIHLR---EA 191
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRkleEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 192 DREKSRAVQELSEQNQRLLDQLSRASEVER--QLSMQVHALREDFREKNSSTNQHIIRLESLQA---EQVLEIKMLSDRK 266
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEkaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieERIKELEEKEERL 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824467 267 RELEHRLSATLEENDLLQGTVEELQD-RVLILERQGHDK---DLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKrltGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-224 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 112 LAARLGKALLERN--QDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELESDVKQLQDELERQQI 186
Cdd:TIGR02169 817 IEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110
....*....|....*....|....*....|....*...
gi 578824467 187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLS 224
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
134-293 |
1.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 134 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRL---- 209
Cdd:COG1579 2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 210 --LDQLSRASEVErQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG1579 80 eqLGNVRNNKEYE-ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*.
gi 578824467 288 EELQDR 293
Cdd:COG1579 159 EELEAE 164
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-354 |
2.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 174 VKQLQDELERQQIHlrEADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQ--VHALREDFREKNSSTNQHIIRLESL 251
Cdd:COG3096 481 VCKIAGEVERSQAW--QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQqnAERLLEEFCQRIGQQLDAAEELEEL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLI-------LERQGHdkdlQLHQSQLELQEVrLSCRQ 324
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdaLERLRE----QSGEALADSQEV-TAAMQ 633
|
170 180 190
....*....|....*....|....*....|.
gi 578824467 325 LQVKVE-ELTEERSLqsSAATSTSLLSEIEQ 354
Cdd:COG3096 634 QLLERErEATVERDE--LAARKQALESQIER 662
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-353 |
2.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 130 QYEQMHKELTDKLEHLEQEKHELRRRFENREG--EWEGRVSELESDVKQLQDELERQqihlREADREKSRAVQELSEQNQ 207
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 208 RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQ--AEQVLEIKMLSDRKRELEHRLSATLEENDLLQG 285
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824467 286 TVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLScrQLQVKVEELTEER-SLQSSAATSTSLLSEIE 353
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--QVEEKLDELREERdDLQAEIGAVENELEELE 694
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
122-349 |
2.67e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 122 ERNQDMSRQYEQMHKELTDKLEHLE----QEKHELRRRFENREgewegrVSELESDVKQLQDELERQQIHLREADrekSR 197
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTLS------LRQLESRLAQTLDQLQNAQNDLAEYN---SQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 198 AV--QELSEQNQRLLDQ-LSRASEVERQLsmqvhalredfreKNSSTNQHIIRLES---LQAEQVLEIKMLSDRKRELEH 271
Cdd:PRK11281 151 LVslQTQPERAQAALYAnSQRLQQIRNLL-------------KGGKVGGKALRPSQrvlLQAEQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824467 272 rlSATLEenDLLQGTVEELQDRVLILERQghdkdLQLhqsqleLQEVrLSCRQLQVKVEELTEERSLQSSAATSTSLL 349
Cdd:PRK11281 218 --NTQLQ--DLLQKQRDYLTARIQRLEHQ-----LQL------LQEA-INSKRLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
98-236 |
3.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQ-----YEQMHKELTDKLEHLEQEKHELRRRFENREgEWEGRVSELES 172
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLlqllpLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEA 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824467 173 DVKQLQDELERQQIHLREADREksrAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFRE 236
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
114-298 |
4.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 114 ARLGKALLERNQDMsRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEG--RVSELESDVKQLQDELERQQIHL 188
Cdd:PRK03918 241 EELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSM--QVHALREDFREKNSSTNQHIIRLESLQAEQVL-EIKMLSDR 265
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRLTGLTPEKLEkELEELEKA 399
|
170 180 190
....*....|....*....|....*....|...
gi 578824467 266 KRELEHRLSATLEENDLLQGTVEELQDRVLILE 298
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
121-489 |
4.63e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRfENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:pfam05483 70 FENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQK-ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 201 ELSEQNQ---RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAeQVLEIKMLSDRKRELEHRLSATL 277
Cdd:pfam05483 149 ENNATRHlcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV-QAENARLEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 278 EENdlLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEelTEERSLQSSAATSTSLLSEIEQSME 357
Cdd:pfam05483 228 EEE--YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK--LQDENLKELIEKKDHLTKELEDIKM 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 358 AEELEQEREQLRLQLWEAYCQVRYLCSHLRgndsadsavstDSSMDESSETSSAKDVPAGSLRT---ALNELKRLIQSIV 434
Cdd:pfam05483 304 SLQRSMSTQKALEEDLQIATKTICQLTEEK-----------EAQMEELNKAKAAHSFVVTEFEAttcSLEELLRTEQQRL 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578824467 435 DGMEPTVTLLSVEMTALKEERDRLRVTSEDKEPK-EQLQKAIRDRDEAIAKKNAVE 489
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEKKQFE 428
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
118-357 |
5.57e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRrfenregewegRVSELESDVKQLQDELERQQIHLREADREKsr 197
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ-----------EKTELLVEQGRLQLQADRHQEHIRARDSLI-- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 198 avqeLSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSatl 277
Cdd:TIGR00606 371 ----QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE--- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 278 EENDLLQGTVEELQDRVLILER-QGHDKDLQLHQSQLELQEVRLSCRQLQVKVE-ELTEERSLQSSAATSTSLLSEIEQS 355
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQE 523
|
..
gi 578824467 356 ME 357
Cdd:TIGR00606 524 ME 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-358 |
7.05e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 120 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELESDVKQLQDELerqqihl 188
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLeSLQAEQVleiKMLSDR--- 265
Cdd:pfam15921 334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQN---KRLWDRdtg 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 266 --------KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTE 334
Cdd:pfam15921 410 nsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260
....*....|....*....|....*...
gi 578824467 335 ER-SLQSSAATSTSL---LSEIEQSMEA 358
Cdd:pfam15921 487 KKmTLESSERTVSDLtasLQEKERAIEA 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-549 |
9.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 251 LQAE-QVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKV 329
Cdd:COG1196 218 LKEElKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 330 EELTEE-RSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAycQVRYLCSHLRGNDSADSAVSTDSSMDESSEt 408
Cdd:COG1196 298 ARLEQDiARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824467 409 ssakdvpAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAV 488
Cdd:COG1196 375 -------AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578824467 489 ELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHLKERSQPAAA 549
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| |
