|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
83-397 |
7.20e-121 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 355.38 E-value: 7.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 83 NEKVTMQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYGPGSCRgldrDYSKYHLTIEDLKSKIISSTAANANIILQ 162
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 163 IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAG-GNV 241
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083132 322 SATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDEN 397
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-387 |
1.18e-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: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 188 EADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHE-EEMKVLQCAaggnvnvEMNAAPGVDLTVLLNNMRAEYEA 266
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLE-------ERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 267 LAEQNRRDAEAwfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETE---GNYCSQL 343
Cdd:TIGR02168 770 LEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLEEQI 847
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907083132 344 AQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
94-368 |
8.70e-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: 48.51 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 94 RLASYLDNVKALEEANSELERKIKTWHEKygpgsCRGLDRDYSKYHLTIEDLKSKI---------ISSTAANANIILQID 164
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEE-----LEELTAELQELEEKLEELRLEVseleeeieeLQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 165 NARLAADDFRLKY-ENELtlhQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAGGNVNV 243
Cdd:TIGR02168 301 EQQKQILRERLANlERQL---EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 244 E---MNAAPGVDLTV----LLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAAtsaRTELTELKRSLQTLEI 316
Cdd:TIGR02168 378 EeqlETLRSKVAQLElqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL---QAELEELEEELEELQE 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083132 317 ELQSLSATKHSLECSLAETEGNYCS---QLAQIQAQISALEEQLHQVRTETEGQK 368
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAaerELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
261-458 |
3.63e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 261 RAEYEALAEQnrrdaEAWFQEKSATLQQQISndlgaatSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGNYC 340
Cdd:TIGR02169 722 EKEIEQLEQE-----EEKLKERLEELEEDLS-------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 341 -SQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETY-CRLIDGDENSCSVSKGFEsgtSGNSPKDVS 418
Cdd:TIGR02169 790 hSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELqEQRIDLKEQIKSIEKEIE---NLNGKKEEL 866
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907083132 419 KTTLVKT--VVEEIDQRGKVLSSRIHSIEEKMSKMSNGKAEQ 458
Cdd:TIGR02169 867 EEELEELeaALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-374 |
4.10e-05 |
|
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: 46.20 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 141 TIEDLKSKIISSTAANANIILQIDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMT 220
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 221 YLKKNHEEEMKVLQCAAGGNVNVEMNAAPGVDLTVL----LNNMRAEYEAL----------AEQNRRDAEAWfqEKSAT- 285
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreaLDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEd 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 286 LQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETE 365
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR----SELEELSEELRELESKRSELRRELE 918
|
....*....
gi 1907083132 366 GQKLEHEQL 374
Cdd:TIGR02168 919 ELREKLAQL 927
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
302-384 |
4.38e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 302 TELTELKRSLQTLEIELQSLSAtkhslecslaETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHL 381
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
...
gi 1907083132 382 EKE 384
Cdd:COG0542 481 EQR 483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-386 |
8.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 261 RAEYEALAEQNRR--DAEAWFQEKSATLQQQI-SNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEG 337
Cdd:COG4913 301 RAELARLEAELERleARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907083132 338 NYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-430 |
1.17e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 144 DLKSKIISSTAANANIILQIDNARLAADdFRLK--YENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLS--EEM 219
Cdd:pfam05483 187 DLNNNIEKMILAFEELRVQAENARLEMH-FKLKedHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTflLEE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 220 TYLKKNHEEEMKVLQcaaggNVNVEMNAAPGVDLTVLLNNMRAEYEalaeqnrrdaeawfqeKSATLQQQISNDLGAATS 299
Cdd:pfam05483 266 SRDKANQLEEKTKLQ-----DENLKELIEKKDHLTKELEDIKMSLQ----------------RSMSTQKALEEDLQIATK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 300 ARTELTELKRSlqtlEIELQSLSATKHSLecSLAETEGNYCSQ---LAQIQAQISALEEQLHQVRTETEGQKLEHEQLLD 376
Cdd:pfam05483 325 TICQLTEEKEA----QMEELNKAKAAHSF--VVTEFEATTCSLeelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907083132 377 IKAHLEKEIETYCRLIDGDENSCSVSKGFESGTSGNSPKDVSKTTLVKTVVEEI 430
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-387 |
1.22e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 261 RAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGN-- 338
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907083132 339 -YCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:COG1196 306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-339 |
3.18e-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: 43.51 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 88 MQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYgpgscRGLDRDYSKYHLTIEDLKSKII---SSTAANANIILQ-- 162
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERL-----ANLERQLEELEAQLEELESKLDelaEELAELEEKLEElk 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 163 --IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEemkvlqcaaggn 240
Cdd:TIGR02168 351 eeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER------------ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 241 vnvemnaapgvdltvLLNNMRAEYEALAEQNRRDAEAWFQEKS---ATLQQQISNDLGAATSARTELTELKRSLQTLEIE 317
Cdd:TIGR02168 419 ---------------LQQEIEELLKKLEEAELKELQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250 260
....*....|....*....|..
gi 1907083132 318 LQSLSATKHSLECSLAETEGNY 339
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFS 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-386 |
3.23e-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: 43.51 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 93 NRLASYLDNVKALEEANSELERKIKTWH------EKYgpgscRGLDRDYSKYHLTI-----EDLKSKI--ISSTAANANI 159
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLErqaekaERY-----KELKAELRELELALlvlrlEELREELeeLQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 160 ILQIDNARLAADDFRLkyeNELTL-HQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEemkvlqcaag 238
Cdd:TIGR02168 254 ELEELTAELQELEEKL---EELRLeVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 239 gnvnvemnaapgvdltvlLNNMRAEYEALAEQNRRDAEAWfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIEL 318
Cdd:TIGR02168 321 ------------------LEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083132 319 QSLSATKHSLEcslaetegnycSQLAQIQAQISALEEQLHQV---------RTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:TIGR02168 382 ETLRSKVAQLE-----------LQIASLNNEIERLEARLERLedrrerlqqEIEELLKKLEEAELKELQAELEELEE 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-368 |
3.85e-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: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 162 QIDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLqcAAGGNV 241
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 242 NVEMNAAPGvdLTVLLNN-------MRAEY-EALAEQNRRDAEAwFQEKSATLQQQISndlgAATSARTELTELKRSLQT 313
Cdd:COG4942 113 LYRLGRQPP--LALLLSPedfldavRRLQYlKYLAPARREQAEE-LRADLAELAALRA----ELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083132 314 LEIELQSLSATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQK 368
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
261-390 |
4.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 261 RAEYEALAEQNRRDAEAwfQEKSATLQQQISNDLGA--ATSARTELTELKRSLQTLEIELQSLSAtkhslecslaetegn 338
Cdd:COG4717 384 EEELRAALEQAEEYQEL--KEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEE--------------- 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907083132 339 ycsQLAQIQAQISALEEQLHQVRTETEGQKLEHEQlldikAHLEKEIETYCR 390
Cdd:COG4717 447 ---ELEELREELAELEAELEQLEEDGELAELLQEL-----EELKAELRELAE 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
265-448 |
5.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 265 EALAEQNRRDAEAwfQEKSATLQQQIS--NDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLEcSLAEtegnycsQ 342
Cdd:COG4913 624 EELAEAEERLEAL--EAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA-ALEE-------Q 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 343 LAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDENSCsvskgFEsgtsgNSPKDVSKTTL 422
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----LE-----ERFAAALGDAV 763
|
170 180
....*....|....*....|....*.
gi 1907083132 423 VKTVVEEIDQRGKVLSSRIHSIEEKM 448
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-386 |
6.05e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 165 NARLAADDFRLKYENELtlhQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAGG-NVNV 243
Cdd:TIGR02169 660 RAPRGGILFSRSEPAEL---QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 244 EMNAAPGVDLTVL---LNNMRAEYEALA---EQNRRDAEAwFQEKSATL-----QQQISNDLGAATSARTELTELKRSLQ 312
Cdd:TIGR02169 737 ERLEELEEDLSSLeqeIENVKSELKELEariEELEEDLHK-LEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083132 313 TLEIELQSLSATKHSLECSLAETEG--NYC-SQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEqrIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
272-393 |
1.69e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.77 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 272 RRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGNYcsQLAQIQA--- 348
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEV--EQAELRAkal 746
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907083132 349 QISAlEEQLHQVRTETEgQKLEHEQLLD------IKAHLEKEIETYCRLID 393
Cdd:PTZ00491 747 RIEA-EAELEKLRKRQE-LELEYEQAQNeleiakAKELADIEATKFERIVE 795
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
257-351 |
1.76e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 257 LNNMRAEYEALAEQNRRDAE-------AWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLE 329
Cdd:pfam07902 229 LDDLRAEFTRSNQGMRTELEskisglqSTQQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNYSSLTQTVKGLQ 308
|
90 100
....*....|....*....|..
gi 1907083132 330 CSLAETEGNYCSQLAQIQAQIS 351
Cdd:pfam07902 309 STVSDPNSKLESRITQLAGLIE 330
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
176-387 |
1.83e-03 |
|
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: 40.72 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 176 KYENELTLHQNVEADINGLRRVL------DELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQcaaggnvnvemNAAP 249
Cdd:TIGR00618 271 ELRAQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK-----------QQSS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 250 GVDLTVLLNNMRAEYEALAEQNrrDAEAWFQEKSA----------TLQQQISNDLGAATSARTELTELKRSLQTLEIELQ 319
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAH--EVATSIREISCqqhtltqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083132 320 SLSATKHSL-----ECSLAETEGNYCSQLAQIQAQISALEEQlHQVRTEtEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:TIGR00618 418 AFRDLQGQLahakkQQELQQRYAELCAAAITCTAQCEKLEKI-HLQESA-QSLKEREQQLQTKEQIHLQETRK 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
266-363 |
2.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 266 ALAEQNRRDAEawfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQ 345
Cdd:COG4942 15 AAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAE 87
|
90
....*....|....*...
gi 1907083132 346 IQAQISALEEQLHQVRTE 363
Cdd:COG4942 88 LEKEIAELRAELEAQKEE 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
296-460 |
2.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 296 AATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLl 375
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELAELEKEIAEL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 376 diKAHLEKEIETYCRLIDGDENSCSVSKgFESGTSGNSPKDVSKT-TLVKTVVEEIDQRGKVLSSRIHSIEEKMSKMSNG 454
Cdd:COG4942 96 --RAELEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRlQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
....*.
gi 1907083132 455 KAEQRV 460
Cdd:COG4942 173 RAELEA 178
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
178-372 |
2.47e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 178 ENELTLHQNVEADINGLRRVLDELtlcrtdqELQYESLSEEMTYLKKNHEEEMKVLqcaaggNVNVEMNAAPGVDLTVLL 257
Cdd:cd00176 36 EALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 258 NNMRAEYEALAEQnrRDAEAWFQEKSATLQQQ-ISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLEcslaetE 336
Cdd:cd00176 103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907083132 337 GNYCSQLAQIQAQISALEEQLHQVRTETE--GQKLEHE 372
Cdd:cd00176 175 EGHPDADEEIEEKLEELNERWEELLELAEerQKKLEEA 212
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
256-363 |
2.61e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.83 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 256 LLNNM--RAEYEAL--AEQNRRDAEAWFQEKSATL-----QQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATkh 326
Cdd:COG3524 166 LVNQLseRAREDAVrfAEEEVERAEERLRDAREALlafrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSY-- 243
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907083132 327 slecsLAETEgnycSQLAQIQAQISALEEQLHQVRTE 363
Cdd:COG3524 244 -----LSPNS----PQVRQLRRRIAALEKQIAAERAR 271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
289-394 |
3.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 289 QISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVrTETEGQK 368
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE----ERIEELKKEIEELEEKVKEL-KELKEKA 292
|
90 100 110
....*....|....*....|....*....|...
gi 1907083132 369 LEHEQL-------LDIKAHLEKEIETYCRLIDG 394
Cdd:PRK03918 293 EEYIKLsefyeeyLDELREIEKRLSRLEEEING 325
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
138-364 |
5.84e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.85 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 138 YHLTIEDLKSKIISSTAANANIILQI--DNARL------AADDFRLKYENELTL---HQNVEAD----------INGLRR 196
Cdd:smart00787 68 YQFSCKELKKYISEGRDLFKEIEEETliNNPPLfkeyfsASPDVKLLMDKQFQLvktFARLEAKkmwyewrmklLEGLKE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 197 VLDE-LTLCRTDQEL--QYE----SLSEEMTYLKKNHEEEMKVLQcaaggNVNVEMNAAPGVDLTVLlnnmraeyealae 269
Cdd:smart00787 148 GLDEnLEGLKEDYKLlmKELellnSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRA------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 270 qnrrdaeawfQEKSATLQQQISNDlgaatsaRTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQA- 348
Cdd:smart00787 210 ----------KEKLKKLLQEIMIK-------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAE----KKLEQCRGf 268
|
250
....*....|....*....
gi 1907083132 349 ---QISALEEQLHQVRTET 364
Cdd:smart00787 269 tfkEIEKLKEQLKLLQSLT 287
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
141-448 |
6.95e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.11 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 141 TIEDLKSKIISSTAANANIILQIDNARLAADDFRL------------KYENELTLHQNVEADI---NGLR-RVLDELTLC 204
Cdd:PLN02939 82 TVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQtnskdgeqlsdfQLEDLVGMIQNAEKNIlllNQARlQALEDLEKI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 205 RTDQElqyeSLSEEMTYLKKNHEEEMKVLQCAAGGNVNVEMNAApgvdltvLLNNMRAEYEALAEQNRRDAEAWFQEKSA 284
Cdd:PLN02939 162 LTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEE-------QLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 285 TLQQQIS--NDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETegnycsqlaqiQAQISaleeQLHQVRT 362
Cdd:PLN02939 231 LKEENMLlkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVA-----------QEDVS----KLSPLQY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 363 ETEGQKLEHEQLLDIKAhlEKEIETYCRLIDGDEN-SCSVSKGFESGTSGNspkdVSKTTLVKtvVEEIDQRGKVLSSRI 441
Cdd:PLN02939 296 DCWWEKVENLQDLLDRA--TNQVEKAALVLDQNQDlRDKVDKLEASLKEAN----VSKFSSYK--VELLQQKLKLLEERL 367
|
....*..
gi 1907083132 442 HSIEEKM 448
Cdd:PLN02939 368 QASDHEI 374
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
252-388 |
7.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 252 DLTVLLNNMRAEYEALAEQ--NRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLE 329
Cdd:COG4372 49 QLREELEQAREELEQLEEEleQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083132 330 CSLAETEGNY---CSQLAQIQAQISALEEQLHQVRTETEgqKLEHEQLLDIKAHLEKEIETY 388
Cdd:COG4372 129 QQRKQLEAQIaelQSEIAEREEELKELEEQLESLQEELA--ALEQELQALSEAEAEQALDEL 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
257-387 |
8.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.46 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 257 LNNMRAEYEAlAEQNRRDAEAwfqeKSATLQQQISNDLGAATSART--ELTELKRSLQTLEIELQSLSAT---------- 324
Cdd:COG3206 221 LSELESQLAE-ARAELAEAEA----RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARytpnhpdvia 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083132 325 --------KHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDikahLEKEIET 387
Cdd:COG3206 296 lraqiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEV 362
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
257-386 |
9.35e-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: 37.60 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083132 257 LNNMRAEYEALAEQNRRdaeawFQEKSATLQQQISND---LGAATSAR------TELTELKRSLQTLEIELQSLSATKHS 327
Cdd:COG1579 47 LEAAKTELEDLEKEIKR-----LELEIEEVEARIKKYeeqLGNVRNNKeyealqKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083132 328 LECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETEGqklEHEQLLDIKAHLEKEIE 386
Cdd:COG1579 122 LEEELAELE----AELAELEAELEEKKAELDEELAELEA---ELEELEAEREELAAKIP 173
|
|
| |
