|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-338 |
1.82e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 6 IEEKSKLLEKF--SLVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAE 83
Cdd:TIGR02168 679 IEELEEKIEELeeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 84 AKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHIKTLTE 163
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 164 RLLKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEE 243
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 244 LTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklskVDEKI 315
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE----AEALE 960
|
330 340
....*....|....*....|...
gi 1227954602 316 SHATEELETYRKRAKDLEEELER 338
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6-395 |
2.93e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 6 IEEKSKLLEKFS--LVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKR----------IQSLEDE 73
Cdd:TIGR04523 133 KKENKKNIDKFLteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklelllsnLKKKIQK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 74 SKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTfedskvhAEQVLND 153
Cdd:TIGR04523 213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ-------NNKKIKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 154 KESHIKTLTERLLKMK-----DWAAMLGEDITDDDNLELEMNSE-SENGAYLDNppkgaLKKLIhaAKLNASLKTLEGER 227
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQ-----LNEQI--SQLKKELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 228 NQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLHRKLTVEE 298
Cdd:TIGR04523 359 SEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 299 NYRL--------EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLND 370
Cdd:TIGR04523 439 NSEIkdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKD 514
|
410 420
....*....|....*....|....*
gi 1227954602 371 LRKENAhnRQKLTETELKFELLEKD 395
Cdd:TIGR04523 515 LTKKIS--SLKEKIEKLESEKKEKE 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-395 |
2.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 213 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 292
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 293 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 369
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 1227954602 370 DLRKENAHNRQKLTETELKFELLEKD 395
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-395 |
3.00e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 213 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---YQENEMK 289
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 290 LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLN 369
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAA 396
|
170 180
....*....|....*....|....*.
gi 1227954602 370 DLRKENAHNRQKLTETELKFELLEKD 395
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-374 |
5.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 55 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 134
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 135 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAA 214
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 215 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkl 294
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 295 tveenyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 374
Cdd:COG1196 482 ------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-261 |
5.79e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 6 IEEKSKLLEKFSLvqkEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSL-EDESKSLKSQVAEA 84
Cdd:TIGR02169 223 YEGYELLKEKEAL---ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 85 KMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHI------ 158
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdke 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 159 -KTLTERLLKMKDWAAMLGEDI----TDDDNLELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQ 229
Cdd:TIGR02169 380 fAETRDELKDYREKLEKLKREInelkRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQ 459
|
250 260 270
....*....|....*....|....*....|..
gi 1227954602 230 IYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 261
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
56-398 |
6.30e-07 |
|
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: 52.80 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 56 QDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFqmnEERLKIAIKDALN----ENSQLQESQKQLLQEAEVwkeqVS 131
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQlteeKEAQMEELNKAKAAHSFV----VT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 132 ELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYLDNppKGAL 207
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLLDE--KKQF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 208 KKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEl 282
Cdd:pfam05483 428 EKIAEELKgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 283 yQENEMKLHRKLTVEENYRLEKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDN 357
Cdd:pfam05483 507 -EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK 585
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1227954602 358 WLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYA 398
Cdd:pfam05483 586 EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-399 |
7.68e-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: 52.75 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 63 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 135
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 136 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 215
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 216 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 294
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 295 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 374
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 1227954602 375 NAHNRQKLTETELKFELLEKDPYAL 399
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
214-338 |
9.02e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 293
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1227954602 294 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 338
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-337 |
1.38e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 55 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 121
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 122 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 198
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 199 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 275
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954602 276 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 337
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-347 |
1.60e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 18 LVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTfKIFQMNEer 97
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSE-- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 98 lkiaIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGE 177
Cdd:TIGR04523 442 ----IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 178 DITDDDNLELEMNSEsengayldnppkgalkklihAAKLNASLKTLEGERNQIyiqlsEVDKTKEELTEHIKNLQTEQAS 257
Cdd:TIGR04523 518 KISSLKEKIEKLESE--------------------KKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 258 LQSENTHFENENQKLQQKLKVmtelYQENEMKLHRKLTveenyrlEKEEKLSKVDEKISHATEE---LETYRKRAKDLEE 334
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEnekLSSIIKNIKSKKN 641
|
330
....*....|...
gi 1227954602 335 ELERTIHSYQGQI 347
Cdd:TIGR04523 642 KLKQEVKQIKETI 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
20-340 |
2.24e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 20 QKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLK 99
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 100 IAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDI 179
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 180 T------DDDNLELEmNSESEN-----GAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHI 248
Cdd:TIGR04523 569 EieelkqTQKSLKKK-QEEKQElidqkEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 249 KNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYR 326
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFS 727
|
330
....*....|....
gi 1227954602 327 KRAKDLEEELERTI 340
Cdd:TIGR04523 728 KELENIIKNFNKKF 741
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
102-287 |
4.18e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 102 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 181
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 182 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 261
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 1227954602 262 NTHFENENQKLQQKLKVMTELYQENE 287
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-395 |
4.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 6 IEEKSKLLEKfsLVQKEATCEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSLEDESKSLKSQVAEAK 85
Cdd:PRK03918 278 LEEKVKELKE--LKEKAEEYIKLSEFYEEYLDEL--------------REIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 86 MTFKIFQMNEERLKIaikdaLNENSQLQESQKQLLQEAEVWKEQVSELN--------------KQKVTFEDSKVHAEQV- 150
Cdd:PRK03918 342 ELKKKLKELEKRLEE-----LEERHELYEEAKAKKEELERLKKRLTGLTpeklekeleelekaKEEIEEEISKITARIGe 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 151 LNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELeMNSESENGAYLDNPPKGALKKLihaAKLNASLKTLEGERNQI 230
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 231 --YIQLSEVDKTKEELTEHIKNLQTEQasLQSENTHFENENQKLQqKLK-----VMTELYQENEMKlhRKLTVEENYRLE 303
Cdd:PRK03918 493 seLIKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLI-KLKgeiksLKKELEKLEELK--KKLAELEKKLDE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 304 KEEKLSKVDEKIshateeletyRKRAKDLEEELERTIHSYqgqiisheKKAHDNWLAARNAERNLNDLRKENAHNRQKLT 383
Cdd:PRK03918 568 LEEELAELLKEL----------EELGFESVEELEERLKEL--------EPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
410
....*....|..
gi 1227954602 384 ETELKFELLEKD 395
Cdd:PRK03918 630 KAFEELAETEKR 641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-340 |
4.81e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 96 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 174
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 175 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 252
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 253 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 332
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1227954602 333 EEELERTI 340
Cdd:COG4942 226 EALIARLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-353 |
1.28e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 207 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 282
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227954602 283 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 353
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
28-395 |
1.34e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 28 LNRSNSELE---DEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKD 104
Cdd:TIGR04523 105 LSKINSEIKndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK---KQKEELENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 105 ALNENSQLQESQKQLL-------------QEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDw 171
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLklelllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 172 aamLGEDITD---DDNLELEMN----SESENGAYLDNPPKGALKKLIHA---AKLNASLKTLEGERNQIYIQLSEVDKTK 241
Cdd:TIGR04523 261 ---EQNKIKKqlsEKQKELEQNnkkiKELEKQLNQLKSEISDLNNQKEQdwnKELKSELKNQEKKLEEIQNQISQNNKII 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 242 EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVmteLYQENEMKLHRKLTVEE-----NYRLEKEEKLSK-VDEKI 315
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK---LKKENQSYKQEIKNLESqindlESKIQNQEKLNQqKDEQI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 316 SHATEELETYRKRAKDLEEE---LERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELL 392
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
...
gi 1227954602 393 EKD 395
Cdd:TIGR04523 495 EKE 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-338 |
2.65e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 2 LSGLIEEKSKLLEKfsLVQKEAT----CEKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSL 77
Cdd:TIGR02169 714 ASRKIGEIEKEIEQ--LEQEEEKlkerLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 78 KSQVAEakmtfkifqmneerlkiaIKDALNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK--- 154
Cdd:TIGR02169 778 EEALND------------------LEARLSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtle 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 155 ----ESHIKTLTERLLKMKDWAAMLGEDItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQ 229
Cdd:TIGR02169 828 keylEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 230 IYIQLSEVDKTKEELT-------EHIKNLQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRL 302
Cdd:TIGR02169 894 LEAQLRELERKIEELEaqiekkrKRLSELKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQ 961
|
330 340 350
....*....|....*....|....*....|....*.
gi 1227954602 303 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 338
Cdd:TIGR02169 962 RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-416 |
3.20e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 54 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 133
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 134 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 213
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 293
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 294 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 373
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1227954602 374 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 416
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
65-395 |
3.65e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 65 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 143
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 144 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 223
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 224 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 296
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 297 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 366
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 1227954602 367 NLNDLRKENAHNRQKLTETELKFELLEKD 395
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
127-338 |
4.29e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 127 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 193
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 194 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 260
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954602 261 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 338
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-400 |
4.70e-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: 46.97 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLqsenthfENENQKLQQKLKvmtELYQENEMkLHRK 293
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQILRERLA---NLERQLEE-LEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 294 LTVEENYRLEKEEKLSKVDEKISHATEELETYR---KRAKDLEEELERTIHSYQGQIISHEKKAHD--NWLAARNAERNL 368
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEaelEELEAELEELESRLEELEEQLETLRSKVAQleLQIASLNNEIER 404
|
170 180 190
....*....|....*....|....*....|..
gi 1227954602 369 NDLRKENAHNRQKLTETELKFELLEKDPYALD 400
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-259 |
6.83e-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: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 53 HSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 125
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 126 WKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayldNPPKG 205
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE-----ELSLE 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1227954602 206 ALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 259
Cdd:TIGR02169 955 DVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-394 |
8.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 220 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEEN 299
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 300 YR--LEKEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAH 377
Cdd:COG4717 148 LEelEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1227954602 378 NRQKLTETELKFELLEK 394
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
34-346 |
2.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 34 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 107
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 108 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 186
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 187 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 266
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 267 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 346
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
65-394 |
2.82e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 65 KRIQSLEDESKSLKSQVAEAKMTF-----KIFQMNEERLKIAI-----KDALNEN-SQLQESQKQLLQ------------ 121
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLkknkdKINKLNSDLSKINSeikndKEQKNKLeVELNKLEKQKKEnkknidkfltei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 122 -----EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN-SESEN 195
Cdd:TIGR04523 148 kkkekELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 196 gayldnppkgalkklihaAKLNASLKTLEGERNQIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENT---HFENE 268
Cdd:TIGR04523 228 ------------------NQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 269 NQKLQQKLKVMTELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQ 344
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQ 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1227954602 345 GQIISHEKKAHDNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 394
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
58-394 |
3.47e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 58 ELMADISKRIQSLEDEskslKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEaevwkeqVSELnkQK 137
Cdd:pfam01576 268 ELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQE-------VTEL--KK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 138 VTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GEDITDDDNLELEMNSESENGAYLDNPPKGalkklih 212
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAKQALESENAELQAELRTLQQAKQDSEHKR------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 213 aaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQEnemklhr 292
Cdd:pfam01576 408 --------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD------- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 293 kltVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE---ELERTIHSYQGQIISHEKKAHDNWLAARNAERNLN 369
Cdd:pfam01576 473 ---TQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
330 340
....*....|....*....|....*
gi 1227954602 370 DLRKENAHNRQKLTETELKFELLEK 394
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-339 |
4.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 291
Cdd:COG4717 105 EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1227954602 292 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 339
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
214-402 |
4.72e-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: 43.21 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY---------- 283
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 284 -----------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 349
Cdd:COG4942 117 grqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1227954602 350 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 402
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
53-388 |
6.21e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 53 HSEQDELMADISKRIQSLEDESKSLKS-QVAEAKMTFKIFQMNEERLKIAIKdalnenSQLQESQKQLLQEAEVWKEQVS 131
Cdd:TIGR01612 488 NSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLIH 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 132 ELNKQKVTFEDSKVHAeqvlndkESHIKTLTERLLKMKDwaamlgeDITDDDNLELEMNSESENGAYLDNPPKGA--LKK 209
Cdd:TIGR01612 562 EIKKELEEENEDSIHL-------EKEIKDLFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLKK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 210 LIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTEQASLQSENTH-FENENQKLQQKLkvmTELYQENE 287
Cdd:TIGR01612 628 II--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKENA 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 288 MKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAHD 356
Cdd:TIGR01612 689 ID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILED 759
|
330 340 350
....*....|....*....|....*....|...
gi 1227954602 357 NWLAARNAERNLNDLRKENAH-NRQKLTETELK 388
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
57-169 |
6.62e-04 |
|
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: 42.31 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 57 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 136
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 1227954602 137 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 169
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
57-285 |
7.24e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 57 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 123
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 124 EVWKEQVSELNKQKVTFEDSKVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 192
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 193 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 251
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270
....*....|....*....|....*....|....*..
gi 1227954602 252 QTEQASLQSENTH-FE--NENQKLQQKLKVMTELYQE 285
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEE 1761
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
55-287 |
7.98e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 55 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 133
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 134 NKQKVTFEDSKVHAEQVLNDKESHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPK 204
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 205 GALKKLIHAAKLNASLKTLEGE-RNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY 283
Cdd:pfam12128 440 YRLKSRLGELKLRLNQATATPElLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
....
gi 1227954602 284 QENE 287
Cdd:pfam12128 520 SALD 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-309 |
9.74e-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: 42.74 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 18 LVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEER 97
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE----------LESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 98 LKIAIKDAlnenSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGE 177
Cdd:TIGR02168 332 LDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 178 DITD-DDNLElemNSESENGAYLDNPPKGALKKLIHA-AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQ 255
Cdd:TIGR02168 408 RLERlEDRRE---RLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 256 ASLQSENTHFENENQKLQQKLKVMTELYQENEMK------LHRKLTVEENYRLEKEEKLS 309
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAIEAALG 544
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-344 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 220 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 293
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954602 294 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 344
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
60-285 |
1.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 60 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNeerlkiaikdalNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 139
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 140 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 213
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954602 214 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 285
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
7-352 |
1.67e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 7 EEKSKLLEKfsLVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKhseqdelmADISKRIQSLEDESKSLKSQVAEAKM 86
Cdd:pfam02463 195 LKLQELKLK--EQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER--------IDLLQELLRDEQEEIESSKQEIEKEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 87 TFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLL 166
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 167 KMKDWAAMLGEDITDDDNLELEMNSESENGAYldnppkgaLKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELT- 245
Cdd:pfam02463 345 KELEIKREAEEEEEEELEKLQEKLEQLEEELL--------AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARq 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 246 --EHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENEMKLHRKLTVEENYRLEKEEKLSKvdEKISHATEELE 323
Cdd:pfam02463 417 leDLLKEEKKEELEILEEEEESIELKQGKLTEEK--EELEKQELKLLKDELELKKSEDLLKETQLVK--LQEQLELLLSR 492
|
330 340
....*....|....*....|....*....
gi 1227954602 324 TYRKRAKDLEEELERTIHSYQGQIISHEK 352
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
226-293 |
1.90e-03 |
|
Regulator of replication initiation timing YabA [Replication, recombination and repair];
Pssm-ID: 443564 [Multi-domain] Cd Length: 107 Bit Score: 38.31 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954602 226 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 293
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
20-385 |
2.09e-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: 41.49 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 20 QKEATCEKLNRSNSELEDEilclEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLK 99
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDIL----QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 100 IAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLG 176
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 177 EDITDDDNL---ELEMNSESENGAYLDNPPKGALKKLIHAAK--LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNL 251
Cdd:TIGR00618 542 TSEEDVYHQltsERKQRASLKEQMQEIQQSFSILTQCDNRSKedIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 252 QtEQASLQSENTHFENENQKLQQKLKVMTE-----LYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHAT------- 319
Cdd:TIGR00618 622 Q-PEQDLQDVRLHLQQCSQELALKLTALHAlqltlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemla 700
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954602 320 ------EELETYRKRAKDLEEELERTIHSyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 385
Cdd:TIGR00618 701 qcqtllRELETHIEEYDREFNEIENASSS-LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
62-337 |
2.43e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 62 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL---LQEAEV----WKEQVSELN 134
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseLEEAREavedRREEIEELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 135 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITdddnlELEMNSESENGAYLDNppkgalKKLIHAA 214
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREER-------DELREREA-----ELEATLRTARERVEEA------EALLEAG 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 215 KLNASLKTLEGErnQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHF------ENENQKLQQKLKVMTELYQENEM 288
Cdd:PRK02224 453 KCPECGQPVEGS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRE 530
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1227954602 289 KLHRKLTVEENYRLEKEEKLSKVDEKISHAT---EELETYRKRAKDLEEELE 337
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAeaeEEAEEAREEVAELNSKLA 582
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
31-380 |
2.52e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 31 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEN- 109
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERk 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 110 -------SQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 181
Cdd:pfam12128 678 dsanerlNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 182 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 252
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 253 TEQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 330
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1227954602 331 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 380
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-353 |
2.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKE--ELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 291
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227954602 292 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKK 353
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-338 |
3.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 60 MADISKRIQSLEDESKSLKSQVAEAKMTFKifqmNEERLkIAIKDALNENSQLQESQKQL--------LQEAEVWKEQVS 131
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK----KESEL-IKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 132 ELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEmNSESENGAYLDnpPKGALK 208
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLE--LKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 209 KLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----EQASLQSENTHFENENQKLQQKLKVMTELY 283
Cdd:PRK03918 613 EL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954602 284 QENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 338
Cdd:PRK03918 690 EEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
70-332 |
3.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 70 LEDESKSLKSQVAEAKMTFkifQMNEERLKIAIKDALNENSQLQESQKQLlQEAEVwkeQVSELNkqkvtfEDskVHAEQ 149
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQKNNALKKI-RELEA---QISELQ------ED--LESER 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 150 VLNDK-ESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihaAKLNASLKTLEGERN 228
Cdd:pfam01576 285 AARNKaEKQRRDLGEELEALKTEL----EDTLDTTAAQQELRSKRE-------------------QEVTELKKALEEETR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 229 QIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMK----------LHRKL 294
Cdd:pfam01576 342 SHEAQLQEMRQkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKrkklegqlqeLQARL 421
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1227954602 295 TVEENYRLEKEEKLSKVD---EKISHATEELETYR-KRAKDL 332
Cdd:pfam01576 422 SESERQRAELAEKLSKLQselESVSSLLNEAEGKNiKLSKDV 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
214-366 |
3.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 214 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL-KVMTELYQE------- 285
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSggsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 286 -------------NEMKLHRKLTVEENYRLEK----EEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQI- 347
Cdd:COG3883 106 dvllgsesfsdflDRLSALSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLa 185
|
170 180
....*....|....*....|
gi 1227954602 348 -ISHEKKAHDNWLAARNAER 366
Cdd:COG3883 186 qLSAEEAAAEAQLAELEAEL 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
303-386 |
4.74e-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: 39.75 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 303 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 382
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 1227954602 383 TETE 386
Cdd:COG4942 100 EAQK 103
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
226-384 |
6.46e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 226 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQAslqsenthfENENQKLQQKLKVMTELyqenemklhrkLTVEENYRLEKE 305
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA---------EEALEEIEERIDQLYDL-----------LEKEVDAKKYVE 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227954602 306 EKLSKVDEKISHATEELetyrkraKDLEEELERTIHSYqgqIISHEKKAHdnwlaARNAERNLNDLRKENAHNRQKLTE 384
Cdd:pfam06160 291 KNLPEIEDYLEHAEEQN-------KELKEELERVQQSY---TLNENELER-----VRGLEKQLEELEKRYDEIVERLEE 354
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
95-417 |
6.92e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 95 EERLKIAIKDALNENSQ--LQESQKQLLQEaevwKEQVSELNKQKVTF-EDSKVHAEQVLNDKESHIKTLTERLLKMKDW 171
Cdd:COG5022 858 KKRFSLLKKETIYLQSAqrVELAERQLQEL----KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 172 AAMLgEDITDDDNLELEMNSESENGAYLDnppkgalkklihaakLNASLKTLEGERNQIYIQL-----------SEVDKT 240
Cdd:COG5022 934 KKLL-NNIDLEEGPSIEYVKLPELNKLHE---------------VESKLKETSEEYEDLLKKStilvregnkanSELKNF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 241 KEELTEHIKNLQTEQASLQS--ENTHFENENQKLQQKLKVM-TELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISH 317
Cdd:COG5022 998 KKELAELSKQYGALQESTKQlkELPVEVAELQSASKIISSEsTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 318 ATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNwlaARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPY 397
Cdd:COG5022 1078 LDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQF---IVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
330 340
....*....|....*....|
gi 1227954602 398 ALDVPNTAFGREHSPYGPSP 417
Cdd:COG5022 1155 ELDGLFWEANLEALPSPPPF 1174
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
205-371 |
8.77e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 205 GALKKLIHAAKLNASLKTLEGERNQIYIQLsevdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLkvmtelyQ 284
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKALL-------DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-------E 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 285 ENEMKLHRKLTvEENYRLEKEEkLSKVDEKIshaTEELETYRKRAKDLEEELERTIHSYQGQiISHEKKAHDNWLAARNA 364
Cdd:cd22656 160 TLEKALKDLLT-DEGGAIARKE-IKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAK-LAAALRLIADLTAADTD 233
|
....*..
gi 1227954602 365 ERNLNDL 371
Cdd:cd22656 234 LDNLLAL 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
57-374 |
9.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 57 DELMADIsKRIQSLEDESKSLKSQVAEAKMTF-KIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNK 135
Cdd:COG4717 149 EELEERL-EELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 136 QKVTFEDSKVHA--EQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNL-----------ELEMNSESENGAYLDNP 202
Cdd:COG4717 228 ELEQLENELEAAalEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 203 PKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSEntHFENENQKLQQKLKVMTE- 281
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEe 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 282 -------LYQENEMKLHRKLTVEENYRLEK---------------EEKLSKVDEKISHATEELETYRKRAKDLEEELERT 339
Cdd:COG4717 386 elraaleQAEEYQELKEELEELEEQLEELLgeleellealdeeelEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1227954602 340 IHSYQGQIISHEKKAHDN--------WLAARNAERNLNDLRKE 374
Cdd:COG4717 466 EEDGELAELLQELEELKAelrelaeeWAALKLALELLEEAREE 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
226-338 |
9.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954602 226 ERNQIYIQLSEVDKTKEE-LTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR--KLTVEEnyrl 302
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEEnLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEE---- 154
|
90 100 110
....*....|....*....|....*....|....*.
gi 1227954602 303 EKEEKLSKVDEKISHatEELETYRKRAKDLEEELER 338
Cdd:PRK12704 155 AKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADK 188
|
|
| |
