|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-389 |
6.56e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 57 IEEKSKLLEKF--SLVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAE 134
Cdd:TIGR02168 679 IEELEEKIEELeeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 135 AKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHIKTLTE 214
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 215 RLLKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEE 294
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 295 LTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklskVDEKI 366
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE----AEALE 960
|
330 340
....*....|....*....|...
gi 1227954611 367 SHATEELETYRKRAKDLEEELER 389
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKE 983
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-449 |
1.07e-08 |
|
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: 58.58 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 45 REKKLALMLSGLIEEKSKLLEKFSLVqkEATCEKLNR--SNSELEDEILclekeLKEEKSKHSEQDELmADISKRIQSLE 122
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLL--EESRDKANQleEKTKLQDENL-----KELIEKKDHLTKEL-EDIKMSLQRSM 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 123 DESKSLKSQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEAEVwkeqVSELNKQKVTFEDSKVHAEQVL 202
Cdd:pfam05483 310 STQKALEEDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHSFV----VTEFEATTCSLEELLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 203 NDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYLDNppKGALKKLIHAAK-----LNASLKT 273
Cdd:pfam05483 373 EKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLLDE--KKQFEKIAEELKgkeqeLIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 274 LEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTElyQENEMKLHRKLTVEENYRL 353
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--EASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 354 EKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAH 428
Cdd:pfam05483 526 KKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
410 420
....*....|....*....|.
gi 1227954611 429 NRQKLTETELKFELLEKDPYA 449
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSA 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-398 |
6.16e-08 |
|
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: 56.18 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 69 LVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTfKIFQMNEer 148
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSE-- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 149 lkiaIKDALNENSQLQESQKQLLQEAEVWKEQVSEL----NKQKVTFEDSKvhaeQVLNDKESHIKTLTERLLKMKDWAA 224
Cdd:TIGR04523 442 ----IKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsiNKIKQNLEQKQ----KELKSKEKELKKLNEEKKELEEKVK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 225 MLGEDITDDDNLELEMNSESengayldnppkgalkklihaAKLNASLKTLEGERNQIyiqlsEVDKTKEELTEHIKNLQT 304
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEK--------------------KEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNK 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 305 EQASLQSENTHFENENQKLQQKLKVmtelYQENEMKLHRKLTveenyrlEKEEKLSKVDEKISHATEE---LETYRKRAK 381
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEnekLSSIIKNIK 637
|
330
....*....|....*..
gi 1227954611 382 DLEEELERTIHSYQGQI 398
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETI 654
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-312 |
8.64e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 45 REKKLALMLSGLIEEKSKLLEKFSLVQKEAT---CEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSL 121
Cdd:TIGR02169 205 REREKAERYQALLKEKREYEGYELLKEKEALerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 122 -EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQ 200
Cdd:TIGR02169 285 gEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 201 VLNDKESHI-------KTLTERLLKMKDWAAMLGEDI----TDDDNLELEMNSESENGAYLDNPPKGA---LKKLIHAAK 266
Cdd:TIGR02169 365 ELEDLRAELeevdkefAETRDELKDYREKLEKLKREInelkRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKE 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1227954611 267 -LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 312
Cdd:TIGR02169 445 dKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-446 |
1.52e-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: 55.06 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 264 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 343
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 344 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 420
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 1227954611 421 DLRKENAHNRQKLTETELKFELLEKD 446
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
264-446 |
2.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 264 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---YQENEMK 340
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 341 LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLN 420
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAA 396
|
170 180
....*....|....*....|....*.
gi 1227954611 421 DLRKENAHNRQKLTETELKFELLEKD 446
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-391 |
2.71e-07 |
|
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: 54.26 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 56 LIEEKSKLLEKFSLV-----QKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKS 130
Cdd:TIGR04523 389 LESQINDLESKIQNQeklnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 131 QVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIK 210
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 211 TLTERLLKMKDWAAMLGEDIT------DDDNLELEmNSESEN-----GAYLDNPPKGALKKLIHAAKLNASLKTLEGERN 279
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKNKEieelkqTQKSLKKK-QEEKQElidqkEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 280 QIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEE 357
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLP 707
|
330 340 350
....*....|....*....|....*....|....
gi 1227954611 358 KLSKVDEKISHATEELETYRKRAKDLEEELERTI 391
Cdd:TIGR04523 708 KLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-450 |
2.93e-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: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 114 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 186
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 187 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 266
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 267 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 345
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 346 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 425
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 1227954611 426 NAHNRQKLTETELKFELLEKDPYAL 450
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-425 |
4.00e-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: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 106 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 185
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 186 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAA 265
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 266 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkl 345
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 346 tveenyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 425
Cdd:COG1196 482 ------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
79-446 |
4.56e-07 |
|
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: 53.49 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 79 LNRSNSELE---DEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKD 155
Cdd:TIGR04523 105 LSKINSEIKndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK---KQKEELENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 156 ALNENSQLQESQKQLL-------------QEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDw 222
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLklelllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 223 aamLGEDITD---DDNLELEMN----SESENGAyldNPPKGALKKLIHAA------KLNASLKTLEGERNQIYIQLSEVD 289
Cdd:TIGR04523 261 ---EQNKIKKqlsEKQKELEQNnkkiKELEKQL---NQLKSEISDLNNQKeqdwnkELKSELKNQEKKLEEIQNQISQNN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 290 KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVmteLYQENEMKLHRKLTVEE-----NYRLEKEEKLSK-VD 363
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK---LKKENQSYKQEIKNLESqindlESKIQNQEKLNQqKD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 364 EKISHATEELETYRKRAKDLEEE---LERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKF 440
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
....*.
gi 1227954611 441 ELLEKD 446
Cdd:TIGR04523 492 KSKEKE 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-388 |
5.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 106 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 172
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 173 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 249
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 250 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 326
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954611 327 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 388
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
57-446 |
8.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 57 IEEKSKLLEKfsLVQKEATCEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSLEDESKSLKSQVAEAK 136
Cdd:PRK03918 278 LEEKVKELKE--LKEKAEEYIKLSEFYEEYLDEL--------------REIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 137 MTFKIFQMNEERLKIaikdaLNENSQLQESQKQLLQEAEVWKEQVSELN--------------KQKVTFEDSKVHAEQV- 201
Cdd:PRK03918 342 ELKKKLKELEKRLEE-----LEERHELYEEAKAKKEELERLKKRLTGLTpeklekeleelekaKEEIEEEISKITARIGe 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 202 LNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELeMNSESENGAYLDNPPKGALKKLihaAKLNASLKTLEGERNQI 281
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 282 --YIQLSEVDKTKEELTEHIKNLQTEQasLQSENTHFENENQKLQqKLK-----VMTELYQENEMKlhRKLTVEENYRLE 354
Cdd:PRK03918 493 seLIKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLI-KLKgeiksLKKELEKLEELK--KKLAELEKKLDE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 355 KEEKLSKVDEKIshateeletyRKRAKDLEEELERTIHSYqgqiisheKKAHDNWLAARNAERNLNDLRKENAHNRQKLT 434
Cdd:PRK03918 568 LEEELAELLKEL----------EELGFESVEELEERLKEL--------EPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
410
....*....|..
gi 1227954611 435 ETELKFELLEKD 446
Cdd:PRK03918 630 KAFEELAETEKR 641
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
265-389 |
8.67e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 344
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1227954611 345 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 389
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
153-338 |
1.37e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 153 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 232
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 233 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 312
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 1227954611 313 NTHFENENQKLQQKLKVMTELYQENE 338
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-391 |
2.94e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 147 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 225
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 226 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 303
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 304 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 383
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1227954611 384 EEELERTI 391
Cdd:COG4942 226 EALIARLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-404 |
5.29e-06 |
|
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: 48.38 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 258 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 333
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227954611 334 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 404
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-389 |
6.15e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 53 LSGLIEEKSKLLEKfsLVQKEAT----CEKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSL 128
Cdd:TIGR02169 714 ASRKIGEIEKEIEQ--LEQEEEKlkerLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 129 KSQVAEakmtfkifqmneerlkiaIKDALNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK--- 205
Cdd:TIGR02169 778 EEALND------------------LEARLSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtle 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 206 ----ESHIKTLTERLLKMKDWAAMLGEDItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQ 280
Cdd:TIGR02169 828 keylEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 281 IYIQLSEVDKTKEELT-------EHIKNLQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRL 353
Cdd:TIGR02169 894 LEAQLRELERKIEELEaqiekkrKRLSELKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQ 961
|
330 340 350
....*....|....*....|....*....|....*.
gi 1227954611 354 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 389
Cdd:TIGR02169 962 RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
116-446 |
7.83e-06 |
|
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: 49.58 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 116 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 194
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 195 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 274
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 275 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 347
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 348 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 417
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 1227954611 418 NLNDLRKENAHNRQKLTETELKFELLEKD 446
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-445 |
8.09e-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: 49.25 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 116 KRIQSLEDESKSLKSQVAEAKMTF-----KIFQMNEERLKIAI-----KDALNEN-SQLQESQKQLLQ------------ 172
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLkknkdKINKLNSDLSKINSeikndKEQKNKLeVELNKLEKQKKEnkknidkfltei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 173 -----EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN-SESEN 246
Cdd:TIGR04523 148 kkkekELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 247 gayldnppkgalkklihaAKLNASLKTLEGERNQIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENT---HFENE 319
Cdd:TIGR04523 228 ------------------NQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 320 NQKLQQKLKVMTELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQ 395
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQ 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1227954611 396 GQIISHEKKAHDNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 445
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-467 |
9.91e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 105 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 184
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 185 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 264
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 344
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 345 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 424
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1227954611 425 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 467
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
178-389 |
2.06e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 178 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 244
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 245 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 311
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954611 312 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 389
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-310 |
3.43e-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: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 104 HSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 176
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 177 WKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayldNPPKG 256
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE-----ELSLE 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1227954611 257 ALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 310
Cdd:TIGR02169 955 DVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
109-445 |
4.89e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 109 ELMADISKRIQSLEDEskslKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEaevwkeqVSELnkQK 188
Cdd:pfam01576 268 ELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQE-------VTEL--KK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 189 VTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GEDITDDDNLELEMNSESENGAYLDNPPKGalkklih 263
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAKQALESENAELQAELRTLQQAKQDSEHKR------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 264 aaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqenEMKLHr 343
Cdd:pfam01576 408 --------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL-------ESQLQ- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 344 klTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE---ELERTIHSYQGQIISHEKKAHDNWLAARNAERNLN 420
Cdd:pfam01576 472 --DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
330 340
....*....|....*....|....*
gi 1227954611 421 DLRKENAHNRQKLTETELKFELLEK 445
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
271-445 |
5.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 271 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEEN 350
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 351 YR--LEKEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAH 428
Cdd:COG4717 148 LEelEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1227954611 429 NRQKLTETELKFELLEK 445
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
108-408 |
6.14e-05 |
|
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: 46.97 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 108 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 174
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 175 EVWKEQVSELNKQKVTFEDSKVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 243
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 244 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 302
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 303 QTEQASLQSENTH-FE--NENQKLQQKLKVMTELYQENeMKLHRKLTveeNYRlekeEKLSKvdEKISHatEELETYRKR 379
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEEF-IELYNIIA---GCL----ETVSK--EPITY--DEIKNTRIN 1792
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1227954611 380 AKD--LEE-ELERTIHSYQ--------GQIISHEKKAHDN 408
Cdd:TIGR01612 1793 AQNefLKIiEIEKKSKSYLddieakefDRIINHFKKKLDH 1832
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
104-439 |
7.28e-05 |
|
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: 46.58 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 104 HSEQDELMADISKRIQSLEDESKSLKS-QVAEAKMTFKIFQMNEERLKIAIKdalnenSQLQESQKQLLQEAEVWKEQVS 182
Cdd:TIGR01612 488 NSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLIH 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 183 ELNKQKVTFEDSKVHAEQVLNDkeshiktLTERLLKMKDwaamlgeDITDDDNLELEMNSESENGAYLDNPPKGA--LKK 260
Cdd:TIGR01612 562 EIKKELEEENEDSIHLEKEIKD-------LFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLKK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 261 LIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTEQASLQSENTH-FENENQKLQQKLkvmTELYQENE 338
Cdd:TIGR01612 628 II--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKENA 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 339 MKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAHD 407
Cdd:TIGR01612 689 ID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILED 759
|
330 340 350
....*....|....*....|....*....|...
gi 1227954611 408 NWLAARNAERNLNDLRKENAH-NRQKLTETELK 439
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
85-397 |
8.88e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 85 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 158
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 159 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 237
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 238 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 317
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 318 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 397
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
36-403 |
2.14e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 36 SVRSRLY-VGREKKLALM--------LSGLIEEKSKLLEKFSLVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKhse 106
Cdd:pfam02463 162 AAGSRLKrKKKEALKKLIeetenlaeLIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 107 qdelmADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNK 186
Cdd:pfam02463 239 -----IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 187 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYldnppkgaLKKLIHAAK 266
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL--------AKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 267 LNASLKTLEGERNQIYIQLSEVDKTKEELT---EHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENEMKLHR 343
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARqleDLLKEEKKEELEILEEEEESIELKQGKLTEEK--EELEKQELKLLKD 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 344 KLTVEENYRLEKEEKLSKvdEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEK 403
Cdd:pfam02463 464 ELELKKSEDLLKETQLVK--LQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-360 |
3.01e-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: 44.28 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 35 RSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFS-----LVQKEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDE 109
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELEeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 110 LMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQKQLLQEAEVWKEQVSELNKQKV 189
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 190 TFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESENGAYLDNPPKGALKKLIHA-AKL 267
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEIEELLKKLEEAELKELQAElEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 268 NASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMK------L 341
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvL 525
|
330
....*....|....*....
gi 1227954611 342 HRKLTVEENYRLEKEEKLS 360
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALG 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
265-390 |
3.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 342
Cdd:COG4717 105 EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1227954611 343 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 390
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
71-436 |
3.60e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 71 QKEATCEKLNRSNSELEDEilclEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLK 150
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDIL----QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 151 IAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLG 227
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 228 EDItddDNLELEMNSESENGAYLDNPPKGALKKL-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHI 299
Cdd:TIGR00618 542 TSE---EDVYHQLTSERKQRASLKEQMQEIQQSFsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 300 KNLQtEQASLQSENTHFENENQKLQQKL----KVMTELYQENE------MKLHRKLTVEENYRLEKE-----EKLSKVDE 364
Cdd:TIGR00618 619 RKLQ-PEQDLQDVRLHLQQCSQELALKLtalhALQLTLTQERVrehalsIRVLPKELLASRQLALQKmqsekEQLTYWKE 697
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227954611 365 KISHATE---ELETYRKRAKDLEEELERTIHSyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 436
Cdd:TIGR00618 698 MLAQCQTllrELETHIEEYDREFNEIENASSS-LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
108-220 |
3.83e-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: 43.08 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 108 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 187
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 1227954611 188 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 220
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
265-453 |
4.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY---------- 334
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 335 -----------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 400
Cdd:COG4942 117 grqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1227954611 401 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 453
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
30-422 |
4.42e-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: 43.89 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 30 LWRSFRSVRSRLYVGREKKLALMLSGLIEE---------------KSKLLEKFSLVQK-EATCEKLNRSNSEledeilcl 93
Cdd:TIGR01612 657 IYSTIKSELSKIYEDDIDALYNELSSIVKEnaidntedkaklddlKSKIDKEYDKIQNmETATVELHLSNIE-------- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 94 ekelkeekSKHSEQDELMADISKRIQSleDESKSLKSQVAEakmtfkiFQMNEERLKIAIKDALNENSQLQESQKQLLQE 173
Cdd:TIGR01612 729 --------NKKNELLDIIVEIKKHIHG--EINKDLNKILED-------FKNKEKELSNKINDYAKEKDELNKYKSKISEI 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 174 AEVWKEQVSELNKQ----KVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 249
Cdd:TIGR01612 792 KNHYNDQINIDNIKdedaKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 250 LDNPPKGAL--------KKLIHAAK--LNASLKTLEGERNQIYiQLSEVD---KTKEELTEHIKNLQTEQASLqsenthf 316
Cdd:TIGR01612 872 LTNKIKAEIsddklndyEKKFNDSKslINEINKSIEEEYQNIN-TLKKVDeyiKICENTKESIEKFHNKQNIL------- 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 317 eneNQKLQQKLKVMTE---LYQENEMKLHRKLTVEENyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIhs 393
Cdd:TIGR01612 944 ---KEILNKNIDTIKEsnlIEKSYKDKFDNTLIDKIN-ELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENML-- 1017
|
410 420
....*....|....*....|....*....
gi 1227954611 394 YQgQIISHEKKAHDNWLAARNAERNLNDL 422
Cdd:TIGR01612 1018 YH-QFDEKEKATNDIEQKIEDANKNIPNI 1045
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
106-338 |
4.43e-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: 43.67 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 106 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 184
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 185 NKQKVTFEDSKVHAEQVLNDKESHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPK 255
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 256 GALKKLIHAAK--LNASLKTLEgERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL 333
Cdd:pfam12128 440 YRLKSRLGELKlrLNQATATPE-LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
....*
gi 1227954611 334 YQENE 338
Cdd:pfam12128 519 QSALD 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
113-444 |
8.40e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 113 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSElnkqkvtfe 192
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 193 dskvhAEQVLNDKESHIKTLTERLlkmkdwaamlgEDITDD-DNLELEMNSESENgayldnppKGALKKLIhaAKLNASL 271
Cdd:PRK02224 382 -----RREEIEELEEEIEELRERF-----------GDAPVDlGNAEDFLEELREE--------RDELRERE--AELEATL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 272 KTLEG--ERNQiyiQLSEVDKTKE-----ELTEHIKNL---QTEQASLQSENTHFENENQKLQQKLKVMTELyQENEMKL 341
Cdd:PRK02224 436 RTARErvEEAE---ALLEAGKCPEcgqpvEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 342 HRKLTVEENYRLEKEEKLSKVDEKishaTEELETYRKRAKDLEEELERTIHSYQgqiishekKAHDNWLAARNAERNLND 421
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAA--------EAEEEAEEAREEVAELNS 579
|
330 340
....*....|....*....|...
gi 1227954611 422 LRKENAHNRQKLTETELKFELLE 444
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
46-404 |
8.81e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 46 EKKLALMLSGLIEEKSKLLEKFSLVQKEatcekLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSL---E 122
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQ-----LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsleK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 123 DESKSLKSQVAEAKMTFKIFQ-------MNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtFEDSK 195
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ---LESTK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 196 VHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDitdddnlELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLE 275
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 276 GERNQIYIQLSEVDKTKEELTEHIKNL--------------QTEQASLQSENTHFENENQKLQ----------QKLKVMT 331
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilkdkkdakiRELEARV 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 332 ELYQENEMKL----HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 404
Cdd:pfam15921 628 SDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
111-389 |
9.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 111 MADISKRIQSLEDESKSLKSQVAEAKMTFKifqmNEERLkIAIKDALNENSQLQESQKQL--------LQEAEVWKEQVS 182
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK----KESEL-IKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 183 ELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEmNSESENGAYLDnpPKGALK 259
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLE--LKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 260 KLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----EQASLQSENTHFENENQKLQQKLKVMTELY 334
Cdd:PRK03918 613 EL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954611 335 QENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 389
Cdd:PRK03918 690 EEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
57-414 |
1.14e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 57 IEEKSKLLEKfslvQKEATCEKLNRSNSELEDeilclekELKEEKSKHSEQDELMADI---SKRIQSLEDESKSLKSQVA 133
Cdd:pfam05483 273 LEEKTKLQDE----NLKELIEKKDHLTKELED-------IKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 134 EAKMTFKI----------------------FQMNEERLKIAIKDALNENSQLQESQKqLLQEAEVWKEQVSEL--NKQKV 189
Cdd:pfam05483 342 KAKAAHSFvvtefeattcsleellrteqqrLEKNEDQLKIITMELQKKSSELEEMTK-FKNNKEVELEELKKIlaEDEKL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 190 TFEDSKVH--AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMnseSENGAYLDNPPKGALKKLIHAAKL 267
Cdd:pfam05483 421 LDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV---EDLKTELEKEKLKNIELTAHCDKL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 268 NASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMK 340
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKhqediinCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 341 LHRKLTVEE-----------NYRLEKEEKLSKVDE----------KISHATEELETYRKRAKDLEEELERTIHSYQGQII 399
Cdd:pfam05483 578 IEYEVLKKEkqmkilenkcnNLKKQIENKNKNIEElhqenkalkkKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID 657
|
410
....*....|....*
gi 1227954611 400 SHEKKAHDNWLAARN 414
Cdd:pfam05483 658 NYQKEIEDKKISEEK 672
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-395 |
1.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 271 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 344
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954611 345 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 395
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-417 |
1.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL-KVMTELYQE------- 336
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSggsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 337 -------------NEMKLHRKLTVEENYRLEK----EEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQI- 398
Cdd:COG3883 106 dvllgsesfsdflDRLSALSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLa 185
|
170 180
....*....|....*....|
gi 1227954611 399 -ISHEKKAHDNWLAARNAER 417
Cdd:COG3883 186 qLSAEEAAAEAQLAELEAEL 205
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-336 |
1.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 111 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNeerlkiaikdalNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 190
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 191 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 264
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954611 265 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 336
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
82-431 |
1.35e-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: 42.13 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 82 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIF--QMNEERLKI------AI 153
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKnkalaeRK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 154 KDALNENSQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 232
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 233 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 303
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 304 TEQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 381
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1227954611 382 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 431
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
263-446 |
1.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 263 HAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL-KVMTELYQENE--M 339
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELeQARSELEQLEEelE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 340 KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERtihsyqgqiISHEKKAHDNWLAARNAErnL 419
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---------LEAQIAELQSEIAEREEE--L 152
|
170 180
....*....|....*....|....*..
gi 1227954611 420 NDLRKENAHNRQKLTETELKFELLEKD 446
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEA 179
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
277-344 |
1.49e-03 |
|
Regulator of replication initiation timing YabA [Replication, recombination and repair];
Pssm-ID: 443564 [Multi-domain] Cd Length: 107 Bit Score: 38.70 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954611 277 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 344
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
202-407 |
1.62e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 202 LNDKESHIKTL----TERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLdNPPKGALKKLIHAAKLN-----ASLK 272
Cdd:pfam05483 235 INDKEKQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSlqrsmSTQK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 273 TLEgERNQIYI------------QLSEVDKTKEELTEHIKNLQTEQASLQ----SENTHFENENQKLqqKLKVMTELYQE 336
Cdd:pfam05483 314 ALE-EDLQIATkticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEellrTEQQRLEKNEDQL--KIITMELQKKS 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227954611 337 NEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETyrkrakdLEEELERTIHSYQGQIISHEKKAHD 407
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEK-------IAEELKGKEQELIFLLQAREKEIHD 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
253-404 |
1.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 253 PPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFE--NENQKLQQKLKVM 330
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 331 TELYQENEMKLHRKLTVEENYR---------------------LEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 389
Cdd:COG4717 145 PERLEELEERLEELRELEEELEeleaelaelqeeleelleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*...
gi 1227954611 390 T---IHSYQGQIISHEKK 404
Cdd:COG4717 225 LeeeLEQLENELEAAALE 242
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
108-435 |
1.99e-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: 41.38 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 108 DELMADISKRIQSLEDESKSLKSQvaeakmtfkifqmnEERLKIAIKDALNEnsqLQESQKQLLQEAEVWKEQVSELNKQ 187
Cdd:pfam06160 92 EELLDDIEEDIKQILEELDELLES--------------EEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 188 KVTFEDSKVHAEQvLNDKESHIKtlterllkmkdwAAMLGEDITDD-DNLELEMNsesengayldnppkgALKKLIHAAK 266
Cdd:pfam06160 155 LAEIEEEFSQFEE-LTESGDYLE------------AREVLEKLEEEtDALEELME---------------DIPPLYEELK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 267 ---------LNASLKTLEG-----ERNQIYIQLSEVDKTKEELTEHIKNLQTEQAslqsenthfENENQKLQQKLKVMTE 332
Cdd:pfam06160 207 telpdqleeLKEGYREMEEegyalEHLNVDKEIQQLEEQLEENLALLENLELDEA---------EEALEEIEERIDQLYD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 333 LyqenemklhrkLTVEENYRLEKEEKLSKVDEKISHATEELetyrkraKDLEEELERTIHSYqgqIISHekkahdNWLA- 411
Cdd:pfam06160 278 L-----------LEKEVDAKKYVEKNLPEIEDYLEHAEEQN-------KELKEELERVQQSY---TLNE------NELEr 330
|
330 340
....*....|....*....|....
gi 1227954611 412 ARNAERNLNDLRKENAHNRQKLTE 435
Cdd:pfam06160 331 VRGLEKQLEELEKRYDEIVERLEE 354
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
143-390 |
2.04e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 143 QMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKvtfEDSKVHAEQVLNDKESHIKTLTERLLKMKDW 222
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQV---KELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 223 AAMLGEDITDDDNLELEMNSESENGayldnPPKGALKKLIhaAKL-----NASLkTLEGERnQIYIQLSEVD------KT 291
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAG-----GSIDKLRKEI--ERLewrqqTEVL-SPEEEK-ELVEKIKELEkelekaKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 292 KEELTEHIKNLQTEQASLQSE-NTHFENEN---QKLQQKLKVMTELYQE-NEMK-----LHRKLtveenyrLEKEEKLSK 361
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEaEEIHKKIKelaEEAQELHEEMIELYKEaDELRkeadeLHKEI-------VEAQEKADE 227
|
250 260
....*....|....*....|....*....
gi 1227954611 362 VDEKISHATEELETYRKRAKDLEEELERT 390
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
108-425 |
3.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 108 DELMADIsKRIQSLEDESKSLKSQVAEAK--MTFKIFQMNEERLKiAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 185
Cdd:COG4717 149 EELEERL-EELRELEEELEELEAELAELQeeLEELLEQLSLATEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 186 KQKVTFEDSKVHA--EQVLNDKESHIKTLTERLLkmkdWAAMLGEDITDDDNL---------------ELEMNSESENGA 248
Cdd:COG4717 227 EELEQLENELEAAalEERLKEARLLLLIAAALLA----LLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 249 YLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSEntHFENENQKLQQKLK 328
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 329 VMTE--------LYQENEMKLHRKLTVEENYRLEK---------------EEKLSKVDEKISHATEELETYRKRAKDLEE 385
Cdd:COG4717 381 VEDEeelraaleQAEEYQELKEELEELEEQLEELLgeleellealdeeelEEELEELEEELEELEEELEELREELAELEA 460
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1227954611 386 ELERTIHSYQGQIISHEKKAHDN--------WLAARNAERNLNDLRKE 425
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAelrelaeeWAALKLALELLEEAREE 508
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
146-468 |
3.87e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 146 EERLKIAIKDALNENSQ--LQESQKQLLQEaevwKEQVSELNKQKVTF-EDSKVHAEQVLNDKESHIKTLTERLLKMKDW 222
Cdd:COG5022 858 KKRFSLLKKETIYLQSAqrVELAERQLQEL----KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 223 AAMLgEDITDDDNLELEMNSESENGAYLDnppkgalkklihaakLNASLKTLEGERNQIYIQL-----------SEVDKT 291
Cdd:COG5022 934 KKLL-NNIDLEEGPSIEYVKLPELNKLHE---------------VESKLKETSEEYEDLLKKStilvregnkanSELKNF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 292 KEELTEHIKNLQTEQASLQS--ENTHFENENQKLQQKLKVM-TELYQENEM-KLHRKLTVEENYrLEKEEKLSKVDEKIS 367
Cdd:COG5022 998 KKELAELSKQYGALQESTKQlkELPVEVAELQSASKIISSEsTELSILKPLqKLKGLLLLENNQ-LQARYKALKLRRENS 1076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 368 HATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNwlaARNAERNLNDLRKENAHNRQKLTETELKFELLEKDP 447
Cdd:COG5022 1077 LLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQF---IVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQ 1153
|
330 340
....*....|....*....|.
gi 1227954611 448 YALDVPNTAFGREHSPYGPSP 468
Cdd:COG5022 1154 LELDGLFWEANLEALPSPPPF 1174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-437 |
4.02e-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: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 354 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 433
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 1227954611 434 TETE 437
Cdd:COG4942 100 EAQK 103
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
256-422 |
4.37e-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: 40.05 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 256 GALKKLIHAAKLNASLKTLEGERNQIYIQLsevdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLkvmtelyQ 335
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKALL-------DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-------E 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 336 ENEMKLHRKLTvEENYRLEKEEkLSKVDEKIshaTEELETYRKRAKDLEEELERTIHSYQGQiISHEKKAHDNWLAARNA 415
Cdd:cd22656 160 TLEKALKDLLT-DEGGAIARKE-IKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAK-LAAALRLIADLTAADTD 233
|
....*..
gi 1227954611 416 ERNLNDL 422
Cdd:cd22656 234 LDNLLAL 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
266-451 |
4.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 266 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtELYQENEmklhrKL 345
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE---ELQKERQ-----DL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 346 TVEENyrlEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 425
Cdd:COG4372 128 EQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180
....*....|....*....|....*.
gi 1227954611 426 NAHNRQKLTETELKFELLEKDPYALD 451
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
116-326 |
5.04e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 116 KRIQSLEDESKSLKSQVaEAKMtfKIFQMNEERLKIaikdalnensQLQESQKQLLQEaevwKEQVSELNKQKVTFEDSK 195
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-EAKM--KEVMAKQEGMEG----------KLQVTQKNLEHS----KGKVAQLEEKLVSTEKEK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 196 V----HAEQVLNDKEsHIKTLTERLLKMKDWAAMLGEDI-TDDDNLELEMNSESENgayldnppKGALKKLIHaaKLNAS 270
Cdd:pfam15905 215 IeeksETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLkEKNDEIESLKQSLEEK--------EQELSKQIK--DLNEK 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954611 271 LKTLEGERNQIyiqLSEvDKTKEEltehikNLQTEQASLQSENTHFENENQKLQQK 326
Cdd:pfam15905 284 CKLLESEKEEL---LRE-YEEKEQ------TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
154-390 |
5.22e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 154 KDALNENSQLQESQKQLLQEAEVWKEQVSELN---KQKVTFEDSKVHAEqVLNDKESHIKTLTERLLKMKDWAAMLGEDI 230
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAISKAESATAVAKEAKddaIQAVKAHTDSLKEA-SDTAEISREKATDSALQKAEALAEKLKEVI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 231 TdddnleLEMNSESENGAYLDNPPKGALKKLIHA--------------AKLNASLKTLEGERNQIYIQlsEVDKTKEELT 296
Cdd:pfam09731 200 N------LAKQSEEEAAPPLLDAAPETPPKLPEHldnveekvekaqslAKLVDQYKELVASERIVFQQ--ELVSIFPDII 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 297 EHIKNLQ-TEQASLQSENTHFENENQKLQQKL---KVMTELYQENEMK----LHRKLTVEENYRLE--KEEKLSKVDEKI 366
Cdd:pfam09731 272 PVLKEDNlLSNDDLNSLIAHAHREIDQLSKKLaelKKREEKHIERALEkqkeELDKLAEELSARLEevRAADEAQLRLEF 351
|
250 260
....*....|....*....|....*
gi 1227954611 367 SHATEEL-ETYRKRakdLEEELERT 390
Cdd:pfam09731 352 EREREEIrESYEEK---LRTELERQ 373
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
211-389 |
5.80e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.04 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 211 TLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIhaaKLNASLKTLEGERnQIYIQLSEVDK 290
Cdd:pfam05911 640 TLSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFE---QLKSEKENLEVEL-ASCTENLESTK 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 291 TK-EELTEHIKNLQTEQASLQsenthfeNENQKLQQKLKVMTELYQENEMKLhRKLTVEENYRLEKEEKLSKVDEKISHA 369
Cdd:pfam05911 716 SQlQESEQLIAELRSELASLK-------ESNSLAETQLKCMAESYEDLETRL-TELEAELNELRQKFEALEVELEEEKNC 787
|
170 180
....*....|....*....|
gi 1227954611 370 TEELETyrkRAKDLEEELER 389
Cdd:pfam05911 788 HEELEA---KCLELQEQLER 804
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
265-437 |
6.78e-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: 39.95 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 265 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--------E 336
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQlrarieelR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 337 NEMKLHRKLTVEENYRLEKE------EKLSKVDEKISHATEEL-ETYRKRAKDLEeelERTIHSYQGQIISHEKKAHDNW 409
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELqSKMRSRAKLLM---KRAAHVKQQSSIEEQRRLLQTL 350
|
170 180
....*....|....*....|....*....
gi 1227954611 410 LAARNAERNLNDLRKE-NAHNRQKLTETE 437
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSiREISCQQHTLTQ 379
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
260-436 |
7.42e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.97 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 260 KLIHAAKLNASLKTLEGErNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENenqklQQKLKVMTelYQENEM 339
Cdd:pfam09787 25 KLIASLKEGSGVEGLDSS-TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA-----QQQEEAES--SREQLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 340 KLHRKLTVEENYRLEKEEKLSKVDEKISHateeletyrkrakdLEEELERTIHSYQGQIISHEKKAHDnwLAARNAERNL 419
Cdd:pfam09787 97 ELEEQLATERSARREAEAELERLQEELRY--------------LEEELRRSKATLQSRIKDREAEIEK--LRNQLTSKSQ 160
|
170
....*....|....*...
gi 1227954611 420 NDLRKENAHNRQK-LTET 436
Cdd:pfam09787 161 SSSSQSELENRLHqLTET 178
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
58-445 |
7.47e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 58 EEKSKLLEKFSLVQKEATCEKLNRSNSELEDEILclekelkEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKM 137
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKA-------DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 138 TFKIFQMNEERLKIAIKDALNEnSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLL 217
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 218 KmkdwaAMLGEDITDD-DNLELEMNSESENGAYLDNppkgalkklihAAKLNASLKTLEGERNQIYIQLSEVD-KTKEEL 295
Cdd:TIGR00606 630 D-----VCGSQDEESDlERLKEEIEKSSKQRAMLAG-----------ATAVYSQFITQLTDENQSCCPVCQRVfQTEAEL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 296 TEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY--QENEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEE 372
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETL 773
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954611 373 LETY---RKRAKDLEEELErTIHSYQGQIISHEKKAHD--NWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 445
Cdd:TIGR00606 774 LGTImpeEESAKVCLTDVT-IMERFQMELKDVERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
277-389 |
7.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 277 ERNQIYIQLSEVDKTKEE-LTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR--KLTVEEnyrl 353
Cdd:PRK12704 79 ERRNELQKLEKRLLQKEEnLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEE---- 154
|
90 100 110
....*....|....*....|....*....|....*.
gi 1227954611 354 EKEEKLSKVDEKISHatEELETYRKRAKDLEEELER 389
Cdd:PRK12704 155 AKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADK 188
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
106-439 |
7.76e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 106 EQDELMADISKRIQSLEDESKSlkSQVAEAKMtfkifqmnEERL--KIAIKDALNEnsQLQESQKQLLQEAEVWKEQVSE 183
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSSN--TDTALTTL--------EEALseKERIIERLKE--QREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 184 LNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKmkdwaamlgediTDDDNLELEMNSEsengayldnppkgalKKLIH 263
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLK------------KDSKLKSLEIAVE---------------QKKEE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 264 AAKLNASLKTLEgernqiyiQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqenemklhr 343
Cdd:pfam10174 533 CSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV------------- 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 344 kltveENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNwLAARNAERNLNDLR 423
Cdd:pfam10174 592 -----ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK----GAQLLEEARRREDN-LADNSQQLQLEELM 661
|
330
....*....|....*.
gi 1227954611 424 KENAHNRQKLTETELK 439
Cdd:pfam10174 662 GALEKTRQELDATKAR 677
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
53-232 |
8.66e-03 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 38.92 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 53 LSGLIEEKskllekfsLVQKEATCEKLNRSNSELEDEIlclekelkeekskhseqDELMADISKRIQSLEDESKS-LKSQ 131
Cdd:PRK00059 90 LDSLITEK--------VLLQKAKELKLIPSEEELNKEV-----------------DKKINEIKKQFNNDEEQFEEaLKAT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954611 132 vaeakmtfkifQMNEERLKIAIKDalneNSQLQESQKQLLQEAEVWKEQVS---ELNKQKVTFEDSKVHAEQVLNDKESH 208
Cdd:PRK00059 145 -----------GFTEETFKEYLKN----QIIIEKVINEVVKDVKVTDKDAQkyyNENKSKFTEKPNTMHLAHILVKTEDE 209
|
170 180
....*....|....*....|....
gi 1227954611 209 IKTLTERLLKMKDWAAMLGEDITD 232
Cdd:PRK00059 210 AKKVKKRLDKGEDFAKVAKEVSQD 233
|
|
| |
