|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-415 |
1.41e-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: 71.63 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 78 EVESSLKDASFEKEATEAQ--SLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLK 155
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 156 SQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHI 235
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 236 KTLTERLLKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVD 315
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 316 KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklsk 387
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE---- 955
|
330 340
....*....|....*....|....*...
gi 1227954615 388 VDEKISHATEELETYRKRAKDLEEELER 415
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-338 |
3.01e-12 |
|
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: 70.48 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 45 REKKLALMLSGLIEEKSKL------LEKFSLVQK---EYEGYEVESSLKDASFEKEATEAQ--SLEATCEKLNRSNSELE 113
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrrerekAERYQALLKekrEYEGYELLKEKEALERQKEAIERQlaSLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 114 DEIlclekelkeekskhSEQDELMADISKRIQSL-EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQES 192
Cdd:TIGR02169 265 KRL--------------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 193 QKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHI-------KTLTERLLKMKDWAAMLGEDI----TDDDN 261
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKDYREKLEKLKREInelkRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 262 LELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQS 337
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
.
gi 1227954615 338 E 338
Cdd:TIGR02169 491 E 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-424 |
1.08e-10 |
|
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: 65.04 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 96 QSLEATCEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERL 175
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQREL--------------EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 176 KIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGED 255
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 256 ITDDDNLELEMNSESENgayLDNPPKgALKKLIhaAKLNASLKTLEGERNQIYIQLSEV---------DKTKEELTEHIK 326
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKE---LEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEID 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 327 NLQTEQASLQSENTHFENENQKLQQKLKVmtelYQENEMKLHRKLTveenyrlEKEEKLSKVDEKISHATEE---LETYR 403
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQ----KEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEnekLSSII 633
|
330 340
....*....|....*....|.
gi 1227954615 404 KRAKDLEEELERTIHSYQGQI 424
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETI 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
57-417 |
5.62e-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: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 57 IEEKSKLLEKfslVQKEYEGYEVESslkdasfEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDEL 136
Cdd:TIGR04523 365 LEEKQNEIEK---LKKENQSYKQEI-------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 137 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKdalNENSQLQESQKQLLQ----------EAEVWKEQ 206
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSkekelkklneEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 207 VSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKD---WAAMLGEDITDDDNLE-LEMNSES------------ 270
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEeLKQTQKSlkkkqeekqeli 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 271 -ENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKL 349
Cdd:TIGR04523 592 dQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 350 QQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTI 417
Cdd:TIGR04523 672 KTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
78-475 |
1.14e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 78 EVESSLKDASFekeateaqSLEATCEKLNR--SNSELEDEILclekeLKEEKSKHSEQDELmADISKRIQSLEDESKSLK 155
Cdd:pfam05483 251 EKENKMKDLTF--------LLEESRDKANQleEKTKLQDENL-----KELIEKKDHLTKEL-EDIKMSLQRSMSTQKALE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 156 SQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEAEVwkeqVSELNKQKVTFEDSKVHAEQVLNDKESHI 235
Cdd:pfam05483 317 EDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHSFV----VTEFEATTCSLEELLRTEQQRLEKNEDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 236 KTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYLDNppKGALKKLIHAAK-----LNASLKTLEGERNQ 306
Cdd:pfam05483 380 KIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLLDE--KKQFEKIAEELKgkeqeLIFLLQAREKEIHD 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 307 IYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTElyQENEMKLHRKLTVEENYRLEKEE--- 383
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ--EASDMTLELKKHQEDIINCKKQEerm 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 384 --KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTE 461
Cdd:pfam05483 533 lkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
410
....*....|....
gi 1227954615 462 TELKFELLEKDPYA 475
Cdd:pfam05483 613 LHQENKALKKKGSA 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-472 |
2.72e-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: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 290 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 369
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 370 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 446
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 1227954615 447 DLRKENAHNRQKLTETELKFELLEKD 472
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-472 |
2.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 56 LIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelkeekskhSEQDE 135
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK--------------RKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 136 LMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEE--RLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKq 213
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELK---ELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 214 kvtfedskvhaeqvlndKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAA-- 291
Cdd:PRK03918 336 -----------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELek 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 292 ----------KLNASLKTLEGERNQIYIQLSEVDKTK-------EELTEH-----IKNLQTEQASLQSENTHFENENQKL 349
Cdd:PRK03918 399 akeeieeeisKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 350 QQKLKVMtELYQENEMKLHRKLTVEENYRlEKEEKLSKVD-EKISHATEELETYRKRA-------KDLEEELERtIHSYQ 421
Cdd:PRK03918 479 RKELREL-EKVLKKESELIKLKELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLKEKLiklkgeiKSLKKELEK-LEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 422 GQIISHEKK-----------------------------------AHDNWLAARNAERNLNDLRKENAHNRQKLTETELKF 466
Cdd:PRK03918 556 KKLAELEKKldeleeelaellkeleelgfesveeleerlkelepFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
....*.
gi 1227954615 467 ELLEKD 472
Cdd:PRK03918 636 AETEKR 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-415 |
3.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 32 RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDAS-----FEKEATEAQSLEAT----C 102
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD--ELSQELSDASrkigeIEKEIEQLEQEEEKlkerL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 103 EKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerlkiaIKDA 182
Cdd:TIGR02169 740 EELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALND------------------LEAR 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 183 LNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK-------ESHIKTLTERLLKMKDWAAMLGED 255
Cdd:TIGR02169 788 LSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 256 ItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQIYIQLSEVDKTKEELT-------EHIKN 327
Cdd:TIGR02169 856 I-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 328 LQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRLEKEEKLSKVDEKISHATEELETYRKRAK 407
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
....*...
gi 1227954615 408 DLEEELER 415
Cdd:TIGR02169 990 ELKEKRAK 997
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-451 |
4.96e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 71 QKEYEGYEVESSL-----KDASFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelkeekskhseqdelmADISKRIQ 145
Cdd:COG1196 219 KEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAELAELEAEL---------------------EELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 146 SLEDESKSLKSQVAEAKMTfkifqmnEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAE 225
Cdd:COG1196 278 ELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 226 QVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAAKLNASLKTLEGERN 305
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 306 QIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkltveenyRLEKEEKL 385
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE--------LLEELAEA 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954615 386 SKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 451
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-476 |
7.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 140 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 212
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 213 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 292
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 293 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 371
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 372 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 451
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 1227954615 452 NAHNRQKLTETELKFELLEKDPYAL 476
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-353 |
8.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 63 LLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISK 142
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------EEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 143 RIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKV 222
Cdd:COG1196 296 ELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 223 HAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESEngayldnppkgalKKLIHAAKLNASLKTLEG 302
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------------RLEEELEELEEALAELEE 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1227954615 303 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL 353
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
80-472 |
8.94e-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: 52.33 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 80 ESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSeqdelmaDISKRIQSLEDESKSLKSQVA 159
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-------DLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 160 EAKMT---------------FKIFQMNEE--RLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKV 222
Cdd:TIGR04523 184 NIQKNidkiknkllklelllSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 223 HAEQVLNDKESH-------IKTLTERLLKMK------------DWAAMLGEDITDDDNLELEMNSE-SENGAYLDNppkg 282
Cdd:TIGR04523 264 KIKKQLSEKQKEleqnnkkIKELEKQLNQLKseisdlnnqkeqDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQ---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 283 aLKKLIhaAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKV 355
Cdd:TIGR04523 340 -LNEQI--SQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 356 MTELYQ--ENEMKLHRKLTVEENYRL--------EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQII 425
Cdd:TIGR04523 417 LQQEKEllEKEIERLKETIIKNNSEIkdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELK 492
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1227954615 426 SHEKKAHDNWLAARNAERNLNDLRKENAhnRQKLTETELKFELLEKD 472
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKIS--SLKEKIEKLESEKKEKE 537
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
291-415 |
1.10e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 370
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1227954615 371 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 415
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-414 |
1.16e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 132 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 198
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 199 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 275
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 276 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 352
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954615 353 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 414
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-336 |
4.83e-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: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 53 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLE-----KELKEEK 127
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 128 SKHSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEA 200
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 201 EVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayldNPP 280
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE-----ELS 952
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954615 281 KGALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 336
Cdd:TIGR02169 953 LEDVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-386 |
5.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 57 IEEKSKLLEKFSLVQKEYEGYEVESSLKDAS--FEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQD 134
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 135 ELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQKQLLQEAEVWKEQVSELNKQK 214
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 215 VTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESENGAYLDNPPKGALKKLIHA-AK 292
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEIEELLKKLEEAELKELQAElEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 293 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMK------ 366
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgv 524
|
330 340
....*....|....*....|
gi 1227954615 367 LHRKLTVEENYRLEKEEKLS 386
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALG 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
173-417 |
8.36e-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: 48.61 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 173 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 251
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 252 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 329
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 330 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 409
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1227954615 410 EEELERTI 417
Cdd:COG4942 226 EALIARLE 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-364 |
8.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 179 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 258
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 259 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 338
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 1227954615 339 NTHFENENQKLQQKLKVMTELYQENE 364
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-430 |
1.19e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 284 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 359
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227954615 360 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 430
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-471 |
1.41e-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: 48.53 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 59 EKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMA 138
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 139 DISKRIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFE 218
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQ-------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 219 D---SKVHAEQVLNDKESHIKTLTERLLKMKDWAAM---------LGEDITDDDNLE-----------------LEMNSE 269
Cdd:TIGR02169 504 ErvrGGRAVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrLNNVVVEDDAVAkeaiellkrrkagratfLPLNKM 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 270 SENGAYLDNP-PKGALKKL--------------------------IHAAK---LNASLKTLEGE---------------R 304
Cdd:TIGR02169 584 RDERRDLSILsEDGVIGFAvdlvefdpkyepafkyvfgdtlvvedIEAARrlmGKYRMVTLEGElfeksgamtggsrapR 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 305 NQIYIQLSEVDKTkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMT----------ELYQENEMKLHRKLTve 374
Cdd:TIGR02169 664 GGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeiEQLEQEEEKLKERLE-- 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 375 enyrlEKEEKLSKVDEKISHATEELETYRKRAkdleEELERTIHSYQGQIISHEKK-AHDNWLAARNAERNLNDLRKEN- 452
Cdd:TIGR02169 741 -----ELEEDLSSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIe 811
|
490 500
....*....|....*....|..
gi 1227954615 453 ---AHNRQKLTETELKFELLEK 471
Cdd:TIGR02169 812 arlREIEQKLNRLTLEKEYLEK 833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-471 |
1.91e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 142 KRIQSLEDESKSLKSQVAEAKMTF-----KIFQMNEERLKIAI-----KDALNEN-SQLQESQKQLLQ------------ 198
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLkknkdKINKLNSDLSKINSeikndKEQKNKLeVELNKLEKQKKEnkknidkfltei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 199 -----EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN-SESEN 272
Cdd:TIGR04523 148 kkkekELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 273 gayldnppkgalkklihaAKLNASLKTLEGERNQIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENT---HFENE 345
Cdd:TIGR04523 228 ------------------NQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 346 NQKLQQKLKVMTELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQ 421
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQ 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1227954615 422 GQIISHEKKAHDNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 471
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
142-472 |
2.38e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 142 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 220
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 221 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 300
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 301 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 373
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 374 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 443
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 1227954615 444 NLNDLRKENAHNRQKLTETELKFELLEKD 472
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
84-472 |
2.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 84 KDASFEKEATEAQSLEATCEKLNRSNSELEDEI--LCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEA 161
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 162 KMTFKIFQMNEERLKIA-----------IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVlnd 230
Cdd:COG4717 166 EELEAELAELQEELEELleqlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 231 keshiktltERLLKMKDWAAMLGEditdddNLELEMNSESENGAYLDNPPKGALKK---LIHAAKLNASLKTLEGERNQI 307
Cdd:COG4717 243 ---------ERLKEARLLLLIAAA------LLALLGLGGSLLSLILTIAGVLFLVLgllALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 308 YIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELyqENEMKLhrkltveENYRLEKEEKLSK 387
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQL-------EELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 388 VDekishaTEELETYRKRAKDLEE--ELERTIHSYQGQIISHEKKAHDNWLAA---------RNAERNLNDLRKENAHNR 456
Cdd:COG4717 379 AG------VEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELR 452
|
410
....*....|....*.
gi 1227954615 457 QKLTETELKFELLEKD 472
Cdd:COG4717 453 EELAELEAELEQLEED 468
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
204-415 |
3.15e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 204 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 270
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 271 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 337
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227954615 338 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 415
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-493 |
3.17e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 131 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 210
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 211 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 290
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 370
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 371 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 450
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1227954615 451 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 493
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-477 |
4.73e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLqsenthfENENQKLQQKLKvmtELYQENEMkLHRK 370
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQILRERLA---NLERQLEE-LEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 371 LTVEENYRLEKEEKLSKVDEKISHATEELETYR---KRAKDLEEELERTIHSYQGQIISHEKKAHD--NWLAARNAERNL 445
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEaelEELEAELEELESRLEELEEQLETLRSKVAQleLQIASLNNEIER 404
|
170 180 190
....*....|....*....|....*....|..
gi 1227954615 446 NDLRKENAHNRQKLTETELKFELLEKDPYALD 477
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
47-471 |
5.11e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 47 KKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSlkdaSFEKEATEAQSLEATCEKLNRSNSELEDEIlclekelKEE 126
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRL-------EEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 127 KSKHSEQDELMAdISKRIQSLEDESKSLKSQVAEAKMTfkifqmNEERLKIAIKDALNEnsqLQESQKQLLQEAEVWKEQ 206
Cdd:PRK03918 358 EERHELYEEAKA-KKEELERLKKRLTGLTPEKLEKELE------ELEKAKEEIEEEISK---ITARIGELKKEIKELKKA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 207 VSELNKQK---------VTFED-----SKVHAEqvLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNL---------- 262
Cdd:PRK03918 428 IEELKKAKgkcpvcgreLTEEHrkellEEYTAE--LKRIEKELKEIEEKERKLRKELRELEKVLKKESELiklkelaeql 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 263 -ELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNqiyiQLSEVDKTKEELTEHIKNLQTEQASL--QSEN 339
Cdd:PRK03918 506 kELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELlkELEE 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 340 THFENEnQKLQQKLKVMTELYQE-NEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETYRKRAKDLE------- 410
Cdd:PRK03918 582 LGFESV-EELEERLKELEPFYNEyLELKDAEKELEREEKELKKlEEELDKAFEELAETEKRLEELRKELEELEkkyseee 660
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954615 411 -EELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKEnahnRQKLTETELKFELLEK 471
Cdd:PRK03918 661 yEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEK 718
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-440 |
5.46e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 45 REKKLALMLSGLIEEKSKLLE-KFSLVQKEYEGYEVEsslkdasfEKEATEAQSLEATCEKLNRSNSELEDeilclekEL 123
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDlTFLLEESRDKANQLE--------EKTKLQDENLKELIEKKDHLTKELED-------IK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 124 KEEKSKHSEQDELMADI---SKRIQSLEDESKSLKSQVAEAKMTFKI----------------------FQMNEERLKIA 178
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELNKAKAAHSFvvtefeattcsleellrteqqrLEKNEDQLKII 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 179 IKDALNENSQLQESQKqLLQEAEVWKEQVSEL--NKQKVTFEDSKVH--AEQVLNDKESHIKTLTERLLKMKDWAAMLGE 254
Cdd:pfam05483 383 TMELQKKSSELEEMTK-FKNNKEVELEELKKIlaEDEKLLDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 255 DITDDDNLELEMnseSENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKN 327
Cdd:pfam05483 462 IKTSEEHYLKEV---EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqediinCKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 328 LQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEE-----------NYRLEKEEKLSKVDE------ 390
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEkqmkilenkcnNLKKQIENKNKNIEElhqenk 618
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1227954615 391 ----KISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARN 440
Cdd:pfam05483 619 alkkKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
46-471 |
5.53e-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: 46.71 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 46 EKKLALMLSGLI--EEKSKLLEKFSLVQkEYEGYEVESSLKdasfeKEATEAQSLEATCEKLNRSNSELEDEILCLEKEL 123
Cdd:pfam01576 158 EERISEFTSNLAeeEEKAKSLSKLKNKH-EAMISDLEERLK-----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 124 KEEKSKHSEQDELMADISKRiqsLEDES----------KSLKSQVAEAKMTFKIFQMNE--------------ERLKIAI 179
Cdd:pfam01576 232 AELRAQLAKKEEELQAALAR---LEEETaqknnalkkiRELEAQISELQEDLESERAARnkaekqrrdlgeelEALKTEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 180 KDALNENSQLQESQKQLLQEaevwkeqVSELnkQKVTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GE 254
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQE-------VTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 255 DITDDDNLELEMNSESENGAYLDNPPKGalkklihaaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQAS 334
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 335 LQSENTHFENENQKLQQKLKVMtelyqenEMKLHrklTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE--- 411
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSL-------ESQLQ---DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakr 513
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 412 ELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 471
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
134-434 |
6.28e-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: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 134 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 200
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 201 EVWKEQVSELNKQKVTFEDSKVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 269
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 270 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 328
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 329 QTEQASLQSENTH-FE--NENQKLQQKLKVMTELYQENeMKLHRKLTveeNYRlekeEKLSKvdEKISHatEELETYRKR 405
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEEF-IELYNIIA---GCL----ETVSK--EPITY--DEIKNTRIN 1792
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1227954615 406 AKD--LEE-ELERTIHSYQ--------GQIISHEKKAHDN 434
Cdd:TIGR01612 1793 AQNefLKIiEIEKKSKSYLddieakefDRIINHFKKKLDH 1832
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
130-465 |
7.69e-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: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 130 HSEQDELMADISKRIQSLEDESKSLKS-QVAEAKMTFKIFQMNEERLKIAIKdalnenSQLQESQKQLLQEAEVWKEQVS 208
Cdd:TIGR01612 488 NSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLIH 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 209 ELNKQKVTFEDSKVHAEQVLNDkeshiktLTERLLKMKDwaamlgeDITDDDNLELEMNSESENGAYLDNPPKGA--LKK 286
Cdd:TIGR01612 562 EIKKELEEENEDSIHLEKEIKD-------LFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLKK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 287 LIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTEQASLQSENTH-FENENQKLQQKLkvmTELYQENE 364
Cdd:TIGR01612 628 II--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKENA 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 365 MKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAHD 433
Cdd:TIGR01612 689 ID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILED 759
|
330 340 350
....*....|....*....|....*....|...
gi 1227954615 434 NWLAARNAERNLNDLRKENAH-NRQKLTETELK 465
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
297-471 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 297 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEEN 376
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 377 YR--LEKEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAH 454
Cdd:COG4717 148 LEelEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1227954615 455 NRQKLTETELKFELLEK 471
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
30-448 |
1.08e-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: 45.81 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 30 LWRSFRSVRSRLYVGREKKLALMLSGLIEEKskllekfslvqkEYEGYEVESSLKD--ASFEKEATEAQSLEATCEKLNR 107
Cdd:TIGR01612 657 IYSTIKSELSKIYEDDIDALYNELSSIVKEN------------AIDNTEDKAKLDDlkSKIDKEYDKIQNMETATVELHL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 108 SNSEledeilclekelkeekSKHSEQDELMADISKRIQSleDESKSLKSQVAEakmtfkiFQMNEERLKIAIKDALNENS 187
Cdd:TIGR01612 725 SNIE----------------NKKNELLDIIVEIKKHIHG--EINKDLNKILED-------FKNKEKELSNKINDYAKEKD 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 188 QLQESQKQLLQEAEVWKEQVSELNKQ----KVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE 263
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKdedaKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCK 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 264 LEMNSESENGAYLDNPPKGAL--------KKLIHAAK--LNASLKTLEGERNQIYiQLSEVD---KTKEELTEHIKNLQT 330
Cdd:TIGR01612 860 EKIDSEHEQFAELTNKIKAEIsddklndyEKKFNDSKslINEINKSIEEEYQNIN-TLKKVDeyiKICENTKESIEKFHN 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 331 EQASLqsenthfeneNQKLQQKLKVMTE---LYQENEMKLHRKLTVEENyRLEKEEKLSKVDEKISHATEELETYRKRAK 407
Cdd:TIGR01612 939 KQNIL----------KEILNKNIDTIKEsnlIEKSYKDKFDNTLIDKIN-ELDKAFKDASLNDYEAKNNELIKYFNDLKA 1007
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1227954615 408 DLEEELERTIhsYQgQIISHEKKAHDNWLAARNAERNLNDL 448
Cdd:TIGR01612 1008 NLGKNKENML--YH-QFDEKEKATNDIEQKIEDANKNIPNI 1045
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
111-423 |
1.35e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 111 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 184
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 185 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 263
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 264 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 343
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 344 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 423
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
78-364 |
1.82e-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: 45.21 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 78 EVESSLKD----ASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKS 153
Cdd:pfam12128 222 QVEHWIRDiqaiAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 154 LKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKE 232
Cdd:pfam12128 302 KRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 233 SHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGE 303
Cdd:pfam12128 382 SKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954615 304 -RNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENE 364
Cdd:pfam12128 462 lLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALD 523
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
53-471 |
3.68e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 53 LSGLIEEKSKLLEK--FSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKH 130
Cdd:TIGR00606 438 LGRTIELKKEILEKkqEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 131 SEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEnSQLQESQKQLLQEAEVWKEQVSEL 210
Cdd:TIGR00606 518 RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKL 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 211 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKmkdwAAMLGEDITDDDNLELEMNSESENGAYLDNppkgalkklihA 290
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEDKLFD----VCGSQDEESDLERLKEEIEKSSKQRAMLAG-----------A 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVD-KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY--QENEMKL 367
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 368 HRKLTVEENYRLEK-EEKLSKVDEKISHATEELETY---RKRAKDLEEELErTIHSYQGQIISHEKKAHD--NWLAARNA 441
Cdd:TIGR00606 742 KEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQMELKDVERKIAQqaAKLQGSDL 820
|
410 420 430
....*....|....*....|....*....|
gi 1227954615 442 ERNLNDLRKENAHNRQKLTETELKFELLEK 471
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
134-246 |
4.00e-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: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 134 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 213
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 1227954615 214 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 246
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-462 |
5.88e-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: 43.42 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 57 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATE-------AQSLEATCEKLNRSNSELEDEilclEKELKEEKSK 129
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihtlQQQKTTLTQKLQSLCKELDIL----QREQATIDTR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 130 HSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSE 209
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 210 LNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLGEDItddDNLELEMNSESENGAYLDNPPKGALKK 286
Cdd:TIGR00618 496 LLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSE---EDVYHQLTSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 287 L-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHIKNLQtEQASLQSENTHFENENQKLQQKLKVMTE 358
Cdd:TIGR00618 572 FsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 359 L-----YQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHAT-------------EELETYRKRAKDLEEELERTIHSy 420
Cdd:TIGR00618 651 LqltltQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlaqcqtllRELETHIEEYDREFNEIENASSS- 729
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1227954615 421 QGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 462
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
291-479 |
7.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY---------- 360
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 361 -----------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 426
Cdd:COG4942 117 grqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1227954615 427 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 479
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
81-430 |
9.00e-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: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 81 SSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSL---EDESKSLKSQ 157
Cdd:pfam15921 327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 158 VAEAKMTFKIFQ-------MNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtFEDSKVHAEQVLND 230
Cdd:pfam15921 407 DTGNSITIDHLRrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ---LESTKEMLRKVVEE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 231 KESHIKTLTERLLKMKDWAAMLGEDitdddnlELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQ 310
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 311 LSEVDKTKEELTEHIKNL--------------QTEQASLQSENTHFENENQKLQ----------QKLKVMTELYQENEMK 366
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilkdkkdakiRELEARVSDLELEKVK 636
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227954615 367 L----HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 430
Cdd:pfam15921 637 LvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
86-414 |
1.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 86 ASFEKEATEAQSLEATCEKLN-------RSNSELEDEIlclEKELKEEKSKHSEQDELMAD----------ISKRIQSLE 148
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRetiaeteREREELAEEV---RDLRERLEELEEERDDLLAEaglddadaeaVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 149 DESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL---LQEAEV----WKEQVSELNKQKVTFEDSK 221
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseLEEAREavedRREEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 222 VHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITdddnlELEMNSESENGAYLDNppkgalKKLIHAAKLNASLKTLE 301
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREER-------DELREREA-----ELEATLRTARERVEEA------EALLEAGKCPECGQPVE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 302 GErnQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHF------ENENQKLQQKLKVMTELYQENEMKLHRKLTVEE 375
Cdd:PRK02224 463 GS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1227954615 376 NYRLEKEEKLSKVDEKISHAT---EELETYRKRAKDLEEELE 414
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAeaeEEAEEAREEVAELNSKLA 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-337 |
1.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 53 LSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEA-------QSLEATCEKLNRSNSELEDEILCLEKELKE 125
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeaeiEELEAQIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 126 EKSKHSEQDE-------LMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQ 198
Cdd:TIGR02168 815 LNEEAANLRErleslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 199 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwaamlgEDITDDDNLELEMNSESENGayLDN 278
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ-------ERLSEEYSLTLEEAEALENK--IED 965
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 279 PPKGALKKLIhaaKLNASLKTLeGERNQIYIQ-LSEVDKTKEELTEHIKNLQTEQASLQS 337
Cdd:TIGR02168 966 DEEEARRRLK---RLENKIKEL-GPVNLAAIEeYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
57-415 |
1.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 57 IEEKSKLLEKFSLVQKEYEGYEVEssLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSE---- 132
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkka 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 133 ---------------QDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQM--NEERLKIAIKDALNENSQLQESQKQ 195
Cdd:PRK03918 435 kgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlKKESELIKLKELAEQLKELEEKLKK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 196 L--------LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLEL 264
Cdd:PRK03918 515 YnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 265 EmNSESENGAYLDnpPKGALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----EQASLQSEN 339
Cdd:PRK03918 595 K-ELEPFYNEYLE--LKDAEKEL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEY 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954615 340 THFENENQKLQQKLKVMTELYQENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 415
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-239 |
1.31e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 32 RSFRSVRSRLY-----VGREKKLALMLSGLIEEKSKLLEKFSLVQKEYE--GYEVESSLKDASFEKEATEAQSleatcEK 104
Cdd:TIGR02168 817 EEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEAL-----AL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 105 LNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAE-AKMTFKIFQMNEERLKIAIKDAL 183
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEAR 971
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227954615 184 NENSQLQESQKQL-------LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLN--DKESHIKTLT 239
Cdd:TIGR02168 972 RRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEeiDREARERFKD 1036
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
303-370 |
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 1227954615 303 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 370
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-421 |
1.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 297 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 370
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954615 371 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 421
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-414 |
2.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 78 EVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQ 157
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 158 VAEakmtfkifqmNEERlkiaikdalneNSQLQESQKQLLQEAEVWKEQVSELN--KQKVTFEdsKVHAEQVLNDKESHI 235
Cdd:pfam01576 84 LEE----------EEER-----------SQQLQNEKKKMQQHIQDLEEQLDEEEaaRQKLQLE--KVTTEAKIKKLEEDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 236 KTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNppkgalKKLIHAAKLNASLKTLEGERNQIYIQLSEVD 315
Cdd:pfam01576 141 LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKN------KHEAMISDLEERLKKEEKGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 316 KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENE-MKLHRKLtveENYRLEKEEKLSKvdEKISH 394
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKNNaLKKIREL---EAQISELQEDLES--ERAAR 287
|
330 340
....*....|....*....|
gi 1227954615 395 ATEEletyrKRAKDLEEELE 414
Cdd:pfam01576 288 NKAE-----KQRRDLGEELE 302
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
108-457 |
2.44e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 108 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEN- 186
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERk 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 187 -------SQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 258
Cdd:pfam12128 678 dsanerlNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 259 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 329
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 330 TEQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 407
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1227954615 408 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 457
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
228-433 |
2.63e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 228 LNDKESHIKTL----TERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLdNPPKGALKKLIHAAKLN-----ASLK 298
Cdd:pfam05483 235 INDKEKQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSlqrsmSTQK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 299 TLEGE---RNQIYIQLSEVDKTKEE------------LTEHIKNLQTEQASLQSENTHFENENQKLqqKLKVMTELYQEN 363
Cdd:pfam05483 314 ALEEDlqiATKTICQLTEEKEAQMEelnkakaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQL--KIITMELQKKSS 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 364 EMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETyrkrakdLEEELERTIHSYQGQIISHEKKAHD 433
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEK-------IAEELKGKEQELIFLLQAREKEIHD 454
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
137-362 |
2.80e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 137 MADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNeerlkiaikdalNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 216
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 217 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 290
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954615 291 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 362
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
134-461 |
3.22e-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: 40.61 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 134 DELMADISKRIQSLEDESKSLKSQvaeakmtfkifqmnEERLKIAIKDALNEnsqLQESQKQLLQEAEVWKEQVSELNKQ 213
Cdd:pfam06160 92 EELLDDIEEDIKQILEELDELLES--------------EEKNREEVEELKDK---YRELRKTLLANRFSYGPAIDELEKQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 214 KVTFEDSKVHAEQvLNDKESHIKtlterllkmkdwAAMLGEDITDD-DNLELEMNsesengayldnppkgALKKLIHAAK 292
Cdd:pfam06160 155 LAEIEEEFSQFEE-LTESGDYLE------------AREVLEKLEEEtDALEELME---------------DIPPLYEELK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 293 ---------LNASLKTLEG-----ERNQIYIQLSEVDKTKEELTEHIKNLQTEQAslqsenthfENENQKLQQKLKVMTE 358
Cdd:pfam06160 207 telpdqleeLKEGYREMEEegyalEHLNVDKEIQQLEEQLEENLALLENLELDEA---------EEALEEIEERIDQLYD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 359 LyqenemklhrkLTVEENYRLEKEEKLSKVDEKISHATEELetyrkraKDLEEELERTIHSYqgqIISHEKKAHdnwlaA 438
Cdd:pfam06160 278 L-----------LEKEVDAKKYVEKNLPEIEDYLEHAEEQN-------KELKEELERVQQSY---TLNENELER-----V 331
|
330 340
....*....|....*....|...
gi 1227954615 439 RNAERNLNDLRKENAHNRQKLTE 461
Cdd:pfam06160 332 RGLEKQLEELEKRYDEIVERLEE 354
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
58-467 |
3.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 58 EEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELM 137
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 138 ADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKiaiKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtf 217
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA---- 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 218 EDSKVHAEQVLNDKEShiktlterllKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAklnasl 297
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEA----------KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA------ 1569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 298 KTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtelYQENEMKLHRKLTVEENY 377
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEEEKKKVEQLKKKEAE 1644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 378 RLEKEEKLSKVDEKISHATEEL----ETYRKRAKDL--EEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 451
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEakkaEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
410
....*....|....*.
gi 1227954615 452 NAHNRQKLTETELKFE 467
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAE 1740
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
172-494 |
4.23e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 172 EERLKIAIKDALNENSQ--LQESQKQLLQEaevwKEQVSELNKQKVTF-EDSKVHAEQVLNDKESHIKTLTERLLKMKDW 248
Cdd:COG5022 858 KKRFSLLKKETIYLQSAqrVELAERQLQEL----KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 249 AAMLgEDITDDDNLELEMNSESENGAYLDNppkgalkklihaaklNASLKTLEGERNQIYIQL-----------SEVDKT 317
Cdd:COG5022 934 KKLL-NNIDLEEGPSIEYVKLPELNKLHEV---------------ESKLKETSEEYEDLLKKStilvregnkanSELKNF 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 318 KEELTEHIKNLQTEQASLQS--ENTHFENENQKLQQKLKVM-TELYQENEM-KLHRKLTVEENYrLEKEEKLSKVDEKIS 393
Cdd:COG5022 998 KKELAELSKQYGALQESTKQlkELPVEVAELQSASKIISSEsTELSILKPLqKLKGLLLLENNQ-LQARYKALKLRRENS 1076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 394 HATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNwlaARNAERNLNDLRKENAHNRQKLTETELKFELLEKDP 473
Cdd:COG5022 1077 LLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQF---IVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQ 1153
|
330 340
....*....|....*....|.
gi 1227954615 474 YALDVPNTAFGREHSPYGPSP 494
Cdd:COG5022 1154 LELDGLFWEANLEALPSPPPF 1174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
44-414 |
5.77e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 44 GREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDE---ILCLE 120
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdMTLEL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 121 KELKEEKSKHSEQDELMAdisKRIQSLEDESKSLKSQVAEAKMTFKIfQMNEERLKIaikDALNENSQLQESqkQLLQEA 200
Cdd:pfam05483 516 KKHQEDIINCKKQEERML---KQIENLEEKEMNLRDELESVREEFIQ-KGDEVKCKL---DKSEENARSIEY--EVLKKE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 201 EVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLgeditddDNLELEMNSESEN-GAYLDNp 279
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV-------NKLELELASAKQKfEEIIDN- 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 280 pkgaLKKLIHAAKLnaSLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHfenenqklqQKLKVMTEl 359
Cdd:pfam05483 659 ----YQKEIEDKKI--SEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKH---------QYDKIIEE- 722
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954615 360 yQENEMKLHRKLTVEE-NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELE 414
Cdd:pfam05483 723 -RDSELGLYKNKEQEQsSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
49-415 |
5.93e-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: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 49 LALMLSGLIEEKS--KLLEKFSLVQKEYEGYEVESSlKDASFEKEATEAQSLEATCeKLNRSNSELEDEiLCLEKELKEE 126
Cdd:pfam05911 461 ISVILESHVTQKSigKILEDIRCALQDINDSLPEAD-SCLSSGHPSTDASCDYITC-KENSSVVEKEGS-VSGDDKSSEE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 127 KSKHSEQDELMADISKRIQSLEDESK-SLKSQvaeaKMTFKIFQMNE--ERLKIAIKDALNENSQLQESQKQLlqeaevw 203
Cdd:pfam05911 538 TSKQSIQQDLSKAISKIIDFVEGLSKeALDDQ----DTSSDSSELSEvlQQFSATCNDVLSGKADLEDFVLEL------- 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 204 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGA 283
Cdd:pfam05911 607 SHILDWISNHCFSLLDVSSMEDEIKKHDCIDKVTLSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRL 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 284 LKKLIhaaKLNASLKTLEGERnQIYIQLSEVDKTK-EELTEHIKNLQTEQASLQsenthfeNENQKLQQKLKVMTELYQE 362
Cdd:pfam05911 687 KEEFE---QLKSEKENLEVEL-ASCTENLESTKSQlQESEQLIAELRSELASLK-------ESNSLAETQLKCMAESYED 755
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1227954615 363 NEMKLhRKLTVEENYRLEKEEKLSKVDEKISHATEELETyrkRAKDLEEELER 415
Cdd:pfam05911 756 LETRL-TELEAELNELRQKFEALEVELEEEKNCHEELEA---KCLELQEQLER 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-463 |
6.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 380 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 459
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 1227954615 460 TETE 463
Cdd:COG4942 100 EAQK 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-414 |
7.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 46 EKKLALMLSGLIEEKSKLLEKfsLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKE 125
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 126 EKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQK-QLLQEAEVwK 204
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKaDEAKKAEE-K 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 205 EQVSELNK-QKVTFEDSKVHAEQVLNDKESHIKTLtERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGA 283
Cdd:PTZ00121 1546 KKADELKKaEELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 284 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtelYQEN 363
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK-----KEAE 1699
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1227954615 364 EMKLHRKLTVEENYRLEKEEKLSKVDE----KISHATEELETYRKRAKDLEEELE 414
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
169-416 |
7.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 169 QMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKvtfedsKVHAEQVLNDKEShIKTLTERLLKMKDW 248
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQV------KELREEAQELREK-RDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 249 AAMLGEDITDDDNlELEMNSESENGAYLDNPPKGALKKLIhaAKL-----NASLkTLEGERnQIYIQLSEVD------KT 317
Cdd:COG1340 80 RDELNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEI--ERLewrqqTEVL-SPEEEK-ELVEKIKELEkelekaKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 318 KEELTEHIKNLQTEQASLQSE-NTHFENEN---QKLQQKLKVMTELYQE-NEMK-----LHRKLtveenyrLEKEEKLSK 387
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEaEEIHKKIKelaEEAQELHEEMIELYKEaDELRkeadeLHKEI-------VEAQEKADE 227
|
250 260
....*....|....*....|....*....
gi 1227954615 388 VDEKISHATEELETYRKRAKDLEEELERT 416
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
291-443 |
7.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 291 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL-KVMTELYQE------- 362
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSggsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 363 -------------NEMKLHRKLTVEENYRLEK----EEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQI- 424
Cdd:COG3883 106 dvllgsesfsdflDRLSALSKIADADADLLEElkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLa 185
|
170 180
....*....|....*....|
gi 1227954615 425 -ISHEKKAHDNWLAARNAER 443
Cdd:COG3883 186 qLSAEEAAAEAQLAELEAEL 205
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-415 |
8.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 78 EVESSLKDAS-----FEKEAT----EAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRI---- 144
Cdd:PRK02224 325 ELRDRLEECRvaaqaHNEEAEslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdap 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 145 ---QSLEDESKSLKSQVAEAKMtfkifQMNEERLKI-AIKDALNENSQLQESQK-----QLLQEA------EVWKEQVSE 209
Cdd:PRK02224 405 vdlGNAEDFLEELREERDELRE-----REAELEATLrTARERVEEAEALLEAGKcpecgQPVEGSphvetiEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 210 LNKQKVTFEDSKVHAEQVLNDKESHIKTLT--ERLLKMKDWAAMLGED---ITDDDNLELEmnSESENGAYLDNppkgal 284
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAErreTIEEKRERAE--ELRERAAELEA------ 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 285 kkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTeQASLQSENTHFENENQKLQQKLKVMTELYQENE 364
Cdd:PRK02224 552 ----EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227954615 365 MKL----HRKLTVEENY---RLEK--------EEKLSKVDEKISHATEELETYRKRAKDLEEELER 415
Cdd:PRK02224 627 ERLaekrERKRELEAEFdeaRIEEaredkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
87-467 |
9.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 87 SFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELM----------------------------- 137
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdeqlndlyhnhqrtvrekerel 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 138 ADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLK--IAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKV 215
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 216 TFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIhaaKLNA 295
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL---ELDQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 296 SLKTLEGErnqiyIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKlkvmTELYQENEMKLHRKLTvee 375
Cdd:TIGR00606 479 ELRKAERE-----LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH----TTTRTQMEMLTKDKMD--- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 376 nyrleKEEKLSKVDEKISHATEELETYRKRAKdleeELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKEnahn 455
Cdd:TIGR00606 547 -----KDEQIRKIKSRHSDELTSLLGYFPNKK----QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE---- 613
|
410
....*....|..
gi 1227954615 456 RQKLTETELKFE 467
Cdd:TIGR00606 614 LESKEEQLSSYE 625
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
286-462 |
9.64e-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: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 286 KLIHAAKLNASLKTLEGErNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENenqklQQKLKVMTelYQENEM 365
Cdd:pfam09787 25 KLIASLKEGSGVEGLDSS-TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA-----QQQEEAES--SREQLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 366 KLHRKLTVEENYRLEKEEKLSKVDEKISHateeletyrkrakdLEEELERTIHSYQGQIISHEKKAHDnwLAARNAERNL 445
Cdd:pfam09787 97 ELEEQLATERSARREAEAELERLQEELRY--------------LEEELRRSKATLQSRIKDREAEIEK--LRNQLTSKSQ 160
|
170
....*....|....*...
gi 1227954615 446 NDLRKENAHNRQK-LTET 462
Cdd:pfam09787 161 SSSSQSELENRLHqLTET 178
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
60-352 |
9.78e-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: 39.02 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 60 KSKLLEK--FSLVQkeyEGYEVESSLKDASFEKEATEAQSLEATCEK--LNRSNSELEDEILCLEKELKEEKSKHSEQDE 135
Cdd:pfam15905 74 DQKELEKeiRALVQ---ERGEQDKRLQALEEELEKVEAKLNAAVREKtsLSASVASLEKQLLELTRVNELLKAKFSEDGT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 136 lmadiSKRIQSLEDESKSLKSQVaEAKMtfKIFQMNEERLKIaikdalnensQLQESQKQLLQEaevwKEQVSELNKQKV 215
Cdd:pfam15905 151 -----QKKMSSLSMELMKLRNKL-EAKM--KEVMAKQEGMEG----------KLQVTQKNLEHS----KGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 216 TFEDSKV----HAEQVLNDKEsHIKTLTERLLKMKDWAAMLGEDI-TDDDNLELEMNSESENgayldnppKGALKKLIHa 290
Cdd:pfam15905 209 STEKEKIeeksETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLkEKNDEIESLKQSLEEK--------EQELSKQIK- 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227954615 291 aKLNASLKTLEGERNQIYIQlsevDKTKEEltehikNLQTEQASLQSENTHFENENQKLQQK 352
Cdd:pfam15905 279 -DLNEKCKLLESEKEELLRE----YEEKEQ------TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
282-448 |
9.95e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 282 GALKKLIHAAKLNASLKTLEGERNQIYIQLsevdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLkvmtelyQ 361
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKALL-------DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-------E 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227954615 362 ENEMKLHRKLTvEENYRLEKEEkLSKVDEKIshaTEELETYRKRAKDLEEELERTIHSYQGQiISHEKKAHDNWLAARNA 441
Cdd:cd22656 160 TLEKALKDLLT-DEGGAIARKE-IKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAK-LAAALRLIADLTAADTD 233
|
....*..
gi 1227954615 442 ERNLNDL 448
Cdd:cd22656 234 LDNLLAL 240
|
|
| |
