|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-563 |
1.02e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 287 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 366
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 367 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 446
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 447 EAEFSSAGHSLQDKQSVEetsgegpevemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 526
Cdd:COG1196 381 LEELAEELLEALRAAAEL--------------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270
....*....|....*....|....*....|....*..
gi 966915605 527 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-563 |
1.16e-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: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 298 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 374
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 375 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 454
Cdd:TIGR02168 742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 455 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEK-------QQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRR 527
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270
....*....|....*....|....*....|....*.
gi 966915605 528 DSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-592 |
4.75e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 274 ALLGRPAPFGDVCLLRLQELqRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRE----------SLKVALQKH 343
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqisALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 344 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPtlEDHQKQSQQLKDSELKSTELQEKVTELE 423
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE--AQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 424 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQV 503
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 504 QSLEQEVAQEEGTSQALREEaqrrdsaLQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppsPDTAQLALELYQEL 583
Cdd:TIGR02168 897 EELSEELRELESKRSELRRE-------LEELREKLAQLELRLEGLEVRIDNLQERLSEEY------SLTLEEAEALENKI 963
|
....*....
gi 966915605 584 ASCLQDLQA 592
Cdd:TIGR02168 964 EDDEEEARR 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
289-563 |
9.31e-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: 68.56 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 360
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 361 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 426
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 427 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 506
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 966915605 507 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-506 |
7.98e-10 |
|
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: 62.38 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 243 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 317
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 318 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 391
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 392 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGP 471
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270
....*....|....*....|....*....|....*
gi 966915605 472 EVEMESWQKQYDSLqKIVEKQQQKMDQLRSQVQSL 506
Cdd:TIGR02168 495 ERLQENLEGFSEGV-KALLKNQSGLSGILGVLSEL 528
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
172-559 |
1.05e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 61.76 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 172 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 249
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 250 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 301
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 302 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 365
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 366 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 445
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 446 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE--------------VA 511
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLS 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 966915605 512 QEEGTSQALREEAQRRDsalQQLRTAVKELSVQNQDLIEKNLTLQEHL 559
Cdd:pfam10174 447 EKERIIERLKEQRERED---RERLEELESLKKENKDLKEKVSALQPEL 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-539 |
1.53e-09 |
|
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: 60.16 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 305 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 381
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 382 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQ 461
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915605 462 SVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 539
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
231-555 |
2.88e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 231 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 305
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 306 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 385
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 386 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 463
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 464 EETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELsv 543
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-- 543
|
330
....*....|..
gi 966915605 544 qNQDLIEKNLTL 555
Cdd:TIGR04523 544 -EDELNKDDFEL 554
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
376-651 |
3.02e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 376 REKQQRIETLE-------RYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQR 446
Cdd:COG1196 196 GELERQLEPLErqaekaeRYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 447 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 526
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 527 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppsPDTAQLALELYQELASCLQDLQAVCSIVTQRAQGHDP 606
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966915605 607 NLSLLLGIHSAQHPETQLDLQkpdvIKRKLEEVQQLRRDIEDLRT 651
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEE----EAELEEEEEALLELLAELLE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
188-593 |
4.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 188 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 267
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 268 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 347
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 348 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 427
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 428 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSgegpevemESWQKQYDSLQKIVEKQQQKMDQLR-SQVQSL 506
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL--------LEAEADYEGFLEGVKAALLLAGLRGlAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 507 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKnLTLQEHLRQAQPGSPPSPDTAQLALELYQELASC 586
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
....*..
gi 966915605 587 LQDLQAV 593
Cdd:COG1196 608 LREADAR 614
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
345-582 |
4.68e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 345 EEVKKQEERVKGRDKH--INNLKKKCQKESEQ----NREKQQRIETLERylADLpTLEDHQKQSQQLKDSELKSTELQEK 418
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHerLNGLESELAELDEEieryEEQREQARETRDE--ADE-VLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 419 VTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQ 498
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 499 LRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQnQDLIEKNLtlqEHLRQAQPGSPPSPDTAQLALE 578
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE-IEELEEEI---EELRERFGDAPVDLGNAEDFLE 415
|
....
gi 966915605 579 LYQE 582
Cdd:PRK02224 416 ELRE 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-561 |
7.19e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 319
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 320 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 399
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 400 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQdkqsvEETSGEgpevEMESWQ 479
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-----EEHRKE----LLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 480 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEegtsqalrEEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHL 559
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKE--------SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
..
gi 966915605 560 RQ 561
Cdd:PRK03918 531 KE 532
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-563 |
9.27e-09 |
|
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: 58.91 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 358 DKHINNLKKKCQKeSEQNREKQQRIETLERYLA--DLPTLEDHQKQSQ--------QLKDSELKSTELQEKVTELESLLE 427
Cdd:TIGR02168 199 ERQLKSLERQAEK-AERYKELKAELRELELALLvlRLEELREELEELQeelkeaeeELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 428 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 507
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966915605 508 QEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
290-557 |
1.41e-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: 58.11 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 290 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 367
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 368 CQKESEQNREKQQRIETLERYLADLPT--------LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 437
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKqlnqlkseISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 438 TQLESLRQreaefssaghSLQDKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgts 517
Cdd:TIGR04523 342 EQISQLKK----------ELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE--- 404
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 966915605 518 qalrEEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQE 557
Cdd:TIGR04523 405 ----KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-509 |
2.03e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 184 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 261
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 262 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 341
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 342 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT-LEDHQKQSQQLKDSELKSTELQEKVT 420
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKeRDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 421 ELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSV-----EETSGEGP-----EVEMESWQKQYDSLQKIVE 490
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveEEIRALEPvnmlaIQEYEEVLKRLDELKEKRA 996
|
330
....*....|....*....
gi 966915605 491 KQQQKMDQLRSQVQSLEQE 509
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
253-495 |
3.08e-08 |
|
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: 55.97 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 253 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 325
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 326 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 398
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 399 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQREaefssaghslqdkqsveETSGEGPEVEME 476
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREY-----------------EEKEQTLNAELE 310
|
250
....*....|....*....
gi 966915605 477 SWQKQYDSLQKIVEKQQQK 495
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
300-568 |
5.64e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.22 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 300 LRAQFAQKTEALSREKIDLEKKLSASEVEVQLiresLKVALQKHSEEVKKQEERVKGRDKHiNNLKKKCQKESEQNREkq 379
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMSTDALEQEI----LQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARRQ-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 380 qrIETLERYLADLPTLEDHQKQSQqLKDSELKSTELQEKVTELEslLEE-----TQAICRDR------------------ 436
Cdd:PRK10929 153 --LNEIERRLQTLGTPNTPLAQAQ-LTALQAESAALKALVDELE--LAQlsannRQELARLRselakkrsqqldaylqal 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 437 ETQLESLRQREAEfssagHSLQDKQSVEETSGEGPEVEMESWQKQYDsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT 516
Cdd:PRK10929 228 RNQLNSQRQREAE-----RALESTELLAEQSGDLPKSIVAQFKINRE-LSQALNQQAQRMDLIASQQRQAASQTLQVRQA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915605 517 SQALREEAQRRDSA-------------------LQQLRTAVKELSVQN---QDLIEKnltLQEHLRQAQPGSPP 568
Cdd:PRK10929 302 LNTLREQSQWLGVSnalgealraqvarlpempkPQQLDTEMAQLRVQRlryEDLLNK---QPQLRQIRQADGQP 372
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
351-558 |
5.65e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 351 EERVKGRDKHINNLKKKcqkESEQNREKQQRIETLeryladLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQ 430
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKK---NGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 431 AicrDRETQLESLrQREAEFSSAGHS----LQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQ---V 503
Cdd:PHA02562 265 A---KIKSKIEQF-QKVIKMYEKGGVcptcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEIMDEFNEQskkL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 966915605 504 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAV----KELSVQNQDLIEKNLTLQEH 558
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnaEELAKLQDELDKIVKTKSEL 398
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
372-592 |
6.57e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 372 SEQNREKQQRIETLERYLADLptledhqKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 451
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 452 SAGHSLQDKQSVEETSGEgpEVEMESwqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE-EGTSQALREEAQRRDSA 530
Cdd:COG3206 254 DALPELLQSPVIQQLRAQ--LAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAR 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 531 LQQLRTAVKELSVQNQDLIEKNLTLQEHLRQaqpgsppspdtAQLALELYQELASCLQDLQA 592
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLERE-----------VEVARELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-563 |
9.34e-08 |
|
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: 54.77 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 338 VALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQE 417
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 418 KVTELESLLEETQAICRDRETQLESLRQREA--------EFSSAGHSLQDKQSVeetsgegpeveMESWQKQYDSLQKIV 489
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPlalllspeDFLDAVRRLQYLKYL-----------APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915605 490 EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
339-525 |
3.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 339 ALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEK 418
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 419 VTELESLLEEtqaiCRDRETQLESLRQREAEfssaghsLQDKQSVEEtsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQ 498
Cdd:COG4717 155 LEELRELEEE----LEELEAELAELQEELEE-------LLEQLSLAT------EEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*..
gi 966915605 499 LRSQVQSLEQEVAQEEGTSQALREEAQ 525
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-648 |
6.07e-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: 52.76 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 370 KESEQNREKQQRIETLERYLADLPT---------------------------------LEDHQKQSQQLKDSELKSTELQ 416
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSelrrienrldelsqelsdasrkigeiekeieqlEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 417 EKVTELESLLEETQAICRDRETQLESLRQREAEFSSAghslQDKQSVEETSGEGPEVEME--SWQKQYDSLQKIVEKQQQ 494
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----LSHSRIPEIQAELSKLEEEvsRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 495 KMDQLRSQVQSLEQEV-------AQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGsp 567
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRidlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK-- 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 568 pspdTAQLALElYQELASCLQDLQAVCSIVTQRAQGHDPNLSLLLGIhsaqhPETQLDLQKpdvIKRKLEEVQQLRRDIE 647
Cdd:TIGR02169 905 ----IEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-----PEEELSLED---VQAELQRVEEEIRALE 971
|
.
gi 966915605 648 D 648
Cdd:TIGR02169 972 P 972
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
306-550 |
8.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 306 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 385
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 386 ERYLADLPTLEDHQKQSQQLK----DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSsaghSLQDKQ 461
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 462 SVEETSGEGPE------VEMESWQKQYDSLQkiVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 535
Cdd:PRK03918 355 EELEERHELYEeakakkEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
250
....*....|....*
gi 966915605 536 TAVKELSVQNQDLIE 550
Cdd:PRK03918 433 KAKGKCPVCGRELTE 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-592 |
9.46e-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: 52.38 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 345 EEVKKQEERVKGRDKHINNLKKKCQKESEQN---REKQQRIETLERYLAdLPTLEDHQKQSQQLkDSELksTELQEKVTE 421
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEGYEL-LKEKEALERQKEAI-ERQL--ASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 422 LESLLEETQAICRDRETQLESLRQREAEFSSaGHSLQDKQSVEETSGEGPEVE--MESWQKQYDSLQKIVEKQQQKMDQL 499
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLRVKEKIGELEAEIASLErsIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 500 RSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALEL 579
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250
....*....|...
gi 966915605 580 YQELASCLQDLQA 592
Cdd:TIGR02169 415 LQRLSEELADLNA 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-563 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 376 REKQQRIETLERYLADLptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssagh 455
Cdd:COG4913 258 RELAERYAAARERLAEL----EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL----- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 456 slqdKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 535
Cdd:COG4913 329 ----EAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*...
gi 966915605 536 TAVKELSVQNQDLIEKnltLQEHLRQAQ 563
Cdd:COG4913 401 EALEEALAEAEAALRD---LRRELRELE 425
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
307-588 |
1.16e-06 |
|
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: 52.36 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 307 KTEAlSREKIDLEK-----KLSASEVEVqLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQR 381
Cdd:TIGR01612 1499 KDEA-DKNAKAIEKnkelfEQYKKDVTE-LLNKYSALAIKNKFAKTKKDSEIII---KEIKDAHKKFILEAEKSEQKIKE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 382 IETLERYLADLPTLEDH--------QKQSQQLKDSELKSTELQEKVTELeslLEETQAIcrDRETQLESLRQREAEFSSA 453
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKsnkaaidiQLSLENFENKFLKISDIKKKINDC---LKETESI--EKKISSFSIDSQDTELKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 454 GHSLQDKQSVeetsgegpeveMESWQKQydslQKIVEKQQQKMDQLRSQVQSLEQEVAQ-----EEGTSQALREEAQRRD 528
Cdd:TIGR01612 1649 GDNLNSLQEF-----------LESLKDQ----KKNIEDKKKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANK 1713
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915605 529 SALQQLRTAVKEL------SVQNQDL--IEKNLTLQEHLRQAQpgsppspDTAQLALELYQELASCLQ 588
Cdd:TIGR01612 1714 EEIESIKELIEPTienlisSFNTNDLegIDPNEKLEEYNTEIG-------DIYEEFIELYNIIAGCLE 1774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-557 |
1.31e-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: 51.99 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 306
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 307 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL-----QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK 378
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 379 QQRIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQ 458
Cdd:TIGR02169 832 EKEIQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 459 DKQSVEETsgegpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE---------GTSQALREEAQRRDS 529
Cdd:TIGR02169 903 RKIEELEA--------------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVEEEIR 968
|
330 340 350
....*....|....*....|....*....|....*.
gi 966915605 530 AL--------QQLRTAVKELSvqnqDLIEKNLTLQE 557
Cdd:TIGR02169 969 ALepvnmlaiQEYEEVLKRLD----ELKEKRAKLEE 1000
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
240-513 |
1.36e-06 |
|
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: 51.65 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQeLQRENTFLRA-----QFAQKT-EALSR 313
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMS-LQRSMSTQKAleedlQIATKTiCQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 314 EKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE-------KQQRIETLE 386
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 387 RYLADLPTLEDHQKQSQQLKDsELKSTE------LQEKVTELESLLEETQAI----------CRDRETQLESLRQREAEF 450
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAE-ELKGKEqeliflLQAREKEIHDLEIQLTAIktseehylkeVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 451 SSAGH--SLQDKQSVEETSGEGPEV-----EMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE 513
Cdd:pfam05483 491 TAHCDklLLENKELTQEASDMTLELkkhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
289-557 |
1.65e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRE-NTFLRAQFAQK------TEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhi 361
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANrqrekeKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 362 nnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvteleslLEET 429
Cdd:pfam07888 113 --LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK-------LQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 430 QAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 506
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 966915605 507 eqevaqeegtsQALREEAQrrdSALQQLRTAVKELSVQnqdLIEKNLTLQE 557
Cdd:pfam07888 264 -----------AAQRDRTQ---AELHQARLQAAQLTLQ---LADASLALRE 297
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
307-563 |
2.43e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 307 KTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE------VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQ 380
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 381 RIETLERyladlpTLEDHQKQSQQLKDSELK-STELQEKVTELES---LLEETQAICRDRETQLESLR-QREAEFSSAGH 455
Cdd:TIGR04523 240 EINEKTT------EISNTQTQLNQLKDEQNKiKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNnQKEQDWNKELK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 456 SlqdkqsveetsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 535
Cdd:TIGR04523 314 S-----------------ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260
....*....|....*....|....*...
gi 966915605 536 TAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQE 404
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
288-660 |
2.59e-06 |
|
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: 50.82 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 288 LRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 367
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL--ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 368 -------CQKESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQLKD-----SELKSTELQEKVTELESLLEETQA 431
Cdd:TIGR00606 676 nqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDklksTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNKLQK 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 432 ICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEgpeveMESWQKQYDSLQKIVEKQQQKMD--QLRSQVQSLEQE 509
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-----MERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQE 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 510 VAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspDTAQLALELYQELASCLQD 589
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-------QFEEQLVELSTEVQSLIRE 903
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915605 590 LQAVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDRYAQD 660
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ 974
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
251-541 |
2.65e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 251 DKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQ 330
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 331 lireslkvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQ----SQQL 405
Cdd:pfam07888 140 --------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQrdtqVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 406 KDS----ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGhSLQDKQSVE---------ETSGEGPE 472
Cdd:pfam07888 212 QDTittlTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA-AQRDRTQAElhqarlqaaQLTLQLAD 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915605 473 VEME------SWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE-AQRRDSALQQLRTAVKEL 541
Cdd:pfam07888 291 ASLAlregraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVElGREKDCNRVQLSESRREL 366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
301-582 |
2.91e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 301 RAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVA--LQKHSEEVKKQEERVKGRD--KHINNLKKKCQkES 372
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK--AEEKkkadEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAE-EA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 373 EQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE-------LKSTELQEKVTELESLLEETQAicrDRETQLESLRQ 445
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkadeAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 446 REA--EFSSAGHSLQDKQSVEETSGEGPEVE---MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAL 520
Cdd:PTZ00121 1560 AEEkkKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 521 REEAQRRDSAlQQLRTAVKELSVQNQDLIEKNltlQEHLRQAQPGSPPSPDTAQLALELYQE 582
Cdd:PTZ00121 1640 KKEAEEKKKA-EELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
306-663 |
3.91e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 306 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 385
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 386 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 449
Cdd:PRK02224 320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 450 FSSAGHSLQD----KQSVEETSGE--GPEVEMESWQKqydSLQKIVEKQQQ---------------------KMDQLRSQ 502
Cdd:PRK02224 400 FGDAPVDLGNaedfLEELREERDElrEREAELEATLR---TARERVEEAEAlleagkcpecgqpvegsphveTIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 503 VQSLEQEVAQeegtsqaLREEAQRRDSALQQLRTAVkELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQE 582
Cdd:PRK02224 477 VEELEAELED-------LEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 583 LASCLQDlqavcsivtQRAQGhdpnlslllgihSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDR--YAQD 660
Cdd:PRK02224 549 LEAEAEE---------KREAA------------AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIadAEDE 607
|
...
gi 966915605 661 MGE 663
Cdd:PRK02224 608 IER 610
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-522 |
4.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 319
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 320 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVkgrdKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhq 399
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 400 kqSQQLKDSELKSTELQEKVTELESLLEETQAICRDretqLESLRQREAEFSSAghsLQDKQSVEETSGEGPEVEMESWQ 479
Cdd:PRK03918 320 --EEEINGIEERIKELEEKEERLEELKKKLKELEKR----LEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 966915605 480 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 522
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
240-542 |
4.96e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 318
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 319 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 398
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 399 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 474
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915605 475 MESWQK---QYDSLQKIVEKQQQkmDQLRSQVQSLEQEVAQEEGTSQalrEEAQRRDSALQQLRTAVKELS 542
Cdd:pfam17380 501 LEERKQamiEEERKRKLLEKEME--ERQKAIYEEERRREAEEERRKQ---QEMEERRRIQEQMRKATEERS 566
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
287-535 |
6.23e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 287 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhinnlk 365
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTAR-------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 366 kkcqKESEQNREKQ---QRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQ-EKVTELESLLEETQAICRDRETQLE 441
Cdd:COG3096 499 ----ELLRRYRSQQalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 442 SLRQREAEFSSAGHSLQDKQsvEETSGEGPEvemesWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 521
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARI--KELAARAPA-----WLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERD 647
|
250
....*....|....
gi 966915605 522 EEAQRRDSALQQLR 535
Cdd:COG3096 648 ELAARKQALESQIE 661
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
302-551 |
8.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 302 AQFAQKTEALSREKIDLEKKLSASEV---------EVQLIRESLKV----ALQKHSEEVKKQEERVKGRDKHINNLKKKC 368
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 369 QKESEQNREK---QQRIETLERYLADLptledhQKQSQQLKDSELKstELQEKVTELESLLE---ETQAICRDRETQLES 442
Cdd:PRK03918 549 EKLEELKKKLaelEKKLDELEEELAEL------LKELEELGFESVE--ELEERLKELEPFYNeylELKDAEKELEREEKE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 443 LRQREAEFSSAGHSLQD-KQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 521
Cdd:PRK03918 621 LKKLEEELDKAFEELAEtEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
250 260 270
....*....|....*....|....*....|
gi 966915605 522 EEAQRRDSALQQLRTAVKELSvQNQDLIEK 551
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALE-RVEELREK 729
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-540 |
1.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 366
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 367 KCQKESEQNREKQQRIETLERYLADlptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrdretQLESLRQR 446
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKAD-----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK--------KADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 447 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEvAQEEGTSQALREEAQR 526
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEE 1402
|
250
....*....|....
gi 966915605 527 RDSALQQLRTAVKE 540
Cdd:PTZ00121 1403 DKKKADELKKAAAA 1416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-562 |
1.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 407 DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssaghslqdkQSVEETSGEgpEVEMESWQKQYDSLQ 486
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 487 ---KIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEK-----NLTLQEH 558
Cdd:COG4913 675 aelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEER 754
|
....
gi 966915605 559 LRQA 562
Cdd:COG4913 755 FAAA 758
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-528 |
1.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELlidKQRKHISQLEQKVRESElqvHSALLGRPAPfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLE 319
Cdd:PTZ00121 1549 DELKKAEEL---KKAEEKKKAEEAKKAEE---DKNMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 320 KKLSASEV-EVQLIRESLKVALQKHSEEVKKQEErVKGRDKHINNLKKKCQKESEQNREKQQRIETLEryladlptlEDH 398
Cdd:PTZ00121 1618 AKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE---------EDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 399 QKQSQQLKdselKSTELQEKVTELESLLEEtqaicrdRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESW 478
Cdd:PTZ00121 1688 KKAAEALK----KEAEEAKKAEELKKKEAE-------EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 966915605 479 QKqydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRD 528
Cdd:PTZ00121 1757 KK----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
301-563 |
1.58e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 301 RAQFAQKTEALSR--EKIDLEKKLSASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQ 374
Cdd:PTZ00121 1517 KAEEAKKADEAKKaeEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 375 -----NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREAE 449
Cdd:PTZ00121 1597 vmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 450 FSSAGHSLQDKQSVEETSGEGPEVEMESwQKQYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEGTSQALRE 522
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKaeeenkiKAEEAKKEAEEDKKKAEEAKK 1751
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 966915605 523 EAQRRDSALQQLRTAVK---ELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKkaeEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-561 |
2.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 330 QLIRESLKVALQKHSEE-VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQlkds 408
Cdd:COG4717 41 AFIRAMLLERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 409 ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssaghslqdkqsveetsgegpevemESWQKQYDSLQKI 488
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------------------------RELEEELEELEAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915605 489 VEKQQQKMDQLRSQV-QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSvQNQDLIEKNLTLQEHLRQ 561
Cdd:COG4717 172 LAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-446 |
2.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRENTFLRAQFAQKTEALSREKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKK 367
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLELLEAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 368 CQKESEQNREKQQRIETLERYLADL--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRET 438
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*...
gi 966915605 439 QLESLRQR 446
Cdd:COG4913 427 EIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
290-523 |
2.66e-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: 47.32 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 290 LQELQRENtflrAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEERVKG----RDKHINNLK 365
Cdd:TIGR04523 372 IEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKEtiikNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 366 KKCQ------KESEQNREKQ-QRIETLERYLADLPTLEDHQKQSQQLKDSELKS-----TELQEKVTELE---SLLEETQ 430
Cdd:TIGR04523 447 NQDSvkeliiKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQKELKSKEKELKKlneekKELEEKVKDLTkkiSSLKEKI 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 431 AICRDRETQLES-LRQREAEFSSAGHSLqdKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE 509
Cdd:TIGR04523 527 EKLESEKKEKESkISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
250
....*....|....
gi 966915605 510 VAQEEGTSQALREE 523
Cdd:TIGR04523 605 IEEKEKKISSLEKE 618
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-528 |
3.78e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 290 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCq 369
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 370 keSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAE 449
Cdd:pfam01576 422 --SESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915605 450 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeEGTSQALREEAQRRD 528
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL---EALTQQLEEKAAAYD 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-540 |
3.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNL 364
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--ADEAkkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 365 KKKCQKESEQNREKQQRIETLERylADLPTLEDHQKQSQQLKDSEL-KSTELQEKVTELESLLEETQAICRDRETQLESL 443
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 444 RQ----REAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKqydslqKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQA 519
Cdd:PTZ00121 1647 KKaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
250 260
....*....|....*....|.
gi 966915605 520 LREEAQRRDSALQQLRTAVKE 540
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE 1741
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
291-650 |
4.79e-05 |
|
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: 46.89 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 291 QELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKH---SEEVKKQEERVKgRDKHINNLKKK 367
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLK-KQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 368 CQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlesLRQRE 447
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-----------HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 448 AEFSSAGHSLQDKQSVEETSGEGPEVEMeSWQKQYD---SLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEA 524
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 525 QRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVCSI---VTQRA 601
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavVLARL 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 966915605 602 QGHDPNLSLLLGIHSAQHPE-TQLDLQKPDV--IKRKLEEVQQLRRDIEDLR 650
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPArQDIDNPGPLTrrMQRGEQTYAQLETSEEDVY 548
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-660 |
6.42e-05 |
|
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: 45.91 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 472 EVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELsvqNQDLIEK 551
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 552 NLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDV 631
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*....
gi 966915605 632 IKRKLEEVQQLRRDIEDLRTTMSDRYAQD 660
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
376-586 |
8.48e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 376 REKQQRIETLERYLADLPtlEDHQKQSQQLKDSELKSTELQEKVTELESLLEET-QAICRDRETQLESLRQREAEFSSAG 454
Cdd:PRK04863 840 RQLNRRRVELERALADHE--SQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRFVQQHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 455 HSLQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ------------SLEQEVAQEEGTSQALRE 522
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedaaeMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915605 523 EAQRRDSALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQAQPGSPPSPDTAQLAL-----ELYQELASC 586
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASlkssydaKRQMLQELKQELQDLGVPADSGAEERArarrdELHARLSAN 1072
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
291-518 |
1.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 291 QELQRENTFLRAQFAQKT-EALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhseevkKQEERVKGRDKHINNLKKKCQ 369
Cdd:COG3206 159 EAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEAALEEFRQKNGLV---------DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 370 KESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKD------------SELKST---------ELQEKVTELESLL-E 427
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaeleaelAELSARytpnhpdviALRAQIAALRAQLqQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 428 ETQAICRDRETQLESLRQREAEFSsaghslQDKQSVEETSGEGPEVemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 507
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQ------AQLAQLEARLAELPEL-----EAELRRLEREVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 966915605 508 QEVAQEEGTSQ 518
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
207-640 |
1.27e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 207 QLQNGAICHHPAAFAPSlpILEPAQWISILNSNehLLKEKELLidKQRKHISQLEQKVRESELQVHSALLgrpapfgDVC 286
Cdd:pfam05483 52 QVANSGDCHYQEGLKDS--DFENSEGLSRLYSK--LYKEAEKI--KKWKVSIEAELKQKENKLQENRKII-------EAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 287 LLRLQELQRENTflraQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE-EVKKQEERVKGRDKHINNLK 365
Cdd:pfam05483 119 RKAIQELQFENE----KVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKyEYEREETRQVYMDLNNNIEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 366 KKCQKESEQNREKQQRIETLERYLADLPTLED-HQKQSQQLKDSE-------LKSTELQEKVTELESLLEETqaicRDRE 437
Cdd:pfam05483 195 MILAFEELRVQAENARLEMHFKLKEDHEKIQHlEEEYKKEINDKEkqvslllIQITEKENKMKDLTFLLEES----RDKA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 438 TQL--------ESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE 509
Cdd:pfam05483 271 NQLeektklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 510 VAQEEGTS----QALREEAQRRDSALQQLRTAVKELSVQNQDLIE-------KNLTLQEhLRQAQPGSPPSPDTAQLALE 578
Cdd:pfam05483 351 VTEFEATTcsleELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEE-LKKILAEDEKLLDEKKQFEK 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 579 LYQELASCLQDLQAVcsIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQ 640
Cdd:pfam05483 430 IAEELKGKEQELIFL--LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
364-563 |
1.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 364 LKKKCQKESEQNREKQQRIETLerylaDLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 443
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPEL-----NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 444 RQREAefssAGHSLQDKQSVEEtsgegpevEMESWQKQYDSLqkivEKQQQKMDQLRSQVQSLEQEVAQ-EEGTSQALRE 522
Cdd:COG4717 122 EKLLQ----LLPLYQELEALEA--------ELAELPERLEEL----EERLEELRELEEELEELEAELAElQEELEELLEQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966915605 523 EAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
301-547 |
1.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 301 RAQFAQKTEALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHinnlKKKCQ--KESEQNREK 378
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKA---EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADeaKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 379 QQRIETLERYLAD-LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLlEETQAICRDRETQLESLRQREAEFSSAGHSL 457
Cdd:PTZ00121 1525 DEAKKAEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 458 QDKQSVEETSGEGPEV-------EMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSA 530
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
250
....*....|....*..
gi 966915605 531 LQQLRTAVKELSVQNQD 547
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEE 1700
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
196-540 |
2.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 196 LELIRLQMEQMQLQNGAICHHPAAFapslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 270
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHGRTAGAM-----QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 271 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 339
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 340 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 411
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 412 STELQEKVTELESLLEETQ---AICRDretqlesLRQREaEFSSAGHSLQDKQSVEETSGEGpevemeswqkqYDSLQKI 488
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASlqfAECQD-------IIQRQ-EQESVRLKLQHTLDVKELQGPG-----------YTSNSSM 859
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915605 489 VEKQQQKMDQLRSQ-----VQSLEQEVAQEEGTSQALREEAQRR-DSALQQLRTAVKE 540
Cdd:pfam15921 860 KPRLLQPASFTRTHsnvpsSQSTASFLSHHSRKTNALKEDPTRDlKQLLQELRSVINE 917
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
412-540 |
2.40e-04 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 43.76 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 412 STELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEgpEVEMESWQKQYDSLQKIVEK 491
Cdd:pfam13949 132 SPSVEEQVAKLRELLNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQE--EQLFEEELEKYDPLQNRLEQ 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 966915605 492 QQQKMDQLRSQVQSLEQEVAQEegtSQALREEAQRRDSALQQLRTAVKE 540
Cdd:pfam13949 210 NLHKQEELLKEITEANNEFLQD---KRVDSEKQRQREEALQKLENAYDK 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-539 |
2.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 368
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 369 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 448
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 449 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKIVEkQQQKMDQLRSQVqslEQEVAQEEGTSQAlrEEAQRR 527
Cdd:PTZ00121 1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAE-EKKKADEAKKKA---EEAKKADEAKKKA--EEAKKA 1459
|
250
....*....|..
gi 966915605 528 DSALQQLRTAVK 539
Cdd:PTZ00121 1460 EEAKKKAEEAKK 1471
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
390-541 |
2.79e-04 |
|
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: 43.51 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 390 ADLPTLEDHQKQSQQLKDSELKS-TELQEKVTELESLLEETQAICRDRETQLESLRQReaefssaghsLQDKqsVEETSG 468
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEaKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA----------LKDL--LTDEGG 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915605 469 EGPEVEMESWQKQYDSLQK-IVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEL 541
Cdd:cd22656 175 AIARKEIKDLQKELEKLNEeYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPAL 248
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
309-445 |
2.84e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 309 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 388
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 966915605 389 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 445
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
359-558 |
4.09e-04 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 43.10 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 359 KHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELkSTELQEKVTELESLLEETQAICRDRET 438
Cdd:cd08915 133 EKVTKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPAL-DPEVSEVVSSLRPLLNEVSELEKERER 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 439 QLESLRQREAEFSSAghslqdkQSVEETSGEGPEVEMES-WQKQ---YDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE 514
Cdd:cd08915 212 FISELEIKSRNNDIL-------PKLITEYKKNGTTEFEDlFEEHlkkFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVK 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 966915605 515 GTSqalrEEAQRRDSALQQLRTAVKELS--VQN--------QDLIEKNLTLQEH 558
Cdd:cd08915 285 NSN----DSLDPREEALQDLEASYKKYLelKENlnegskfyNDLIEKVNRLLEE 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-592 |
4.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 236 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREK 315
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 316 IDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR-------------- 381
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 382 ------------------------IETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRE 437
Cdd:COG4717 264 lggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 438 TQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESwqkqYDSLQKIVEKQQQKmDQLRSQVQSLEQEVAQEEGTS 517
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED----EEELRAALEQAEEY-QELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915605 518 QALREEAQRRD--SALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELYQELASCLQDLQA 592
Cdd:COG4717 419 EELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLE--------EDGELAELLQELEELKAELRE 487
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
299-588 |
4.56e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 299 FLRAQFAQK--TEALSREKIDLEKKLSASEVEVQLIRESLKVALqkhseEVKKQEERVKgrdKHINNLKKKCQKESEQNR 376
Cdd:PRK11281 26 FARAASNGDlpTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTL-----ALLDKIDRQK---EETEQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 377 EKQQRIETLERYLADlPTLEDHQKQSQqlkdselksTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAEFSS 452
Cdd:PRK11281 98 QAQAELEALKDDNDE-ETRETLSTLSL---------RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 453 AGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQ---QQKMDQLRSQVQSLEQevaqeegtsqalreeaQRRDs 529
Cdd:PRK11281 168 NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQndlQRKSLEGNTQLQDLLQ----------------KQRD- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915605 530 aLQQLRTAVKELSVQN-QDLI-EKNLTL-QEHLRQAQpgsppSPDTAQLALE---LYQELASCLQ 588
Cdd:PRK11281 231 -YLTARIQRLEHQLQLlQEAInSKRLTLsEKTVQEAQ-----SQDEAARIQAnplVAQELEINLQ 289
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-557 |
4.84e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 243 LKEKELLIDKQRKHISQLEQKVRESE--LQVHSALLGRPAPFGDVCLLRLQELQRENTFLRaQFAQKTEALsreKIDLEK 320
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKEraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEAL---KLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 321 KLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTL 395
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekvKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 396 EDHQKQSQQLKDSELKSTELQEKV----TELESLLEETQAICRDRETQLESLR----QREAEFSSAGHSLQDK----QSV 463
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTrntlKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 464 EETSGEGPEVEMeswqkqydSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSV 543
Cdd:pfam15921 719 EGSDGHAMKVAM--------GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330
....*....|....
gi 966915605 544 QNQDLIEKNLTLQE 557
Cdd:pfam15921 791 ELEVLRSQERRLKE 804
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-565 |
5.03e-04 |
|
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: 42.22 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 380 QRIETLERYLADLPtledhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 459
Cdd:COG1579 17 SELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 460 kqsveetsgegpevemeswQKQYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEG----TSQALREEAQRRD 528
Cdd:COG1579 88 -------------------NKEYEALQKEIESLKRRISDLEDeilelmeRIEELEEELAELEAelaeLEAELEEKKAELD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966915605 529 SALQQLRTAVKELSVQNQDLIEK----NLTLQEHLRQAQPG 565
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKippeLLALYERIRKRKNG 189
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
284-564 |
5.85e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 284 DVCLLRLQELQRENtFLRAQFAQKtealsREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE---VKKQEERVKGRDKH 360
Cdd:COG5022 745 DNIATRIQRAIRGR-YLRRRYLQA-----LKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPllsLLGSRKEYRSYLAC 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 361 INNLKKKCQKESEQN-REKQQR-------IETLERYLADLPTLEDHQKQS------QQLKDSELKSTELQEKVTELESL- 425
Cdd:COG5022 819 IIKLQKTIKREKKLReTEEVEFslkaevlIQKFGRSLKAKKRFSLLKKETiylqsaQRVELAERQLQELKIDVKSISSLk 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 426 --LEETQAICRDRETQLESLRQREAEFSSAgHSLQDKQSVEET-SGEGPEVEMESwqkqydslQKIVEKQQQKMDQLRSQ 502
Cdd:COG5022 899 lvNLELESEIIELKKSLSSDLIENLEFKTE-LIARLKKLLNNIdLEEGPSIEYVK--------LPELNKLHEVESKLKET 969
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 503 VQSLEQEVAQEEgtsqALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQP 564
Cdd:COG5022 970 SEEYEDLLKKST----ILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-563 |
8.28e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 234 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQ--ELQRENTFLRAQFAQKTEAL 311
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAELRAQLAKKEEEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 312 SREKIDLEKKLSASEVEVQLIREslkvaLQKHSEEVKKQEERVKGRDkhinnlkkkcQKESEQNREKQQRIETLERYLAD 391
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRE-----LEAQISELQEDLESERAAR----------NKAEKQRRDLGEELEALKTELED 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 392 lpTLEDHQKQSqqlkdsELKSTELQEkVTELESLLEETQaicRDRETQLESLRQREA----EFSSAGHSLQDKQSVEETS 467
Cdd:pfam01576 311 --TLDTTAAQQ------ELRSKREQE-VTELKKALEEET---RSHEAQLQEMRQKHTqaleELTEQLEQAKRNKANLEKA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 468 GEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQD 547
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
330
....*....|....*.
gi 966915605 548 LIEKNLTLQEHLRQAQ 563
Cdd:pfam01576 459 LSKDVSSLESQLQDTQ 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
255-543 |
1.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 255 KHISQLEQKVReselQVHSALLGRPAPFGDvcllRLQELQRENTFLRAQFAQ-KTE--ALSREKIDLEKKLSasEVEVQL 331
Cdd:pfam15921 317 RQLSDLESTVS----QLRSELREAKRMYED----KIEELEKQLVLANSELTEaRTErdQFSQESGNLDDQLQ--KLLADL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 332 IRESLKVALQKhsEEVKKQEERVKGRDKHINNLKKkcqkESEQNREKQQRIETLERYLADlptlEDHQKQSQQLKDSELK 411
Cdd:pfam15921 387 HKREKELSLEK--EQNKRLWDRDTGNSITIDHLRR----ELDDRNMEVQRLEALLKAMKS----ECQGQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 412 STELqEKVTELESLLEETQAICRDRETQLE----SLRQREAEFSSAGHSLQDKQ-SVEETSGE----------------- 469
Cdd:pfam15921 457 NESL-EKVSSLTAQLESTKEMLRKVVEELTakkmTLESSERTVSDLTASLQEKErAIEATNAEitklrsrvdlklqelqh 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915605 470 --GPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSV 543
Cdd:pfam15921 536 lkNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-453 |
1.05e-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: 42.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 236 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVhsALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREK 315
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEA----------ELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 316 IDLEKKLSASEVEVQLIRESLKVALQKhseeVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptL 395
Cdd:COG4942 111 RALYRLGRQPPLALLLSPEDFLDAVRR----LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL--E 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915605 396 EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSA 453
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-542 |
1.05e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQREntflRAQFAQKTEALSrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLK 365
Cdd:PRK02224 476 RVEELEAE----LEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 366 KKCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselkSTELQEKVTELESL--LEETQAICRDRETQLESL 443
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAEL-------------------NSKLAELKERIESLerIRTLLAAIADAEDEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 444 RQREAEFSSAGHSLQDKQS-----VEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 518
Cdd:PRK02224 612 REKREALAELNDERRERLAekrerKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
250 260 270
....*....|....*....|....*....|
gi 966915605 519 ALREEAQRRDS------ALQQLRTAVKELS 542
Cdd:PRK02224 692 ELEELRERREAlenrveALEALYDEAEELE 721
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
318-508 |
1.09e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 318 LEKKLSAS----EVEVQLIR-ESLKVALQKHSEEVKKQEERVKGRDKHINNlkKKCQKESEQNREKQQRIETLERYLAdl 392
Cdd:COG2433 355 VEKKVPPDvdrdEVKARVIRgLSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVE-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 393 ptledhqkqsqqlkdselkstELQEKVTELESLLEEtqaicrdRETQLESLRQREaefssaghslqdKQSVEEtsgegpE 472
Cdd:COG2433 431 ---------------------ELEAELEEKDERIER-------LERELSEARSEE------------RREIRK------D 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 966915605 473 VEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQ 508
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
357-551 |
1.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 357 RDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---------------LEDHQKQSQQLKdsELKSTELQEKVTE 421
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtalttleeaLSEKERIIERLK--EQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 422 LESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSVEETSG-------EGPEVEMESWQKQYDSLQKIVEKQQQ 494
Cdd:pfam10174 470 LESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkdsklKSLEIAVEQKKEECSKLENQLKKAHN 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915605 495 KMDQLR------SQVQSLEQEVAQEegtsqalREEAQRRDSALQQLRTAVKELSVQNQDLIEK 551
Cdd:pfam10174 546 AEEAVRtnpeinDRIRLLEQEVARY-------KEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
443-561 |
1.18e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.99 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 443 LRQREAEFssaghslqdKQSVEETSGEgPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 522
Cdd:pfam11559 46 QRDRDLEF---------RESLNETIRT-LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKE 115
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 966915605 523 EAQRRDSALQQLRTAvkelsvQNQDLIEKNL---TLQEHLRQ 561
Cdd:pfam11559 116 ELQRLKNALQQIKTQ------FAHEVKKRDReieKLKERLAQ 151
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
290-425 |
1.21e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 290 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 369
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 370 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 425
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
314-533 |
1.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 314 EKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKKKCQKESEQNREKQQRIETLERYLADLp 393
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD-ALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREELGER- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 394 tLEDHQKQSQQLKDSE--LKSTELQEKVTELESLleeTQAICRDRETqLESLRQREAEFSSAGHSLQDKQSVEETSgegp 471
Cdd:COG3883 92 -ARALYRSGGSVSYLDvlLGSESFSDFLDRLSAL---SKIADADADL-LEELKADKAELEAKKAELEAKLAELEAL---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 472 EVEMESWQKQydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQ 533
Cdd:COG3883 163 KAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-649 |
1.41e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 243 LKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRpapfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKL 322
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 323 SASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLE-------RYLADLPTL 395
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaaRLLLLLEAE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 396 EDHQKQSQQLKDSELKS---------TELQEKVTELESLLEET------QAICRD-----------------RETQLESL 443
Cdd:COG1196 501 ADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEAAlaaalqNIVVEDdevaaaaieylkaakagRATFLPLD 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 444 RQREAEFSSAGH-SLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT--SQAL 520
Cdd:COG1196 581 KIRARAALAAALaRGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggSAGG 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 521 REEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELYQELASCLQDLQAVcsIVTQR 600
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------EEERELAEAEEERLEEELEEEA--LEEQL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 966915605 601 AQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDL 649
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
332-562 |
1.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 332 IRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKcqkESEQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSEL 410
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNKIESArADLEDIKIKINELKDKHD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 411 KSTELQE-----KVTELESLLEE-TQAICRDRETQLESLRQREAEFSSAGHSLQDKqsVEETSGEGPEV---------EM 475
Cdd:PRK01156 547 KYEEIKNrykslKLEDLDSKRTSwLNALAVISLIDIETNRSRSNEIKKQLNDLESR--LQEIEIGFPDDksyidksirEI 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 476 ESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE---EAQRRDSALQQLRTAVKELSVQN---QDLI 549
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRarlESTI 704
|
250
....*....|...
gi 966915605 550 EKNLTLQEHLRQA 562
Cdd:PRK01156 705 EILRTRINELSDR 717
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
344-469 |
1.84e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 40.33 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 344 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 423
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 966915605 424 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 469
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
289-565 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 289 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKK-- 366
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 367 -----KCQK-ESEQNREKQQRIETLERYLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaicrDRETQL 440
Cdd:pfam12128 364 kaltgKHQDvTAKYNRRRSKIKEQNNRDIAGI-----KDKLAKIREARDRQLAVAEDDLQALESELRE------QLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 441 ESLRQREAEFSSAGHSLQDKQSVEETSgegPEVEMEswQKQYDSLqkiVEKQQQKMDQLRSQVQSLEQEVAQEEGtsqal 520
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATAT---PELLLQ--LENFDER---IERAREEQEAANAEVERLQSELRQARK----- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 966915605 521 reeaqRRDSA----------LQQLRTAVKELSVQnqdLIEKNLTLQEHLRQAQPG 565
Cdd:pfam12128 500 -----RRDQAsealrqasrrLEERQSALDELELQ---LFPQAGTLLHFLRKEAPD 546
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
290-526 |
2.05e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 290 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLiRESLKVALQKH-----SEEVKKQ----------EERV 354
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTE-KESSLIDLKEHasslaSSGLKKDsklksleiavEQKK 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 355 KGRDKHINNLKKKCQKESEQ--NREKQQRIETLERylaDLPTLEDHQKQSQQ--------LKDSELKSTELQEKVTELES 424
Cdd:pfam10174 531 EECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQ---EVARYKEESGKAQAeverllgiLREVENEKNDKDKKIAELES 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 425 LleeTQAICRDRETQLESLRQREAEFSSAGHSLqdkqsVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ 504
Cdd:pfam10174 608 L---TLRQMKEQNKKVANIKHGQQEMKKKGAQL-----LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
250 260
....*....|....*....|..
gi 966915605 505 SLEQEVAQEEGTSQALREEAQR 526
Cdd:pfam10174 680 STQQSLAEKDGHLTNLRAERRK 701
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
373-550 |
2.41e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 373 EQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSE-LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEF 450
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHeERVEALNELGEQLIEEGhPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 451 SSAGHSLQ---DKQSVEETSGEGPEVE-MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeegtSQALREEAQR 526
Cdd:cd00176 113 RDADDLEQwleEKEAALASEDLGKDLEsVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEG------HPDADEEIEE 186
|
170 180
....*....|....*....|....
gi 966915605 527 RDSALQQLRTAVKELSVQNQDLIE 550
Cdd:cd00176 187 KLEELNERWEELLELAEERQKKLE 210
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
387-600 |
2.69e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 387 RYLADLPTLEDHQKQSQQLKD-------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 459
Cdd:pfam07888 1 KPLDELVTLEEESHGEEGGTDmllvvprAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 460 KQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 539
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915605 540 ELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVCSIVTQR 600
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK 221
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
307-446 |
3.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 307 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 386
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915605 387 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 446
Cdd:PRK12704 117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
435-563 |
3.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 435 DRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQ--QQKMDQLRSQVQSLEQEVAQ 512
Cdd:COG4913 607 DNRAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELER 679
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 966915605 513 EEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 563
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-541 |
3.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 233 ISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKT-EAL 311
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYE--------------------EAKAKKEELERLKKRLTGLTpEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 312 SREKIDLEKKlsasevevqliRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE--KQQRIETLERYL 389
Cdd:PRK03918 390 EKELEELEKA-----------KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 390 ADLPTLEdhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRET--QLESLRQREAEFssaghslqDKQSVEETS 467
Cdd:PRK03918 459 AELKRIE------KELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKY--------NLEELEKKA 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915605 468 GEGPEVEMESwqKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQ-EEGTSQALREEAQRRDSALQQLRTAVKEL 541
Cdd:PRK03918 525 EEYEKLKEKL--IKLKGEIKSLKKELEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKEL 597
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
333-530 |
4.56e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 333 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ---KESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQL 405
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEaisQASRKLRETQNTLNQLNKQIDELNAsiakLEQQQAAQERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 406 KDSELKSTELQEKVTELESLL--EETQAICR----------DRETQLESLRQREAEFSSAGHSLQDKQSVEET------- 466
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILsgEESQRGERilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTllyeqqa 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915605 467 SGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAlREEAQRRDSA 530
Cdd:PRK11637 206 QQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKA-RAEREAREAA 268
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
395-526 |
5.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 395 LEDHQKQSQQLKdsELKSTELQEKVTELESLLEETqaiCRDRETQL----ESLRQREAEFSSAGHSLQDKqsveetsgeg 470
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKE---LRERRNELqkleKRLLQKEENLDRKLELLEKR---------- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915605 471 pEVEMESWQKQYDSLQKIVEKQQQKMDQLRS-QVQSLEqEVA---QEEGTSQAL---REEAQR 526
Cdd:PRK12704 109 -EEELEKKEKELEQKQQELEKKEEELEELIEeQLQELE-RISgltAEEAKEILLekvEEEARH 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-541 |
5.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 361 INNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELE---SLLEETQAICRDRE 437
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 438 TQLESLRQREAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVE-KQQQKMDQLRSQVQSLEQEVAQEEGT 516
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 966915605 517 SQALREEAQRRDSALQQLRTAVKEL 541
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
376-583 |
6.39e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 376 REKQQRIETLERyladlpTLEDHQKQSQQLKDselKSTELQEKVTELESLL--------EETQAICRDRETQLESLRQRE 447
Cdd:COG3096 839 AALRQRRSELER------ELAQHRAQEQQLRQ---QLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 448 AEFSSAGHSLQDKQSVEETSGEGPEvemeswqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE-----------GT 516
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPE--------QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavgllGE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 517 SQALRE---------EAQRRDsALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQ-AQPGSPPSPDTAQLAL-- 577
Cdd:COG3096 982 NSDLNEklrarleqaEEARRE-AREQLRQAQAQYSQYNQVLASlkssrdaKQQTLQELEQElEELGVQADAEAEERARir 1060
|
....*...
gi 966915605 578 --ELYQEL 583
Cdd:COG3096 1061 rdELHEEL 1068
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
309-561 |
6.52e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 309 EALSREKIDLEKKLSASEVEV-QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLER 387
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 388 yladlpTLEDHQKQSQQlKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETS 467
Cdd:TIGR00606 355 ------QADRHQEHIRA-RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 468 GEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQ-RRDSALQQLRTAVKELS 542
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSsdriLELDQELRKAERELSKaEKNSLTETLKKEVKSLQ 507
|
250
....*....|....*....
gi 966915605 543 VQNQDLIEKNLTLQEHLRQ 561
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQ 526
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-446 |
8.20e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 333 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---LEDHQKQSQQLK--- 406
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeYEALQKEIESLKrri 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 966915605 407 -DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 446
Cdd:COG1579 106 sDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
240-527 |
9.39e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.11 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 240 EHLLKEKELLidkQRKhISQLEQKVRESELQVHSALLGRpapfgdvclLRLQELQRENTFLRAQFAQKTEALSREKIDLE 319
Cdd:PLN02939 159 EKILTEKEAL---QGK-INILEMRLSETDARIKLAAQEK---------IHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 320 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKgrdkhinNLKKKCQKESEQNREkqqrietLERYLADlptledhq 399
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQ-FLKAELIEVAETEERVF-------KLEKERSLLDASLRE-------LESKFIV-------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915605 400 KQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREaefssagHSLQDKQSVEETSGEGPEVEMESWQ 479
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRAT----NQVEKAALVLDQN-------QDLRDKVDKLEASLKEANVSKFSSY 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 966915605 480 KqYDSLQ---KIVEKQQQKMDQ-LRSQVQSLEQEVAQEEGTSQALREEAQRR 527
Cdd:PLN02939 352 K-VELLQqklKLLEERLQASDHeIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
|
| |
