|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-657 |
9.72e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 381 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 460
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 461 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 540
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 541 EAEFSSAGHSLQDKQSVEetsgegpevemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 620
Cdd:COG1196 381 LEELAEELLEALRAAAEL--------------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270
....*....|....*....|....*....|....*..
gi 966915599 621 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-657 |
1.95e-13 |
|
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: 74.32 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 392 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 468
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 469 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 548
Cdd:TIGR02168 742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 549 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEK-------QQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRR 621
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270
....*....|....*....|....*....|....*.
gi 966915599 622 DSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-686 |
4.21e-13 |
|
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: 73.17 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 339 EKELLIDKQRKHISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFAQkteaLSREKIDLEKKLSa 418
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEK------------ALAELRKELEELEEELEQ----LRKELEELSRQIS- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 419 sEVEVQLIRESLKValQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQ 498
Cdd:TIGR02168 730 -ALRKDLARLEAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL--KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 499 LKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAEFSSAGHSLQDKQSVEETSgegpevemeswQK 574
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelSEDIESLAAEIEELEELIEEL-----------ES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 575 QYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEaqrrdsaLQQLRTAVKELSVQNQDLIEKNLTLQEHLR 654
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE-------LEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|..
gi 966915599 655 QAQpgsppsPDTAQLALELYQELASCLQDLQA 686
Cdd:TIGR02168 947 EEY------SLTLEEAEALENKIEDDEEEARR 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-657 |
1.12e-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: 72.02 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 454
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 455 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 520
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 521 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 600
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 966915599 601 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
266-653 |
3.57e-11 |
|
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: 66.77 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 266 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 343
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 344 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 395
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 396 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 459
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 460 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 539
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 540 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE--------------VA 605
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLS 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 966915599 606 QEEGTSQALREEAQRRDsalQQLRTAVKELSVQNQDLIEKNLTLQEHL 653
Cdd:pfam10174 447 EKERIIERLKEQRERED---RERLEELESLKKENKDLKEKVSALQPEL 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-600 |
1.19e-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: 65.46 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 337 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 411
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 412 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 485
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 486 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGP 565
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270
....*....|....*....|....*....|....*
gi 966915599 566 EVEMESWQKQYDSLqKIVEKQQQKMDQLRSQVQSL 600
Cdd:TIGR02168 495 ERLQENLEGFSEGV-KALLKNQSGLSGILGVLSEL 528
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
325-649 |
1.44e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 325 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 399
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 400 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 479
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 480 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 557
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 558 EETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELsv 637
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-- 543
|
330
....*....|..
gi 966915599 638 qNQDLIEKNLTL 649
Cdd:TIGR04523 544 -EDELNKDDFEL 554
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
399-633 |
2.00e-10 |
|
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: 63.24 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 399 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 475
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 476 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQ 555
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 556 SVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 633
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-687 |
4.22e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 282 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 361
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 362 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 441
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 442 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 521
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 522 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSgegpevemESWQKQYDSLQKIVEKQQQKMDQLR-SQVQSL 600
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL--------LEAEADYEGFLEGVKAALLLAGLRGlAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 601 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKnLTLQEHLRQAQPGSPPSPDTAQLALELYQELASC 680
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
....*..
gi 966915599 681 LQDLQAV 687
Cdd:COG1196 608 LREADAR 614
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-655 |
4.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 413
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 493
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 494 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQdkqsvEETSGEgpevEMESWQ 573
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-----EEHRKE----LLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 574 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEegtsqalrEEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHL 653
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKE--------SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
..
gi 966915599 654 RQ 655
Cdd:PRK03918 531 KE 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-745 |
5.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 470 REKQQRIETLE-------RYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQR 540
Cdd:COG1196 196 GELERQLEPLErqaekaeRYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 541 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 620
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 621 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppsPDTAQLALELYQELASCLQDLQAVCSIVTQRAQGHDP 700
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966915599 701 NLSLLLGIHSAQHPETQLDLQkpdvIKRKLEEVQQLRRDIEDLRT 745
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEE----EAELEEEEEALLELLAELLE 470
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
439-676 |
9.56e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 439 EEVKKQEERVKGRDKH--INNLKKKCQKESEQ----NREKQQRIETLERylADLpTLEDHQKQSQQLKDSELKSTELQEK 512
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHerLNGLESELAELDEEieryEEQREQARETRDE--ADE-VLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 513 VTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQ 592
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 593 LRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQnQDLIEKNLtlqEHLRQAQPGSPPSPDTAQLALE 672
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE-IEELEEEI---EELRERFGDAPVDLGNAEDFLE 415
|
....
gi 966915599 673 LYQE 676
Cdd:PRK02224 416 ELRE 419
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-654 |
1.03e-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: 61.96 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 384 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 461
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 462 CQKESEQNREKQQRIETLERYLADLPT--------LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 531
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKqlnqlkseISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 532 TQLESLRQreaefssaghSLQDKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgts 611
Cdd:TIGR04523 342 EQISQLKK----------ELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE--- 404
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 966915599 612 qalrEEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLR 654
Cdd:TIGR04523 405 ----KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-657 |
2.06e-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: 61.23 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 452 DKHINNLKKKCQKeSEQNREKQQRIETLERYLA--DLPTLEDHQKQSQ--------QLKDSELKSTELQEKVTELESLLE 521
Cdd:TIGR02168 199 ERQLKSLERQAEK-AERYKELKAELRELELALLvlRLEELREELEELQeelkeaeeELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 522 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966915599 602 QEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
347-589 |
2.16e-09 |
|
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: 59.82 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 347 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 419
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 420 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 492
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 493 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQREaefssaghslqdkqsveETSGEGPEVEME 570
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREY-----------------EEKEQTLNAELE 310
|
250
....*....|....*....
gi 966915599 571 SWQKQYDSLQKIVEKQQQK 589
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-603 |
3.17e-09 |
|
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: 60.47 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 278 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 355
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 356 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 435
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 436 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT-LEDHQKQSQQLKDSELKSTELQEKVT 514
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKeRDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 515 ELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSV-----EETSGEGP-----EVEMESWQKQYDSLQKIVE 584
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveEEIRALEPvnmlaIQEYEEVLKRLDELKEKRA 996
|
330
....*....|....*....
gi 966915599 585 KQQQKMDQLRSQVQSLEQE 603
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
466-686 |
1.19e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 466 SEQNREKQQRIETLERYLADLptledhqKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 545
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 546 SAGHSLQDKQSVEETSGEgpEVEMESwqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE-EGTSQALREEAQRRDSA 624
Cdd:COG3206 254 DALPELLQSPVIQQLRAQ--LAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAR 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 625 LQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAqpgsppspDTAQlalELYQELASCLQDLQA 686
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREV--------EVAR---ELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
432-657 |
1.60e-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: 57.47 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 432 VALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQE 511
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 512 KVTELESLLEETQAICRDRETQLESLRQREA--------EFSSAGHSLQDKQSVeetsgegpeveMESWQKQYDSLQKIV 583
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPlalllspeDFLDAVRRLQYLKYL-----------APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 584 EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-619 |
2.67e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 393 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 468
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 469 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCRDRETQLESLRQREAEfssag 548
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE----- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915599 549 hsLQDKQSVEEtsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 619
Cdd:COG4717 182 --LLEQLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
394-662 |
2.73e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 57.76 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 394 LRAQFAQKTEALSREKIDLEKKLSASEVEVQLiresLKVALQKHSEEVKKQEERVKGRDKHiNNLKKKCQKESEQNREkq 473
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMSTDALEQEI----LQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARRQ-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 474 qrIETLERYLADLPTLEDHQKQSQqLKDSELKSTELQEKVTELEslLEE-----TQAICRDR------------------ 530
Cdd:PRK10929 153 --LNEIERRLQTLGTPNTPLAQAQ-LTALQAESAALKALVDELE--LAQlsannRQELARLRselakkrsqqldaylqal 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 531 ETQLESLRQREAEfssagHSLQDKQSVEETSGEGPEVEMESWQKQYDsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT 610
Cdd:PRK10929 228 RNQLNSQRQREAE-----RALESTELLAEQSGDLPKSIVAQFKINRE-LSQALNQQAQRMDLIASQQRQAASQTLQVRQA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 611 SQALREEAQRRDSA-------------------LQQLRTAVKELSVQN---QDLIEKnltLQEHLRQAQPGSPP 662
Cdd:PRK10929 302 LNTLREQSQWLGVSnalgealraqvarlpempkPQQLDTEMAQLRVQRlryEDLLNK---QPQLRQIRQADGQP 372
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
445-652 |
3.90e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 445 EERVKGRDKHINNLKKKcqkESEQNREKQQRIETLeryladLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQ 524
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKK---NGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 525 AicrDRETQLESLrQREAEFSSAGHS----LQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQ---V 597
Cdd:PHA02562 265 A---KIKSKIEQF-QKVIKMYEKGGVcptcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEIMDEFNEQskkL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 966915599 598 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAV----KELSVQNQDLIEKNLTLQEH 652
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnaEELAKLQDELDKIVKTKSEL 398
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
383-651 |
6.25e-08 |
|
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: 56.06 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRE-NTFLRAQFAQK------TEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhi 455
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANrqrekeKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 456 nnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvteleslLEET 523
Cdd:pfam07888 113 --LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK-------LQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 524 QAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 600
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 966915599 601 eqevaqeegtsQALREEAQrrdSALQQLRTAVKELSVQnqdLIEKNLTLQE 651
Cdd:pfam07888 264 -----------AAQRDRTQ---AELHQARLQAAQLTLQ---LADASLALRE 297
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
464-742 |
7.53e-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: 56.23 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 464 KESEQNREKQQRIETLERYLADLPT---------------------------------LEDHQKQSQQLKDSELKSTELQ 510
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSelrrienrldelsqelsdasrkigeiekeieqlEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 511 EKVTELESLLEETQAICRDRETQLESLRQREAEFSSAghslQDKQSVEETSGEGPEVEME--SWQKQYDSLQKIVEKQQQ 588
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----LSHSRIPEIQAELSKLEEEvsRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 589 KMDQLRSQVQSLEQ----------EVAQEEGTSQALREEAQRRdsaLQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQP 658
Cdd:TIGR02169 827 EKEYLEKEIQELQEqridlkeqikSIEKEIENLNGKKEELEEE---LEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 659 GsppspdTAQLALElYQELASCLQDLQAVCSIVTQRAQGHDPNLSLLLGIhsaqhPETQLDLQKpdvIKRKLEEVQQLRR 738
Cdd:TIGR02169 904 K------IEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-----PEEELSLED---VQAELQRVEEEIR 968
|
....
gi 966915599 739 DIED 742
Cdd:TIGR02169 969 ALEP 972
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
334-607 |
9.54e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQeLQRENTFLRA-----QFAQKT-EALSR 407
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMS-LQRSMSTQKAleedlQIATKTiCQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 408 EKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE-------KQQRIETLE 480
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 481 RYLADLPTLEDHQKQSQQLKDsELKSTE------LQEKVTELESLLEETQAI----------CRDRETQLESLRQREAEF 544
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAE-ELKGKEqeliflLQAREKEIHDLEIQLTAIktseehylkeVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 545 SSAGH--SLQDKQSVEETSGEGPEV-----EMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE 607
Cdd:pfam05483 491 TAHCDklLLENKELTQEASDMTLELkkhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-651 |
1.20e-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: 55.46 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 400
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 401 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL--------QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN 469
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 470 REKqqrIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGH 549
Cdd:TIGR02169 832 EKE---IQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 550 SLQDKQSVEETsgegpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE---------GTSQALREEAQR 620
Cdd:TIGR02169 900 ELERKIEELEA--------------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVEE 965
|
330 340 350
....*....|....*....|....*....|....*....
gi 966915599 621 RDSAL--------QQLRTAVKELSvqnqDLIEKNLTLQE 651
Cdd:TIGR02169 966 EIRALepvnmlaiQEYEEVLKRLD----ELKEKRAKLEE 1000
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
345-635 |
1.26e-07 |
|
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: 54.90 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 345 DKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQ 424
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 425 lireslkvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQ----SQQL 499
Cdd:pfam07888 140 --------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQrdtqVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 500 KDS----ELKSTELQEKVTELESLLEETQAIcRDR----ETQLESLRqreAEFSSAGhSLQDKQSVE---------ETSG 562
Cdd:pfam07888 212 QDTittlTQKLTTAHRKEAENEALLEELRSL-QERlnasERKVEGLG---EELSSMA-AQRDRTQAElhqarlqaaQLTL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 563 EGPEVEME------SWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE-AQRRDSALQQLRTAVKEL 635
Cdd:pfam07888 287 QLADASLAlregraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVElGREKDCNRVQLSESRREL 366
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
400-644 |
1.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 400 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 479
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 480 ERYLADLPTLEDHQKQSQQLK----DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSsaghSLQDKQ 555
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 556 SVEETSGEGPE------VEMESWQKQYDSLQkiVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 629
Cdd:PRK03918 355 EELEERHELYEeakakkEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
250
....*....|....*
gi 966915599 630 TAVKELSVQNQDLIE 644
Cdd:PRK03918 433 KAKGKCPVCGRELTE 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
401-657 |
2.20e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 401 KTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE------VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQ 474
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 475 RIETLERyladlpTLEDHQKQSQQLKDSELK-STELQEKVTELES---LLEETQAICRDRETQLESLR-QREAEFSSAGH 549
Cdd:TIGR04523 240 EINEKTT------EISNTQTQLNQLKDEQNKiKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNnQKEQDWNKELK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 550 SlqdkqsveetsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 629
Cdd:TIGR04523 314 S-----------------ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260
....*....|....*....|....*...
gi 966915599 630 TAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQE 404
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-753 |
2.22e-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: 54.69 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 439 EEVKKQEERVKGRDKHINNLKKKCQKESEQN---REKQQRIETLERYLAdLPTLEDHQKQSQQLkDSELksTELQEKVTE 515
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEGYEL-LKEKEALERQKEAI-ERQL--ASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 516 LESLLEETQAICRDRETQLESLRQREAEFSSaGHSLQDKQSVEETSGEGPEVE--MESWQKQYDSLQKIVEKQQQKMDQL 593
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLRVKEKIGELEAEIASLErsIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 594 RSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALEL 673
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 674 YQELASCLQDL-QAVCSIVTQRAQGHDPNLSLLLGIHSAqhpETQLDLQKPDVIK--RKLEEVQQLRRDIEDLRTTMSDR 750
Cdd:TIGR02169 415 LQRLSEELADLnAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADLSKyeQELYDLKEEYDRVEKELSKLQRE 491
|
...
gi 966915599 751 YAQ 753
Cdd:TIGR02169 492 LAE 494
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
400-757 |
2.90e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 400 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 479
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 480 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 543
Cdd:PRK02224 320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 544 FSSAGHSLQD----KQSVEETSGE--GPEVEMESWQKqydSLQKIVEKQQQ---------------------KMDQLRSQ 596
Cdd:PRK02224 400 FGDAPVDLGNaedfLEELREERDElrEREAELEATLR---TARERVEEAEAlleagkcpecgqpvegsphveTIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 597 VQSLEQEVAQeegtsqaLREEAQRRDSALQQLRTAVkELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQE 676
Cdd:PRK02224 477 VEELEAELED-------LEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 677 LASCLQDlqavcsivtQRAQGhdpnlslllgihSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDR--YAQD 754
Cdd:PRK02224 549 LEAEAEE---------KREAA------------AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIadAEDE 607
|
...
gi 966915599 755 MGE 757
Cdd:PRK02224 608 IER 610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-657 |
3.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 470 REKQQRIETLERYLADLptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssagh 549
Cdd:COG4913 258 RELAERYAAARERLAEL----EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL----- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 550 slqdKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 629
Cdd:COG4913 329 ----EAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*...
gi 966915599 630 TAVKELSVQNQDLIEKnltLQEHLRQAQ 657
Cdd:COG4913 401 EALEEALAEAEAALRD---LRRELRELE 425
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-616 |
4.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 413
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVkgrdKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhq 493
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 494 kqSQQLKDSELKSTELQEKVTELESLLEETQAICRDretqLESLRQREAEFSSAghsLQDKQSVEETSGEGPEVEMESWQ 573
Cdd:PRK03918 320 --EEEINGIEERIKELEEKEERLEELKKKLKELEKR----LEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 966915599 574 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 616
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
401-682 |
4.39e-07 |
|
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: 53.90 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 401 KTEAlSREKIDLEK-----KLSASEVEVqLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQR 475
Cdd:TIGR01612 1499 KDEA-DKNAKAIEKnkelfEQYKKDVTE-LLNKYSALAIKNKFAKTKKDSEIII---KEIKDAHKKFILEAEKSEQKIKE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 476 IETLERYLADLPTLEDH--------QKQSQQLKDSELKSTELQEKVTELeslLEETQAIcrDRETQLESLRQREAEFSSA 547
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKsnkaaidiQLSLENFENKFLKISDIKKKINDC---LKETESI--EKKISSFSIDSQDTELKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 548 GHSLQDKQSVeetsgegpeveMESWQKQydslQKIVEKQQQKMDQLRSQVQSLEQEVAQ-----EEGTSQALREEAQRRD 622
Cdd:TIGR01612 1649 GDNLNSLQEF-----------LESLKDQ----KKNIEDKKKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANK 1713
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 623 SALQQLRTAVKEL------SVQNQDL--IEKNLTLQEHLRQAQpgsppspDTAQLALELYQELASCLQ 682
Cdd:TIGR01612 1714 EEIESIKELIEPTienlisSFNTNDLegIDPNEKLEEYNTEIG-------DIYEEFIELYNIIAGCLE 1774
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-754 |
4.91e-07 |
|
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: 53.51 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 382 LRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 461
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL--ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 462 -------CQKESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQLKD-----SELKSTELQEKVTELESLLEETQA 525
Cdd:TIGR00606 676 nqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDklksTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNKLQK 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 526 ICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEgpeveMESWQKQYDSLQKIVEKQQQKMD--QLRSQVQSLEQE 603
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-----MERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQE 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 604 VAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspDTAQLALELYQELASCLQD 683
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-------QFEEQLVELSTEVQSLIRE 903
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915599 684 LQAVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDRYAQD 754
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ 974
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
334-636 |
6.47e-07 |
|
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: 52.82 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 412
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 413 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 492
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 493 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 568
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915599 569 MESWQK---QYDSLQKIVEKQQQkmDQLRSQVQSLEQEVAQEEGTSQalrEEAQRRDSALQQLRTAVKELS 636
Cdd:pfam17380 501 LEERKQamiEEERKRKLLEKEME--ERQKAIYEEERRREAEEERRKQ---QEMEERRRIQEQMRKATEERS 566
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-676 |
7.46e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 395 RAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVA--LQKHSEEVKKQEERVKGRD--KHINNLKKKCQkES 466
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK--AEEKkkadEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAE-EA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 467 EQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE-------LKSTELQEKVTELESLLEETQAicrDRETQLESLRQ 539
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkadeAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 540 REA--EFSSAGHSLQDKQSVEETSGEGPEVE---MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAL 614
Cdd:PTZ00121 1560 AEEkkKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 615 REEAQRRDSAlQQLRTAVKELSVQNQDLIEKNltlQEHLRQAQPGSPPSPDTAQLALELYQE 676
Cdd:PTZ00121 1640 KKEAEEKKKA-EELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-645 |
7.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 396 AQFAQKTEALSREKIDLEKKLSASEV---------EVQLIRESLKV----ALQKHSEEVKKQEERVKGRDKHINNLKKKC 462
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 463 QKESEQNREK---QQRIETLERYLADLptledhQKQSQQLKDSELKstELQEKVTELESLLE---ETQAICRDRETQLES 536
Cdd:PRK03918 549 EKLEELKKKLaelEKKLDELEEELAEL------LKELEELGFESVE--ELEERLKELEPFYNeylELKDAEKELEREEKE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 537 LRQREAEFSSAGHSLQD-KQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:PRK03918 621 LKKLEEELDKAFEELAEtEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
250 260 270
....*....|....*....|....*....|...
gi 966915599 616 EEAQRRDSA---LQQLRTAVKELsvqnQDLIEK 645
Cdd:PRK03918 701 EELEEREKAkkeLEKLEKALERV----EELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
426-655 |
1.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 426 IRESLKVALQKHSEEVKKQEERVKGRdKHINNLK--KKCQKESEQNREKQQRIETLERYLADLptledhqkqSQQLKDSE 503
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGR-KPELNLKelKELEEELKEAEEKEEEYAELQEELEEL---------EEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 504 LKSTELQEKVTELESLLEetqaiCRDRETQLESLRQREAEFSSAGHSLQDKQSveetsgegpevEMESWQKQYDSLQKIV 583
Cdd:COG4717 109 AELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLE-----------ELRELEEELEELEAEL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915599 584 EKQQQKMDQLRSQV-QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSvQNQDLIEKNLTLQEHLRQ 655
Cdd:COG4717 173 AELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEER 244
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
381-629 |
1.65e-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: 51.88 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 381 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhinnlk 459
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTAR-------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 460 kkcqKESEQNREKQ---QRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQ-EKVTELESLLEETQAICRDRETQLE 535
Cdd:COG3096 499 ----ELLRRYRSQQalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 536 SLRQREAEFSSAGHSLQDKQsvEETSGEGPEvemesWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARI--KELAARAPA-----WLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERD 647
|
250
....*....|....
gi 966915599 616 EEAQRRDSALQQLR 629
Cdd:COG3096 648 ELAARKQALESQIE 661
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-617 |
1.78e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 384 LQELQRENtflrAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEERVKG----RDKHINNL- 458
Cdd:TIGR04523 372 IEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKEtiikNNSEIKDLt 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 459 -----KKKCQKESEQNREKQ-QRIETLER-YLADLPTLEDHQKQSQQlKDSELKS-----TELQEKVTELE---SLLEET 523
Cdd:TIGR04523 447 nqdsvKELIIKNLDNTRESLeTQLKVLSRsINKIKQNLEQKQKELKS-KEKELKKlneekKELEEKVKDLTkkiSSLKEK 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 524 QAICRDRETQLES-LRQREAEFSSAGHSLqdKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQ 602
Cdd:TIGR04523 526 IEKLESEKKEKESkISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
250
....*....|....*
gi 966915599 603 EVAQEEGTSQALREE 617
Cdd:TIGR04523 604 EIEEKEKKISSLEKE 618
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-744 |
3.13e-06 |
|
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: 50.74 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 385 QELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKH---SEEVKKQEERVKgRDKHINNLKKK 461
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLK-KQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 462 CQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlesLRQRE 541
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-----------HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 542 AEFSSAGHSLQDKQSVEETSGEGPEVEMeSWQKQYD---SLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEA 618
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 619 QRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVCSI---VTQRA 695
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavVLARL 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 966915599 696 QGHDPNLSLLLGIHSAQHPE-TQLDLQKPDV--IKRKLEEVQQLRRDIEDLR 744
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPArQDIDNPGPLTrrMQRGEQTYAQLETSEEDVY 548
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-656 |
3.46e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 501 DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssaghslqdkQSVEETSGEgpEVEMESWQKQYDSLQ 580
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 581 ---KIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEK-----NLTLQEH 652
Cdd:COG4913 675 aelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEER 754
|
....
gi 966915599 653 LRQA 656
Cdd:COG4913 755 FAAA 758
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-634 |
3.55e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 460
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 461 KCQKESEQNREKQQRIETLERYLADlptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrdretQLESLRQR 540
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKAD-----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK--------KADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 541 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEvAQEEGTSQALREEAQR 620
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEE 1402
|
250
....*....|....
gi 966915599 621 RDSALQQLRTAVKE 634
Cdd:PTZ00121 1403 DKKKADELKKAAAA 1416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
334-622 |
3.70e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELlidKQRKHISQLEQKVRESElqvHSALLGRPAPfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLE 413
Cdd:PTZ00121 1549 DELKKAEEL---KKAEEKKKAEEAKKAEE---DKNMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 414 KKLSASEV-EVQLIRESLKVALQKHSEEVKKQEErVKGRDKHINNLKKKCQKESEQNREKQQRIETLEryladlptlEDH 492
Cdd:PTZ00121 1618 AKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE---------EDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 493 QKQSQQLKdselKSTELQEKVTELESLLEEtqaicrdRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESW 572
Cdd:PTZ00121 1688 KKAAEALK----KEAEEAKKAEELKKKEAE-------EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 966915599 573 QKqydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRD 622
Cdd:PTZ00121 1757 KK----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
301-734 |
4.21e-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: 50.49 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 301 QLQNGAICHHPAAFAPSlpILEPAQWISILNSNehLLKEKELLidKQRKHISQLEQKVRESELQVHSALL--GRPApfgd 378
Cdd:pfam05483 52 QVANSGDCHYQEGLKDS--DFENSEGLSRLYSK--LYKEAEKI--KKWKVSIEAELKQKENKLQENRKIIeaQRKA---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 379 vcllrLQELQRENTflraQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE-EVKKQEERVKGRDKHINN 457
Cdd:pfam05483 122 -----IQELQFENE----KVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKyEYEREETRQVYMDLNNNI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 458 LKKKCQKESEQNREKQQRIETLERYLADLPTLED-HQKQSQQLKDSE-------LKSTELQEKVTELESLLEETqaicRD 529
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHlEEEYKKEINDKEkqvslllIQITEKENKMKDLTFLLEES----RD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 530 RETQL--------ESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:pfam05483 269 KANQLeektklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 602 QEVAQEEGTS----QALREEAQRRDSALQQLRTAVKELSVQNQDLIE-------KNLTLQEhLRQAQPGSPPSPDTAQLA 670
Cdd:pfam05483 349 FVVTEFEATTcsleELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEE-LKKILAEDEKLLDEKKQF 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 671 LELYQELASCLQDLQAVcsIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQ 734
Cdd:pfam05483 428 EKIAEELKGKEQELIFL--LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-622 |
5.07e-06 |
|
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: 50.17 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 384 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCq 463
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 464 keSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAE 543
Cdd:pfam01576 422 --SESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966915599 544 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeEGTSQALREEAQRRD 622
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL---EALTQQLEEKAAAYD 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-657 |
5.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 395 RAQFAQKTEALSR--EKIDLEKKLSASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQ 468
Cdd:PTZ00121 1517 KAEEAKKADEAKKaeEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 469 -----NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREAE 543
Cdd:PTZ00121 1597 vmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 544 FSSAGHSLQDKQSVEETSGEGPEVEMESwQKQYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEGTSQALRE 616
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKaeeenkiKAEEAKKEAEEDKKKAEEAKK 1751
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 966915599 617 EAQRRDSALQQLRTAVK---ELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKkaeEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
383-540 |
8.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEALSREKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKK 461
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLELLEAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 462 CQKESEQNREKQQRIETLERYLADL--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRET 532
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*...
gi 966915599 533 QLESLRQR 540
Cdd:COG4913 427 EIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-634 |
1.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNL 458
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--ADEAkkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 459 KKKCQKESEQNREKQQRIETLERylADLPTLEDHQKQSQQLKDSEL-KSTELQEKVTELESLLEETQAICRDRETQLESL 537
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 538 RQ----REAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKqydslqKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQA 613
Cdd:PTZ00121 1647 KKaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
250 260
....*....|....*....|.
gi 966915599 614 LREEAQRRDSALQQLRTAVKE 634
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE 1741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
566-753 |
1.50e-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: 47.84 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 566 EVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELsvqNQDLIEK 645
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 646 NLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVcsivtqraqghdpnlslllgihsaqhpeTQLDLQKPDV 725
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL----------------------------APARREQAEE 154
|
170 180
....*....|....*....|....*...
gi 966915599 726 IKRKLEEVQQLRRDIEDLRTTMSDRYAQ 753
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAE 182
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
458-657 |
1.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 458 LKKKCQKESEQNREKQQRIETLerylaDLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 537
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPEL-----NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 538 RQREAefssAGHSLQDKQSVEEtsgegpevEMESWQKQYDSLqkivEKQQQKMDQLRSQVQSLEQEVAQ-EEGTSQALRE 616
Cdd:COG4717 122 EKLLQ----LLPLYQELEALEA--------ELAELPERLEEL----EERLEELRELEEELEELEAELAElQEELEELLEQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966915599 617 EAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
385-612 |
1.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 385 QELQRENTFLRAQFAQKT-EALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhseevkKQEERVKGRDKHINNLKKKCQ 463
Cdd:COG3206 159 EAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEAALEEFRQKNGLV---------DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 464 KESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKD------------SELKST---------ELQEKVTELESLL-E 521
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaeleaelAELSARytpnhpdviALRAQIAALRAQLqQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 522 ETQAICRDRETQLESLRQREAEFSsaghslQDKQSVEETSGEGPEVemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQ------AQLAQLEARLAELPEL-----EAELRRLEREVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 966915599 602 QEVAQEEGTSQ 612
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-686 |
2.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 330 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREK 409
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 410 IDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR-------------- 475
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 476 ----IETLERYLADLPTL----------------EDHQKQSQQLKD----SELKSTELQEKVTELESLLEETQAICRDRE 531
Cdd:COG4717 264 lggsLLSLILTIAGVLFLvlgllallflllarekASLGKEAEELQAlpalEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 532 TQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESwqkqYDSLQKIVEKQQQKmDQLRSQVQSLEQEVAQEEGTS 611
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED----EEELRAALEQAEEY-QELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915599 612 QALREEAQRRD--SALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELYQELASCLQDLQA 686
Cdd:COG4717 419 EELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLE--------EDGELAELLQELEELKAELRE 487
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
470-680 |
2.51e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 470 REKQQRIETLERYLADLPtlEDHQKQSQQLKDSELKSTELQEKVTELESLLEET-QAICRDRETQLESLRQREAEFSSAG 548
Cdd:PRK04863 840 RQLNRRRVELERALADHE--SQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRFVQQHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 549 HSLQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ------------SLEQEVAQEEGTSQALRE 616
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedaaeMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915599 617 EAQRRDSALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQAQPGSPPSPDTAQLAL-----ELYQELASC 680
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASlkssydaKRQMLQELKQELQDLGVPADSGAEERArarrdELHARLSAN 1072
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
290-634 |
3.87e-05 |
|
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: 47.42 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 290 LELIRLQMEQMQLQNGAicHHPAAFAPslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 364
Cdd:pfam15921 564 IEILRQQIENMTQLVGQ--HGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 365 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 433
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 434 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 505
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 506 STELQEKVTELESLLEETQ---AICRDretqlesLRQREaEFSSAGHSLQDKQSVEETSGEGpevemeswqkqYDSLQKI 582
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASlqfAECQD-------IIQRQ-EQESVRLKLQHTLDVKELQGPG-----------YTSNSSM 859
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 583 VEKQQQKMDQLRSQ-----VQSLEQEVAQEEGTSQALREEAQRR-DSALQQLRTAVKE 634
Cdd:pfam15921 860 KPRLLQPASFTRTHsnvpsSQSTASFLSHHSRKTNALKEDPTRDlKQLLQELRSVINE 917
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
474-659 |
4.71e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 474 QRIETLERYLADLPtledhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 553
Cdd:COG1579 17 SELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 554 kqsveetsgegpevemeswQKQYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEG----TSQALREEAQRRD 622
Cdd:COG1579 88 -------------------NKEYEALQKEIESLKRRISDLEDeilelmeRIEELEEELAELEAelaeLEAELEEKKAELD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 966915599 623 SALQQLRTAVKELSVQNQDLIEK----NLTLQEHLRQAQPG 659
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKippeLLALYERIRKRKNG 189
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
328-657 |
5.68e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 328 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQ--ELQRENTFLRAQFAQKTEAL 405
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAELRAQLAKKEEEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 406 SREKIDLEKKLSASEVEVQLIREslkvaLQKHSEEVKKQEERVKGRDkhinnlkkkcQKESEQNREKQQRIETLERYLAD 485
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRE-----LEAQISELQEDLESERAAR----------NKAEKQRRDLGEELEALKTELED 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 486 lpTLEDHQKQSqqlkdsELKSTELQEkVTELESLLEETQaicRDRETQLESLRQREA----EFSSAGHSLQDKQSVEETS 561
Cdd:pfam01576 311 --TLDTTAAQQ------ELRSKREQE-VTELKKALEEET---RSHEAQLQEMRQKHTqaleELTEQLEQAKRNKANLEKA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 562 GEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQD 641
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
330
....*....|....*.
gi 966915599 642 LIEKNLTLQEHLRQAQ 657
Cdd:pfam01576 459 LSKDVSSLESQLQDTQ 474
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-634 |
5.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 395 RAQFAQKTEALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHinnlKKKCQ--KESEQNREK 472
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKA---EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADeaKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 473 QQRIETLERYLAD-LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRET--QLESLRQREAEF---SS 546
Cdd:PTZ00121 1525 DEAKKAEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKlyeEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 547 AGHSLQDKQSVEETSGEGPEV-EMESWQKQYDSLQKIVEKQQQKMDQLR-----SQVQSLEQEVAQEEGTSQA--LREEA 618
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeeNKIKAAEEAKKAEEDKKKAeeAKKAE 1684
|
250
....*....|....*.
gi 966915599 619 QRRDSALQQLRTAVKE 634
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEE 1700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-633 |
9.21e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 462
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 463 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 542
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 543 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKIVEkQQQKMDQLRSQVqslEQEVAQEEGTSQAlrEEAQRR 621
Cdd:PTZ00121 1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAE-EKKKADEAKKKA---EEAKKADEAKKKA--EEAKKA 1459
|
250
....*....|..
gi 966915599 622 DSALQQLRTAVK 633
Cdd:PTZ00121 1460 EEAKKKAEEAKK 1471
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
506-634 |
1.00e-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: 44.92 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 506 STELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEgpEVEMESWQKQYDSLQKIVEK 585
Cdd:pfam13949 132 SPSVEEQVAKLRELLNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQE--EQLFEEELEKYDPLQNRLEQ 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 966915599 586 QQQKMDQLRSQVQSLEQEVAQEegtSQALREEAQRRDSALQQLRTAVKE 634
Cdd:pfam13949 210 NLHKQEELLKEITEANNEFLQD---KRVDSEKQRQREEALQKLENAYDK 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
337-704 |
1.03e-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: 45.88 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 337 LKEKELLIDKQRKHISQLEQKVRESE--LQVHSALLGRPAPFGDVCLLRLQELQRENTFLRaQFAQKTEALsreKIDLEK 414
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKEraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEAL---KLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 415 KLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTL 489
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekvKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 490 EDHQKQSQQLKDSELKSTELQEKV----TELESLLEETQAICRDRETQLESLR----QREAEFSSAGHSLQDK----QSV 557
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTrntlKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 558 EETSGEGPEVEMeswqkqydSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTA----VK 633
Cdd:pfam15921 719 EGSDGHAMKVAM--------GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEknkmAG 790
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 634 ELSV---QNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQlalelYQELASCLQDLQAVCSIVTQRAQGHDPNLSL 704
Cdd:pfam15921 791 ELEVlrsQERRLKEKVANMEVALDKASLQFAECQDIIQ-----RQEQESVRLKLQHTLDVKELQGPGYTSNSSM 859
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
349-652 |
1.24e-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: 45.03 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 349 KHISQLEQKVRESELQVHSALLGRPAPFgDVCLLRLQELQRENTFLRAQFAQKTEALsREKIDLEKKLSASEVEVQLIRE 428
Cdd:cd08915 45 ASIDDLQKPENLPDSIQHSQEIIEEGGL-DNIEQSFKELSKLRQNVEELLQECEELL-EEEAAEDDQLRAKFGTLRWRRP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 429 SLKVALQKHSEEVkkqeervkgrdkhiNNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELkSTE 508
Cdd:cd08915 123 SSDEAAKELYEKV--------------TKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPAL-DPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 509 LQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAghslqdkQSVEETSGEGPEVEMES-WQKQ---YDSLQKIVE 584
Cdd:cd08915 188 VSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDIL-------PKLITEYKKNGTTEFEDlFEEHlkkFDKDLTYVE 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 585 KQQQKMDQLRSQVQSLEQEVAQEEGTSqalrEEAQRRDSALQQLRTAVKELS--VQN--------QDLIEKNLTLQEH 652
Cdd:cd08915 261 KTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYKKYLelKENlnegskfyNDLIEKVNRLLEE 334
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
484-672 |
1.34e-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: 44.67 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 484 ADLPTLEDHQKQSQQLKDSELKS-TELQEKVTELESLLEETQAICRDRETQLESLRQReaefssaghsLQDKqsVEETSG 562
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEaKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA----------LKDL--LTDEGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 563 EGPEVEMESWQKQYDSLQK-IVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEL-SVQNQ 640
Cdd:cd22656 175 AIARKEIKDLQKELEKLNEeYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeKLQGA 254
|
170 180 190
....*....|....*....|....*....|....
gi 966915599 641 -DLIEKNL-TLQEHLRQAqPGSPPSPDTAQLALE 672
Cdd:cd22656 255 wQAIATDLdSLKDLLEDD-ISKIPAAILAKLELE 287
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-743 |
1.49e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 337 LKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRpapfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKL 416
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 417 SASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLE-------RYLADLPTL 489
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaaRLLLLLEAE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 490 EDHQKQSQQLKDSELKS---------TELQEKVTELESLLEET------QAICRD-----------------RETQLESL 537
Cdd:COG1196 501 ADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEAAlaaalqNIVVEDdevaaaaieylkaakagRATFLPLD 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 538 RQREAEFSSAGH-SLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT--SQAL 614
Cdd:COG1196 581 KIRARAALAAALaRGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggSAGG 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 615 REEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELYQELASCLQDLQAVcsIVTQR 694
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------EEERELAEAEEERLEEELEEEA--LEEQL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 966915599 695 AQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDL 743
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
467-644 |
1.54e-04 |
|
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: 43.59 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 467 EQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSE-LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEF 544
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHeERVEALNELGEQLIEEGhPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 545 SSAGHSLQ---DKQSVEETSGEGPEVE-MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeegtSQALREEAQR 620
Cdd:cd00176 113 RDADDLEQwleEKEAALASEDLGKDLEsVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEG------HPDADEEIEE 186
|
170 180
....*....|....*....|....
gi 966915599 621 RDSALQQLRTAVKELSVQNQDLIE 644
Cdd:cd00176 187 KLEELNERWEELLELAEERQKKLE 210
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
451-645 |
1.55e-04 |
|
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: 45.20 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 451 RDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---------------LEDHQKQSQQLKdsELKSTELQEKVTE 515
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtalttleeaLSEKERIIERLK--EQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 516 LESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSVEETSG-------EGPEVEMESWQKQYDSLQKIVEKQQQ 588
Cdd:pfam10174 470 LESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkdsklKSLEIAVEQKKEECSKLENQLKKAHN 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915599 589 KMDQLR------SQVQSLEQEVAQEegtsqalREEAQRRDSALQQLRTAVKELSVQNQDLIEK 645
Cdd:pfam10174 546 AEEAVRtnpeinDRIRLLEQEVARY-------KEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
393-682 |
1.62e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 393 FLRAQFAQK--TEALSREKIDLEKKLSASEVEVQLIRESLKVALqkhseEVKKQEERVKgrdKHINNLKKKCQKESEQNR 470
Cdd:PRK11281 26 FARAASNGDlpTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTL-----ALLDKIDRQK---EETEQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 471 EKQQRIETLERYLADlPTLEDHQKQSQqlkdselksTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAEFSS 546
Cdd:PRK11281 98 QAQAELEALKDDNDE-ETRETLSTLSL---------RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 547 AGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQ---QQKMDQLRSQVQSLEQevaqeegtsqalreeaQRRDs 623
Cdd:PRK11281 168 NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQndlQRKSLEGNTQLQDLLQ----------------KQRD- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915599 624 aLQQLRTAVKELSVQN-QDLI-EKNLTL-QEHLRQAQpgsppSPDTAQLALE---LYQELASCLQ 682
Cdd:PRK11281 231 -YLTARIQRLEHQLQLlQEAInSKRLTLsEKTVQEAQ-----SQDEAARIQAnplVAQELEINLQ 289
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
349-637 |
1.87e-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: 45.11 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 349 KHISQLEQKVReselQVHSALLGRPAPFGDvcllRLQELQRENTFLRAQFAQ-KTE--ALSREKIDLEKKLSasEVEVQL 425
Cdd:pfam15921 317 RQLSDLESTVS----QLRSELREAKRMYED----KIEELEKQLVLANSELTEaRTErdQFSQESGNLDDQLQ--KLLADL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 426 IRESLKVALQKhsEEVKKQEERVKGRDKHINNLKKkcqkESEQNREKQQRIETLERYLADlptlEDHQKQSQQLKDSELK 505
Cdd:pfam15921 387 HKREKELSLEK--EQNKRLWDRDTGNSITIDHLRR----ELDDRNMEVQRLEALLKAMKS----ECQGQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 506 STELqEKVTELESLLEETQAICRDRETQLE----SLRQREAEFSSAGHSLQDKQ-SVEETSGE----------------- 563
Cdd:pfam15921 457 NESL-EKVSSLTAQLESTKEMLRKVVEELTakkmTLESSERTVSDLTASLQEKErAIEATNAEitklrsrvdlklqelqh 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915599 564 --GPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSV 637
Cdd:pfam15921 536 lkNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
537-655 |
1.89e-04 |
|
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: 42.30 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 537 LRQREAEFssaghslqdKQSVEETSGEgPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 616
Cdd:pfam11559 46 QRDRDLEF---------RESLNETIRT-LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKE 115
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 966915599 617 EAQRRDSALQQLRTAvkelsvQNQDLIEKNL---TLQEHLRQ 655
Cdd:pfam11559 116 ELQRLKNALQQIKTQ------FAHEVKKRDReieKLKERLAQ 151
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
403-539 |
1.98e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 403 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 482
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 966915599 483 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 539
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-547 |
2.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 338 KEKELL--IDKQRKHISQLEQKVRESELQVhsALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKK 415
Cdd:COG4942 49 EEKALLkqLAALERRIAALARRIRALEQEL--AALEA----------ELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 416 LSASEVEVQLIRESLKVALQKhseeVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQ 495
Cdd:COG4942 117 GRQPPLALLLSPEDFLDAVRR----LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL--EEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966915599 496 SQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSA 547
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-636 |
2.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQREntflRAQFAQKTEALSrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLK 459
Cdd:PRK02224 476 RVEELEAE----LEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 460 KKCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselkSTELQEKVTELESL--LEETQAICRDRETQLESL 537
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAEL-------------------NSKLAELKERIESLerIRTLLAAIADAEDEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 538 RQREAEFSSAGHSLQDKQS-----VEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 612
Cdd:PRK02224 612 REKREALAELNDERRERLAekrerKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
250 260 270
....*....|....*....|....*....|
gi 966915599 613 ALREEAQRRDS------ALQQLRTAVKELS 636
Cdd:PRK02224 692 ELEELRERREAlenrveALEALYDEAEELE 721
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
383-617 |
2.50e-04 |
|
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: 44.43 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQElQRENtfLRAQFAQKTEALSREKIDLEKKLSASEVEVQLiRESLKVALQKH-----SEEVKKQ----------EER 447
Cdd:pfam10174 454 RLKE-QRER--EDRERLEELESLKKENKDLKEKVSALQPELTE-KESSLIDLKEHasslaSSGLKKDsklksleiavEQK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 448 VKGRDKHINNLKKKCQKESEQ--NREKQQRIETLERylaDLPTLEDHQKQSQQ--------LKDSELKSTELQEKVTELE 517
Cdd:pfam10174 530 KEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQ---EVARYKEESGKAQAeverllgiLREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 518 SLleeTQAICRDRETQLESLRQREAEFSSAGHSLqdkqsVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQV 597
Cdd:pfam10174 607 SL---TLRQMKEQNKKVANIKHGQQEMKKKGAQL-----LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARL 678
|
250 260
....*....|....*....|
gi 966915599 598 QSLEQEVAQEEGTSQALREE 617
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAE 698
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-627 |
2.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 408 EKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKKKCQKESEQNREKQQRIETLERYLADLp 487
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD-ALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREELGER- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 488 tLEDHQKQSQQLKDSE--LKSTELQEKVTELESLleeTQAICRDRETqLESLRQREAEFSSAGHSLQDKQSVEETSgegp 565
Cdd:COG3883 92 -ARALYRSGGSVSYLDvlLGSESFSDFLDRLSAL---SKIADADADL-LEELKADKAELEAKKAELEAKLAELEAL---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 566 EVEMESWQKQydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQ 627
Cdd:COG3883 163 KAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-635 |
3.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 327 ISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKT-EAL 405
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYE--------------------EAKAKKEELERLKKRLTGLTpEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 406 SREKIDLEKKlsasevevqliRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE--KQQRIETLERYL 483
Cdd:PRK03918 390 EKELEELEKA-----------KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 484 ADLPTLEdhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRET--QLESLRQREAEFssaghslqDKQSVEETS 561
Cdd:PRK03918 459 AELKRIE------KELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKY--------NLEELEKKA 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966915599 562 GEGPEVEMESwqKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQ-EEGTSQALREEAQRRDSALQQLRTAVKEL 635
Cdd:PRK03918 525 EEYEKLKEKL--IKLKGEIKSLKKELEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKEL 597
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
378-658 |
3.34e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 378 DVCLLRLQELQRENtFLRAQFAQKtealsREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE---VKKQEERVKGRDKH 454
Cdd:COG5022 745 DNIATRIQRAIRGR-YLRRRYLQA-----LKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPllsLLGSRKEYRSYLAC 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 455 INNLKKKCQKESEQN-REKQQR-------IETLERYLADLPTLEDHQKQS------QQLKDSELKSTELQEKVTELESL- 519
Cdd:COG5022 819 IIKLQKTIKREKKLReTEEVEFslkaevlIQKFGRSLKAKKRFSLLKKETiylqsaQRVELAERQLQELKIDVKSISSLk 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 520 --LEETQAICRDRETQLESLRQREAEFSSAgHSLQDKQSVEET-SGEGPEVEMESwqkqydslQKIVEKQQQKMDQLRSQ 596
Cdd:COG5022 899 lvNLELESEIIELKKSLSSDLIENLEFKTE-LIARLKKLLNNIdLEEGPSIEYVK--------LPELNKLHEVESKLKET 969
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 597 VQSLEQEVAQEEgtsqALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQP 658
Cdd:COG5022 970 SEEYEDLLKKST----ILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-659 |
3.36e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKK-- 460
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 461 -----KCQK-ESEQNREKQQRIETLERYLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaicrDRETQL 534
Cdd:pfam12128 364 kaltgKHQDvTAKYNRRRSKIKEQNNRDIAGI-----KDKLAKIREARDRQLAVAEDDLQALESELRE------QLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 535 ESLRQREAEFSSAGHSLQDKQSVEETSgegPEVEMEswQKQYDSLqkiVEKQQQKMDQLRSQVQSLEQEVAQEEGtsqal 614
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATAT---PELLLQ--LENFDER---IERAREEQEAANAEVERLQSELRQARK----- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 966915599 615 reeaqRRDSA----------LQQLRTAVKELSVQnqdLIEKNLTLQEHLRQAQPG 659
Cdd:pfam12128 500 -----RRDQAsealrqasrrLEERQSALDELELQ---LFPQAGTLLHFLRKEAPD 546
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
384-519 |
4.75e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 384 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 463
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 464 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 519
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
412-602 |
6.25e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 412 LEKKLSAS----EVEVQLIR-ESLKVALQKHSEEVKKQEERVKGRDKHINNlkKKCQKESEQNREKQQRIETLERYLAdl 486
Cdd:COG2433 355 VEKKVPPDvdrdEVKARVIRgLSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVE-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 487 ptledhqkqsqqlkdselkstELQEKVTELESLLEEtqaicrdRETQLESLRQREaefssaghslqdKQSVEEtsgegpE 566
Cdd:COG2433 431 ---------------------ELEAELEEKDERIER-------LERELSEARSEE------------RREIRK------D 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 966915599 567 VEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQ 602
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
481-694 |
7.09e-04 |
|
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: 42.96 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 481 RYLADLPTLEDHQKQSQQLKD-------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 553
Cdd:pfam07888 1 KPLDELVTLEEESHGEEGGTDmllvvprAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 554 KQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 633
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915599 634 ELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQELASCLQDLQAVCSIVTQR 694
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK 221
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
426-656 |
7.84e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 426 IRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKcqkESEQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSEL 504
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNKIESArADLEDIKIKINELKDKHD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 505 KSTELQE-----KVTELESLLEE-TQAICRDRETQLESLRQREAEFSSAGHSLQDKqsVEETSGEGPEV---------EM 569
Cdd:PRK01156 547 KYEEIKNrykslKLEDLDSKRTSwLNALAVISLIDIETNRSRSNEIKKQLNDLESR--LQEIEIGFPDDksyidksirEI 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 570 ESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE---EAQRRDSALQQLRTAVKELSVQN---QDLI 643
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRarlESTI 704
|
250
....*....|...
gi 966915599 644 EKNLTLQEHLRQA 656
Cdd:PRK01156 705 EILRTRINELSDR 717
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
455-651 |
8.10e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 455 INNLKKKCQKESEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKD--SELKS--TELQEKVTELESLLEETQAICRDR 530
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAE--KRDELNAQVKELREeaQELREkrDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 531 ETQLESLRQREAEFSSAGHSLQD-KQSVE------ETSGEGPEVEME------SWQKQYDSLQKIVEkQQQKMDQLRSQV 597
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKlRKEIErlewrqQTEVLSPEEEKElvekikELEKELEKAKKALE-KNEKLKELRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 966915599 598 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQE 651
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
411-592 |
8.26e-04 |
|
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: 41.66 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 411 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 486
Cdd:cd00176 18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 487 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRD---RETQLESLRQREAEFSSA 547
Cdd:cd00176 96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966915599 548 GHSLQDKQSveetsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQ 592
Cdd:cd00176 176 GHPDADEEI---------EEKLEELNERWEELLELAEERQKKLEE 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
278-655 |
8.62e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 278 EQSCELSTCRQQLELIRLQMEQmqlQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELLIdkQRKHISQLEQK 357
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEV---ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL--QREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 358 VRESELQVHSALLGRPapfgdvcllrlQELQRENTFLRAQFAQKTEALSREKIDL---------EKKLSASEVEVQLIRE 428
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQ-----------QELQQRYAELCAAAITCTAQCEKLEKIHlqesaqslkEREQQLQTKEQIHLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 429 SLKVALQKHSEEVKKQEER-VKGRDKHINN----------LKKKCQKESEQNREKQQRIETLERYL-ADLPTLEDHQKQS 496
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCpLCGSCIHPNParqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 497 QQLKDSELKSTELQEKVTE--------LESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQ---------DKQSVEE 559
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEdipnlqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlqqcsQELALKL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 560 TSGEGPEVEMeSWQKQYDSLQKIVEKQQQKMdqlrSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQN 639
Cdd:TIGR00618 646 TALHALQLTL-TQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
410
....*....|....*.
gi 966915599 640 QDLIEKNLTLQEHLRQ 655
Cdd:TIGR00618 721 NEIENASSSLGSDLAA 736
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
438-563 |
8.64e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 41.48 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 438 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 517
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 966915599 518 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 563
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
396-657 |
9.37e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 396 AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQ-EERVKGRDK---HINNL-------KKKCQK 464
Cdd:pfam00038 14 ASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQlDTLTVERARlqlELDNLrlaaedfRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 465 ESEQNREKQQRIETLERYLADLpTLE--DHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQ--------------AIC 527
Cdd:pfam00038 94 ELNLRTSAENDLVGLRKDLDEA-TLArvDLEAKIESLKEElAFLKKNHEEEVRELQAQVSDTQvnvemdaarkldltSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 528 RDRETQLESLRQReaefssaghslqDKQSVEETsgegpevemesWQKQYDSLQKIVEKQ-------QQKMDQLRSQVQSL 600
Cdd:pfam00038 173 AEIRAQYEEIAAK------------NREEAEEW-----------YQSKLEELQQAAARNgdalrsaKEEITELRRTIQSL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966915599 601 EQEVAQEEGTSQAL----REEAQRRDSALQQLRTAVKELSVQNQDLIEknlTLQEHLRQAQ 657
Cdd:pfam00038 230 EIELQSLKKQKASLerqlAETEERYELQLADYQELISELEAELQETRQ---EMARQLREYQ 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
529-678 |
1.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 529 DRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQ--QQKMDQLRSQVQSLEQEVAQ 606
Cdd:COG4913 607 DNRAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 607 EEGTS---QALREEAQRRDSALQQLRTAVKELSVQNQDLiEKNLT-LQEHLRQAQP-----GSPPSPDTAQLALELYQEL 677
Cdd:COG4913 680 LDASSddlAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEqAEEELDELQDrleaaEDLARLELRALLEERFAAA 758
|
.
gi 966915599 678 A 678
Cdd:COG4913 759 L 759
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
400-649 |
1.20e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 400 QKTEALSREKIDLEKKLSASEVEVQLIRESLKValqkhseevkkQEERVKGRDKHINNLKKKCQKESEQNrekqQRIETL 479
Cdd:pfam05557 111 NELSELRRQIQRAELELQSTNSELEELQERLDL-----------LKAKASEAEQLRQNLEKQQSSLAEAE----QRIKEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 480 ERYLAdlptledhqkqsQQLKDSEL--KSTELQEKVTELESLLE----------ETQAICRDRETQLESLRQREAEFSSA 547
Cdd:pfam05557 176 EFEIQ------------SQEQDSEIvkNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRKLEREEKY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 548 ghslQDKQSVEETSGEGPEVEMESWQKQY----------DSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:pfam05557 244 ----REEAATLELEKEKLEQELQSWVKLAqdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
250 260 270
....*....|....*....|....*....|..
gi 966915599 618 AQRRDSALQQLRTAVKELSVQNQDLIEKNLTL 649
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLL 351
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
470-677 |
1.33e-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: 42.25 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 470 REKQQRIETLERyladlpTLEDHQKQSQQLKDselKSTELQEKVTELESLL--------EETQAICRDRETQLESLRQRE 541
Cdd:COG3096 839 AALRQRRSELER------ELAQHRAQEQQLRQ---QLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 542 AEFSSAGHSLQDKQSVEETSGEGPEvemeswqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE-----------GT 610
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPE--------QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavgllGE 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 611 SQALRE---------EAQRRDsALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQ-AQPGSPPSPDTAQLAL-- 671
Cdd:COG3096 982 NSDLNEklrarleqaEEARRE-AREQLRQAQAQYSQYNQVLASlkssrdaKQQTLQELEQElEELGVQADAEAEERARir 1060
|
....*...
gi 966915599 672 --ELYQEL 677
Cdd:COG3096 1061 rdELHEEL 1068
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
427-624 |
1.49e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 427 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ---KESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQL 499
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEaisQASRKLRETQNTLNQLNKQIDELNAsiakLEQQQAAQERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 500 KDSELKSTELQEKVTELESLL--EETQAICR----------DRETQLESLRQREAEFSSAGHSLQDKQSVEET------- 560
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILsgEESQRGERilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTllyeqqa 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 561 SGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAlREEAQRRDSA 624
Cdd:PRK11637 206 QQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKA-RAEREAREAA 268
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-675 |
1.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 381 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 457
Cdd:COG4372 37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 458 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicRDRETQLESL 537
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 538 RqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKmDQLRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:COG4372 189 L-KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL-DALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 618 AQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELYQ 675
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
288-655 |
1.73e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 288 QQLELIRLQMEQMQLQNGAICHHPAAfAPSLPILEPAQWISILNSNEHLLKEKELLIDKQRKHIS----------QLEQK 357
Cdd:PRK10246 251 RLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEevntrlqstmALRAR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 358 VRESELQVHSALLgrpapfgdvcllrlQELQRENTFL----------------RAQFAQKT------EALSREKIDLEKK 415
Cdd:PRK10246 330 IRHHAAKQSAELQ--------------AQQQSLNTWLaehdrfrqwnnelagwRAQFSQQTsdreqlRQWQQQLTHAEQK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 416 LSA-SEVEVQLIRESLKVALQKHSEEvkkqeervkgrdkhiNNLKKKCQKESEQNREKQQRIETLERYLADLPTleDHQK 494
Cdd:PRK10246 396 LNAlPAITLTLTADEVAAALAQHAEQ---------------RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQ--EQTQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 495 QSQQLKDSELKSTELQEKVTELESLLEETQAIcrdreTQLESLRQReaefssaghsLQDKQSVEET-SGEGPEV------ 567
Cdd:PRK10246 459 RNAALNEMRQRYKEKTQQLADVKTICEQEARI-----KDLEAQRAQ----------LQAGQPCPLCgSTSHPAVeayqal 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 568 EMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLrTAVKELSVQNQDLIEKNL 647
Cdd:PRK10246 524 EPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAV-CASLNITLQPQDDIQPWL 602
|
....*...
gi 966915599 648 TLQEHLRQ 655
Cdd:PRK10246 603 DAQEEHER 610
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
399-655 |
1.77e-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: 41.96 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 399 AQKTEALSREKidLEKKLSASEVEV-QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIE 477
Cdd:TIGR00606 273 ALKSRKKQMEK--DNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 478 TLERyladlpTLEDHQKQSQQlKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSV 557
Cdd:TIGR00606 351 RLQL------QADRHQEHIRA-RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 558 EETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQ-RRDSALQQLRTAV 632
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSsdriLELDQELRKAERELSKaEKNSLTETLKKEV 503
|
250 260
....*....|....*....|...
gi 966915599 633 KELSVQNQDLIEKNLTLQEHLRQ 655
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQ 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
401-540 |
1.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 401 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 480
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 481 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 540
Cdd:PRK12704 117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
427-540 |
2.23e-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: 40.29 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 427 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---LEDHQKQSQQLK--- 500
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeYEALQKEIESLKrri 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 966915599 501 -DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 540
Cdd:COG1579 106 sDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
422-647 |
2.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 422 EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLadlptledhQKQSQQLKD 501
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL---------EQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 502 SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQK 581
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966915599 582 IVEKQQQKMDQLRSQVQSLEQEVAQEEgtSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNL 647
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQA--LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
383-660 |
2.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 383 RLQELQRENTFLRAQFAQKTEAL--SREKIDLEKKLsASEVEVqLIRESLKVALQKHSEEVKKQEER---VKGRDKHINN 457
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLeqAKEGLSALNRL-LPRLNL-LADETLADRVEEIREQLDEAEEAkrfVQQHGNALAQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 458 LKK-------------KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSElKSTELQEKvteLESLLEETQ 524
Cdd:PRK04863 923 LEPivsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLA-KNSDLNEK---LRQRLEQAE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 525 AicrDRETQLESLRQREAEFSSAGHSLQDKQSveetsgegpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQS--LEQ 602
Cdd:PRK04863 999 Q---ERTRAREQLRQAQAQLAQYNQVLASLKS------------------SYDAKRQMLQELKQELQDLGVPADSgaEER 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 603 EVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDL--IEKNLTLQEHLRQAQPGS 660
Cdd:PRK04863 1058 ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLrkLERDYHEMREQVVNAKAG 1117
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
396-657 |
2.40e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 396 AQFAQKTEALSREKIDLEKKLSASEVevqlIRESLKVALQkhseevkkqeervkgrdkhinnLKKKCQKESEQNREKQQR 475
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQA----AHSQFEQAYQ----------------------LVRKIAGEVSRSEAWDVA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 476 IETLERYladlptlEDHQKQSQQLKdselkstELQEKVTELESLLEETQaicrdretQLESLRQReaefssaghsLQDKQ 555
Cdd:PRK04863 499 RELLRRL-------REQRHLAEQLQ-------QLRMRLSELEQRLRQQQ--------RAERLLAE----------FCKRL 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 556 SVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREeAQrrdSALQQLRTAVKEL 635
Cdd:PRK04863 547 GKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA-AQ---DALARLREQSGEE 622
|
250 260
....*....|....*....|..
gi 966915599 636 SVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:PRK04863 623 FEDSQDVTEYMQQLLERERELT 644
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
430-654 |
2.56e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 41.14 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 430 LKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQSQQLKDSELKste 508
Cdd:pfam03999 7 LHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDALSEENDKEQRiLQSIADLRAEAAILCLYMRNRLLHEERDPFEPK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 509 lqekvtELESLLEETQAICRDRETQLESLRQREAEFSSAGHslQDKQSVEETSGEG--------PEVE-MESWQKQYDSL 579
Cdd:pfam03999 84 ------KGMSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLE--QLQQLCEELGEEPlpllidplPSLEeLESFRKHLENL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 580 QKIVEKQQQKMDQLRSQVQSL------------EQEVAQEEGTSQAL-REEAQRRDSALQQLRTAVKELSVQNQDLIEKN 646
Cdd:pfam03999 156 RNEKERRLEEVNELKKQIKLLmeeldlvpgtdfEEDLLCESEDNFCLsRENIDKLRKLIKQLEEQKAEREEKIDDLREKI 235
|
....*...
gi 966915599 647 LTLQEHLR 654
Cdd:pfam03999 236 LELWNRLQ 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
455-635 |
2.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 455 INNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELE---SLLEETQAICRDRE 531
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 532 TQLESLRQREAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVE-KQQQKMDQLRSQVQSLEQEVAQEEGT 610
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 966915599 611 SQALREEAQRRDSALQQLRTAVKEL 635
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
493-749 |
2.75e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 493 QKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSlqdkqsveetsgegpEVEMESW 572
Cdd:pfam05557 16 NEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE---------------QAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 573 QKQY-DSLQKIVEKQQQKMDQLRSQVQSLEQEVAqeegtsqALREEAQRRDSALQQLRTAVKELSVQNqDLIEKNLTLQE 651
Cdd:pfam05557 81 KKKYlEALNKKLNEKESQLADAREVISCLKNELS-------ELRRQIQRAELELQSTNSELEELQERL-DLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 652 HLRQAQPGSPPSPDTAQLAL-ELYQELASCLQDlqavcSIVTQRAQghdpnlSLLLGIHsaqhpetqlDLQKpdvikrkl 730
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIkELEFEIQSQEQD-----SEIVKNSK------SELARIP---------ELEK-------- 204
|
250
....*....|....*....
gi 966915599 731 eEVQQLRRDIEDLRTTMSD 749
Cdd:pfam05557 205 -ELERLREHNKHLNENIEN 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
489-620 |
2.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 489 LEDHQKQSQQLKdsELKSTELQEKVTELESLLEETqaiCRDRETQL----ESLRQREAEFSSAGHSLQDKqsveetsgeg 564
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKE---LRERRNELqkleKRLLQKEENLDRKLELLEKR---------- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915599 565 pEVEMESWQKQYDSLQKIVEKQQQKMDQLRS-QVQSLEqEVA---QEEGTSQAL---REEAQR 620
Cdd:PRK12704 109 -EEELEKKEKELEQKQQELEKKEEELEELIEeQLQELE-RISgltAEEAKEILLekvEEEARH 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-654 |
3.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 439 EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAdlptledhqKQSQQLKDSELKSTELQEKVTELES 518
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE---------EVLREINEISSELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 519 LLEETQAIcrdrETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQ--KMDQLRSQ 596
Cdd:PRK03918 229 EVKELEEL----KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEE 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966915599 597 VQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLR 654
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
504-657 |
3.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 504 LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSveetsgegpevEMESWQKQYDSLQKIV 583
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-----------ELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 584 EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
395-657 |
3.70e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 395 RAQFAQKTEALSREKIDLEKKLSASEVEvqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ------KESEQ 468
Cdd:pfam03528 132 RAQWNQYRESAEREIADLRRRLSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTeaedkiKELEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 469 NR----------EKQQRIEtLERYLADLPTledhQKQSQQlKDSElkstELQEKVTELESLLEETqaicRDRETQLESLR 538
Cdd:pfam03528 207 SKmkelnhyleaEKSCRTD-LEMYVAVLNT----QKSVLQ-EDAE----KLRKELHEVCHLLEQE----RQQHNQLKHTW 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 539 QREAE--FSSAGHSLQDKQSVEE--TSGEGPEVEM--ESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgTSQ 612
Cdd:pfam03528 273 QKANDqfLESQRLLMRDMQRMESvlTSEQLRQVEEikKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVE-TSA 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 966915599 613 ALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTL-QEHLRQAQ 657
Cdd:pfam03528 352 PLSNVEEQINSAHGSVHSLDTDVVLGAGDSFNKQEDPfKEGLRRAQ 397
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
412-642 |
4.04e-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: 40.58 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 412 LEKKLSASEVEVQLIREslkvalQKHSEEVKKQEErVKGRDKHINNLKkkcQKESEQNREKQQRietlERYLADLPTLED 491
Cdd:pfam10174 441 LEEALSEKERIIERLKE------QREREDRERLEE-LESLKKENKDLK---EKVSALQPELTEK----ESSLIDLKEHAS 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 492 HQKQSQQLKDSELKSTELQ-----EKVTELESLLEETQAICRDRETQLE---SLRQREAEFSSAGHSLQDKQS-VEETSG 562
Cdd:pfam10174 507 SLASSGLKKDSKLKSLEIAveqkkEECSKLENQLKKAHNAEEAVRTNPEindRIRLLEQEVARYKEESGKAQAeVERLLG 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 563 EGPEVEMESWQKQydslQKIVEKQQQKMDQLRSQ---------VQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 633
Cdd:pfam10174 587 ILREVENEKNDKD----KKIAELESLTLRQMKEQnkkvanikhGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
....*....
gi 966915599 634 ELSVQNQDL 642
Cdd:pfam10174 663 ALEKTRQEL 671
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-522 |
4.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 327 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 401
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 402 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 458
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966915599 459 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 522
Cdd:PRK03918 693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
334-621 |
4.98e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 334 EHLLKEKELLidkQRKhISQLEQKVRESELQVHSALLGRpapfgdvclLRLQELQRENTFLRAQFAQKTEALSREKIDLE 413
Cdd:PLN02939 159 EKILTEKEAL---QGK-INILEMRLSETDARIKLAAQEK---------IHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKgrdkhinNLKKKCQKESEQNREkqqrietLERYLADlptledhq 493
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQ-FLKAELIEVAETEERVF-------KLEKERSLLDASLRE-------LESKFIV-------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 494 KQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREaefssagHSLQDKQSVEETSGEGPEVEMESWQ 573
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRAT----NQVEKAALVLDQN-------QDLRDKVDKLEASLKEANVSKFSSY 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 966915599 574 KqYDSLQ---KIVEKQQQKMDQ-LRSQVQSLEQEVAQEEGTSQALREEAQRR 621
Cdd:PLN02939 352 K-VELLQqklKLLEERLQASDHeIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
463-743 |
5.51e-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: 40.21 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 463 QKESEQNREKQQRiETLERYLADL----------PTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRET 532
Cdd:pfam12128 208 DDGVVPPKSRLNR-QQVEHWIRDIqaiagimkirPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 533 QLES-LRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKI-VEK---QQQKMDQLRSQVQSLEQEVAQE 607
Cdd:pfam12128 287 ELNQlLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETaaaDQEQLPSWQSELENLEERLKAL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 608 EGTSQALREEAQRRDSALQQlrtavkelsvQNQDLIEKNLTLQEHLRQAQPgsppspdtaqlalelyQELASCLQDLQAV 687
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKE----------QNNRDIAGIKDKLAKIREARD----------------RQLAVAEDDLQAL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 688 CSIVTQRAQGHDPNLS------------LLLGIHSAQH-PETQLDL-QKPDVIKRKLEEVQQLRRDIEDL 743
Cdd:pfam12128 421 ESELREQLEAGKLEFNeeeyrlksrlgeLKLRLNQATAtPELLLQLeNFDERIERAREEQEAANAEVERL 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-650 |
6.00e-03 |
|
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: 40.00 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 329 ILNSNEHLLKEKELLIDKQRKHISQLEQKVREselqvhsallgrpapfgdvclLRLQELQRENTFlrAQFAQKTEALSRE 408
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKN---------------------LDKNLNKDEEKI--NNSNNKIKILEQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 409 KIDLEKKLSASEVEV-QLIRESLKVALQ---------KHSEEVKKQEERVKGRDKHIN-------NLKKKCQKESEQNRE 471
Cdd:TIGR04523 84 IKDLNDKLKKNKDKInKLNSDLSKINSEikndkeqknKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 472 KQQRIETLERY----------------------------LADLPTL-EDHQKQSQQLKDSELKSTELQEKVTELESLLEE 522
Cdd:TIGR04523 164 LKKQKEELENElnllekeklniqknidkiknkllklellLSNLKKKiQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 523 TQAICRDRETQLESLRQREAEfssAGHSLQDKQS--------VEETSGEGPEVEME----SWQKQYD---SLQKIVEKQQ 587
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNK---IKKQLSEKQKeleqnnkkIKELEKQLNQLKSEisdlNNQKEQDwnkELKSELKNQE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966915599 588 QKMDQLRSQ-------VQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIE--KNLTLQ 650
Cdd:TIGR04523 321 KKLEEIQNQisqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQeiKNLESQ 392
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
386-650 |
6.20e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 39.84 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 386 ELQREntflRAQFAQKTEALSREKIDLEKKLSAS-------------------------EVEVQLIRE-----SLKVALQ 435
Cdd:pfam03148 61 ELEKE----LEELDEEIELLLEEKRRLEKALEALeeplhiaqecltlrekrqgidlvhdEVEKELLKEvelieGIQELLQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 436 KHSEEVKKQEERVKG---------RDKHIN-NLKKKCQKESEQNREKQQRiETLERYLADLPTLEDHQKQSQQLK---DS 502
Cdd:pfam03148 137 RTLEQAWEQLRLLRAarhklekdlSDKKEAlEIDEKCLSLNNTSPNISYK-PGPTRIPPNSSTPEEWEKFTQDNIeraEK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 503 EL-KSTELQEkvtELESLLEETQAICRD-RETQLESLRQREAEFSSAGHSLQD-KQSVEEtsgegpevEMESWQKQYDSL 579
Cdd:pfam03148 216 ERaASAQLRE---LIDSILEQTANDLRAqADAVNFALRKRIEETEDAKNKLEWqLKKTLQ--------EIAELEKNIEAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 580 QK-IVEK---------------QQQKMDQLRSQVQ-SLEQEVAQEEGTSQALREEAQRRDSALQQLrtaVKELSVQNQDL 642
Cdd:pfam03148 285 EKaIRDKeaplklaqtrlenrtYRPNVELCRDEAQyGLVDEVKELEETIEALKQKLAEAEASLQAL---ERTRLRLEEDI 361
|
....*...
gi 966915599 643 IEKNLTLQ 650
Cdd:pfam03148 362 AVKANSLF 369
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-651 |
6.37e-03 |
|
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: 40.00 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 411 DLEKKLSASEVEV---QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESeqnrekqQRIETLERYLADLP 487
Cdd:TIGR04523 37 QLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 488 TLEDHQKQSQQLKDSELKSTELQEK------------VTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQ--- 552
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQkni 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 553 DKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQRRDSALQQL 628
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEinekTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260
....*....|....*....|...
gi 966915599 629 RTAVKELSVQNQDLIEKNLTLQE 651
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQ 292
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
398-655 |
6.94e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 398 FAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEErvkgrdkhinnLKKKCQKESEQNREKQQRIE 477
Cdd:pfam15905 29 FRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKE-----------LEKEIRALVQERGEQDKRLQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 478 TLEryladlptlEDHQKQSQQLKDSELKSTELQEKVTELESLLEET-------QAICRDRETQlESLRQREAEFSSAGHS 550
Cdd:pfam15905 98 ALE---------EELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellKAKFSEDGTQ-KKMSSLSMELMKLRNK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 551 LQDKQSVEETSGEGPEVEMESwqkqydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRT 630
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQV-------TQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260
....*....|....*....|....*...
gi 966915599 631 AVKELSVQNQDLIEKN---LTLQEHLRQ 655
Cdd:pfam15905 241 YKLDIAQLEELLKEKNdeiESLKQSLEE 268
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
472-631 |
8.05e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 472 KQQRIETLERYLADlptledhQKQSQQLKDSELKSTELQEKVtELESLLEE--------TQAICRDRETQLESLrQREAE 543
Cdd:pfam05667 241 RKRKRTKLLKRIAE-------QLRSAALAGTEATSGASRSAQ-DLAELLSSfsgssttdTGLTKGSRFTHTEKL-QFTNE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 544 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDS 623
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
|
....*...
gi 966915599 624 ALQQLRTA 631
Cdd:pfam05667 392 TLDLLPDA 399
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
484-762 |
8.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 484 ADLPTLEDHQKQSQQLKDSelKSTELQEKVteLESLLEETQAicrdretqleslrqreaefssaghSLQDKQSVEetsge 563
Cdd:PRK11281 33 GDLPTEADVQAQLDALNKQ--KLLEAEDKL--VQQDLEQTLA------------------------LLDKIDRQK----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 564 gpevemeswqKQYDSLQKIVEKQQQKMDQLRSQVQSL---EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQ 640
Cdd:PRK11281 80 ----------EETEQLKQQLAQAPAKLRQAQAELEALkddNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 641 DLIeknlTLQEHLRQAQ---------------------PGSPPSPDTAQLALELYQELASCLQDLQavcsivTQRAQGHD 699
Cdd:PRK11281 150 QLV----SLQTQPERAQaalyansqrlqqirnllkggkVGGKALRPSQRVLLQAEQALLNAQNDLQ------RKSLEGNT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966915599 700 pNLSLLLgihsaqhpETQLDLqkpdvikrKLEEVQQLRRDIEDLRTTMSDRYAQdMGENCVTQ 762
Cdd:PRK11281 220 -QLQDLL--------QKQRDY--------LTARIQRLEHQLQLLQEAINSKRLT-LSEKTVQE 264
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-522 |
8.67e-03 |
|
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: 39.62 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 328 SILNSNEH---LLKEKELLIDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENtflraqfaqktEA 404
Cdd:TIGR04523 579 SLKKKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSLEKE-------------------LEKAKKEN-----------EK 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 405 LSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKESEQNREKqqRIETLERYlA 484
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKELSLHYKK--YITRMIRI-K 704
|
170 180 190
....*....|....*....|....*....|....*...
gi 966915599 485 DLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 522
Cdd:TIGR04523 705 DLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
466-643 |
8.72e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 39.46 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 466 SEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSelkSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 545
Cdd:pfam09730 265 SEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGA---LSEQQEKVNRLTENLEAMRGLQASKERQDALDSEKDRDSH 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 546 SAGHS----------LQDKQSVEETSGEGPEVEMESWQKQYdslQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:pfam09730 342 EDGDYyevdingpeiLECKYRVAVEEAGELREELKALKARY---NTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQ 418
|
170 180 190
....*....|....*....|....*....|..
gi 966915599 616 EEAQRRDSALQQLRTAVKE----LSVQNQDLI 643
Cdd:pfam09730 419 ERIAHLEKELGKTRKVAGEsegsLSVAQDELV 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
381-559 |
9.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 381 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLS----ASEVEVQLIRESLKVALQKHSEeVKKQEERVKGRDKHIN 456
Cdd:PRK03918 548 LEKLEELKKK----LAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 457 NLKKKCQKESEQNREKQQRIETLERYLADLPTL---EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQ 533
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170 180
....*....|....*....|....*.
gi 966915599 534 LESLRQREAEFSSAGHSLQDKQSVEE 559
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERVEELRE 728
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
424-657 |
9.47e-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: 39.11 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 424 QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKDSE 503
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ--SREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 504 LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghslqdkqsveetsgegPEVEMEswqkqydslqKIV 583
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE---------------------RETELE----------RMK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966915599 584 EKQQQKMDQLRSQvqslEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:pfam07888 157 ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
573-741 |
9.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 573 QKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVA--QEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQ 650
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 651 EHLRQAQPGSPpspdtAQLALELYQELASCLQDLQAvcsivtqraqghdpNLSLLLGIHSAQHPE-TQLDLQKPDVIKRK 729
Cdd:COG3206 247 AQLGSGPDALP-----ELLQSPVIQQLRAQLAELEA--------------ELAELSARYTPNHPDvIALRAQIAALRAQL 307
|
170
....*....|..
gi 966915599 730 LEEVQQLRRDIE 741
Cdd:COG3206 308 QQEAQRILASLE 319
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
328-621 |
9.90e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.17 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 328 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 388
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 389 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 460
Cdd:COG5185 348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 461 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELESLLEETQAicrdretQ 533
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESRVSTLKA-------T 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966915599 534 LESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYdsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQA 613
Cdd:COG5185 501 LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN--LIPASELIQASNAKTDGQAANLRTAVIDELTQYLS 578
|
....*...
gi 966915599 614 LREEAQRR 621
Cdd:COG5185 579 TIESQQAR 586
|
|
| |
