|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-657 |
4.01e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 381 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 460
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQR 540
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 541 EAEFSSAGHSLQDKQSVEetsgegpevemeswQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 620
Cdd:COG1196 381 LEELAEELLEALRAAAEL--------------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270
....*....|....*....|....*....|....*..
gi 40538794 621 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-657 |
9.39e-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: 72.01 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 368 ALLGRPAPFGDVCLLRLQELqRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkqeer 447
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-------- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 448 vkgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAIC 527
Cdd:TIGR02168 731 ---LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL--EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 528 REKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE 607
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 40538794 608 EGTSQALREEaqrrdsaLQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02168 886 EEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
266-653 |
2.05e-12 |
|
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: 70.62 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 266 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFGPSLPILEPAQWISILNSNEHLLKEKELL- 343
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 344 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 395
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 396 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVKkQEERVKGRDKHINN----LK 459
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK-QMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 460 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQ 539
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 540 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQE--------------VA 605
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLS 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 40538794 606 QEEGTSQALREEAQRRDsalQQLRTAVKELSVQNQDLIEKNLTLQEHL 653
Cdd:pfam10174 447 EKERIIERLKEQRERED---RERLEELESLKKENKDLKEKVSALQPEL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-657 |
4.03e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 454
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 455 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 520
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 521 EETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSL 600
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 601 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-686 |
1.55e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 381 LLRLQELQREntfLRAQfaqkTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKK 460
Cdd:COG1196 188 LERLEDILGE---LERQ----LEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 K-CQKESEQNREKQQRIE---TLERYLADL-PTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLE 535
Cdd:COG1196 261 ElAELEAELEELRLELEElelELEEAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 536 SLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538794 616 EEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsPPSPDTAQLALELHQELASCLQDLQA 686
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---ELLAELLEEAALLEAALAELLEELAE 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
325-645 |
1.17e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 325 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 399
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 400 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 479
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 480 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETqaICREKEIqlESLRQREAEFSSAGHSLQDKQSV 557
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETI--IKNNSEI--KDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 558 EETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEV-------AQEEGTSQALREEAQRRDSALQQLRT 630
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkiSSLKEKIEKLESEKKEKESKISDLED 545
|
330
....*....|....*.
gi 40538794 631 AVKEL-SVQNQDLIEK 645
Cdd:TIGR04523 546 ELNKDdFELKKENLEK 561
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-745 |
1.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 470 REKQQRIETLE-------RYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICREKEIQLESLRQR 540
Cdd:COG1196 196 GELERQLEPLErqaekaeRYRELKEELKELEAELLLLKLRELEAelEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 541 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 620
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 621 RDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppsPDTAQLALELHQELASCLQDLQAVCSIVTQRAQGHDP 700
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 40538794 701 NLSLLLGIHSAQHPETQLDLQkpdvIKRKLEEVQQLRRDIEDLRT 745
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEE----EAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-602 |
1.29e-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: 65.08 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 337 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 411
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 412 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 485
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 486 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDkqsveetsgegp 565
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER------------ 482
|
250 260 270
....*....|....*....|....*....|....*..
gi 40538794 566 evEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQ 602
Cdd:TIGR02168 483 --ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-652 |
3.16e-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: 63.50 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 384 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 461
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 CQKESEQNREKQQRIET-------LERYLADLPT-LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICREKE 531
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQnnkkikeLEKQLNQLKSeISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 532 IQLESLRQreaefssaghSLQDKQSVEETSGEgpevEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTS 611
Cdd:TIGR04523 342 EQISQLKK----------ELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 40538794 612 QALREEAQRRDSALQQLRTAVKELSVQNQDLIE--KNLTLQEH 652
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeiKDLTNQDS 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-687 |
8.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 282 ELSTCRQQLELIRLQMEQMQLQngaichhpaafgpslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 361
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 362 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 441
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 442 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 521
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 522 ETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSgegpevemESWQKRYDSLQKIVEKQQQKMDQLR-SQVQSL 600
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL--------LEAEADYEGFLEGVKAALLLAGLRGlAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 601 EQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQehLRQAQPGSPPSPDTAQLALELHQELASC 680
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP--LDKIRARAALAAALARGAIGAAVDLVAS 606
|
....*..
gi 40538794 681 LQDLQAV 687
Cdd:COG1196 607 DLREADA 613
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
347-589 |
1.49e-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: 60.21 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 347 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 419
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 420 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 492
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 493 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICREKEIQLESLRQREaefssaghslqdkqsveETSGEGPEVEME 570
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREY-----------------EEKEQTLNAELE 310
|
250
....*....|....*....
gi 40538794 571 SWQKRYDSLQKIVEKQQQK 589
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-655 |
2.51e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 413
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 493
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 494 KQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQdkqsvEETSGEgpevEMESWQ 573
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-----EEHRKE----LLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 574 KRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEegtsqalrEEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHL 653
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKE--------SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
..
gi 40538794 654 RQ 655
Cdd:PRK03918 531 KE 532
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-657 |
6.90e-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: 59.69 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 452 DKHINNLKKKCQKeSEQNREKQQRIETLERYLA--DLPTLEDHQKQSQ--------QLKDSELKSTELQEKVTELESLLE 521
Cdd:TIGR02168 199 ERQLKSLERQAEK-AERYKELKAELRELELALLvlRLEELREELEELQeelkeaeeELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 522 ETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 40538794 602 QEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
399-671 |
8.02e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 399 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 475
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 476 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICREKEIQLESLRQREAEfssaghsLQDKQ 555
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 556 sveetsgegpevemeswqkryDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEL 635
Cdd:COG4942 167 ---------------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 40538794 636 svqnQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLAL 671
Cdd:COG4942 226 ----EALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-603 |
8.88e-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: 59.31 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 278 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFGPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 355
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 356 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 435
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 436 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT-LEDHQKQSQQLKDSELKSTELQEKVT 514
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKeRDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 515 ELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSV-----EETSGEGP-----EVEMESWQKRYDSLQKIVE 584
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveEEIRALEPvnmlaIQEYEEVLKRLDELKEKRA 996
|
330
....*....|....*....
gi 40538794 585 KQQQKMDQLRSQVQSLEQE 603
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-651 |
1.18e-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: 58.93 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQREntflRAQFAQKTEALSREKI 410
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQE----EEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 411 DLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKH--INNLKKKCQKESEQNREKQQRIETLERYLADLpT 488
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIE-ELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRL-T 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 489 LEDHQKQS------QQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSG 562
Cdd:TIGR02169 826 LEKEYLEKeiqelqEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 563 EGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE--EGTSQALREEAQRRDSAL--------QQLRTAV 632
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRALepvnmlaiQEYEEVL 985
|
330
....*....|....*....
gi 40538794 633 KELSvqnqDLIEKNLTLQE 651
Cdd:TIGR02169 986 KRLD----ELKEKRAKLEE 1000
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
445-652 |
2.19e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 57.33 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 445 EERVKGRDKHINNLKKkcqKESEQNREKQQRIETLeryladLPTLEDHQKQSQQLKDSELKSTELQEKVTelESLLEETQ 524
Cdd:PHA02562 194 QQQIKTYNKNIEEQRK---KNGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLNLVMDIEDPS--AALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 525 AICREKEiQLESLrQREAEFSSAGHS----LQDKQSVEETSGEGPEvEMESWQKRYDSLQKIVEKQQQKMDQLRSQ---V 597
Cdd:PHA02562 263 AAAKIKS-KIEQF-QKVIKMYEKGGVcptcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEIMDEFNEQskkL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40538794 598 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAV----KELSVQNQDLIEKNLTLQEH 652
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnaEELAKLQDELDKIVKTKSEL 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
464-742 |
2.27e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 KESEQNREKQQRIETLERYLADLPT---------------------------------LEDHQKQSQQLKDSELKSTELQ 510
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSelrrienrldelsqelsdasrkigeiekeieqlEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 511 EKVTELESLLEETQAICREKEIQLESLRQREAEFSSAghslQDKQSVEETSGEGPEVEME--SWQKRYDSLQKIVEKQQQ 588
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----LSHSRIPEIQAELSKLEEEvsRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 589 KMDQLRSQVQSLEQ----------EVAQEEGTSQALREEAQRRdsaLQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQP 658
Cdd:TIGR02169 827 EKEYLEKEIQELQEqridlkeqikSIEKEIENLNGKKEELEEE---LEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 659 GSppspDTAQLALELHQELASclqDLQAVCSIVTQRAQGHDPNLSLLLGIhsaqhPETQLDLQKpdvIKRKLEEVQQLRR 738
Cdd:TIGR02169 904 KI----EELEAQIEKKRKRLS---ELKAKLEALEEELSEIEDPKGEDEEI-----PEEELSLED---VQAELQRVEEEIR 968
|
....
gi 40538794 739 DIED 742
Cdd:TIGR02169 969 ALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-753 |
2.73e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 439 EEVKKQEERVKGRDKHINNLKKKCQKESEQN---REKQQRIETLERYLAdLPTLEDHQKQSQQLkDSELksTELQEKVTE 515
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEGYEL-LKEKEALERQKEAI-ERQL--ASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 516 LESLLEETQAICREKEIQLESLRQREAEFSSaGHSLQDKQSVEETSGEGPEVE--MESWQKRYDSLQKIVEKQQQKMDQL 593
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLRVKEKIGELEAEIASLErsIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 594 RSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALEL 673
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 674 HQELASCLQDL-QAVCSIVTQRAQGHDPNLSLLLGIHSAqhpETQLDLQKPDVIK--RKLEEVQQLRRDIEDLRTTMSDR 750
Cdd:TIGR02169 415 LQRLSEELADLnAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADLSKyeQELYDLKEEYDRVEKELSKLQRE 491
|
...
gi 40538794 751 YAQ 753
Cdd:TIGR02169 492 LAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
432-657 |
3.23e-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: 56.31 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 432 VALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQE 511
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 512 KVTELESLLEETQAICREKEIQLESLRQREA--------EFSSAGHSLQDKQSVeetsgegpeveMESWQKRYDSLQKIV 583
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPlalllspeDFLDAVRRLQYLKYL-----------APARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 584 EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
400-644 |
3.74e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 400 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 479
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 480 ERYLADLPTLEDHQKQSQQLK----DSELKSTELQEKVTELESLLEETQAICRE---KEIQLESLRQREAEfssaghsLQ 552
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSefyeEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKE-------LE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 553 DKQSVEETSGEGPE------VEMESWQKRYDSLQkiVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQ 626
Cdd:PRK03918 352 KRLEELEERHELYEeakakkEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250
....*....|....*...
gi 40538794 627 QLRTAVKELSVQNQDLIE 644
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTE 447
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
394-662 |
4.47e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 394 LRAQFAQKTEALSREKIDLEKKLSASEVEVQLiresLKVALQKHSEEVKKQEERVKGRDKHiNNLKKKCQKESEQNREkq 473
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMSTDALEQEI----LQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARRQ-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 474 qrIETLERYLADLPTLEDHQKQSQqLKDSELKSTELQEKVTELEslLEETQAICREkEI--------------------- 532
Cdd:PRK10929 153 --LNEIERRLQTLGTPNTPLAQAQ-LTALQAESAALKALVDELE--LAQLSANNRQ-ELarlrselakkrsqqldaylqa 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 533 ---QLESLRQREAEfssagHSLQDKQSVEETSGEGPEVEMESWQKRYDsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEG 609
Cdd:PRK10929 227 lrnQLNSQRQREAE-----RALESTELLAEQSGDLPKSIVAQFKINRE-LSQALNQQAQRMDLIASQQRQAASQTLQVRQ 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40538794 610 TSQALREEAQRRDSA-------------------LQQLRTAVKELSVQN---QDLIEKnltLQEHLRQAQPGSPP 662
Cdd:PRK10929 301 ALNTLREQSQWLGVSnalgealraqvarlpempkPQQLDTEMAQLRVQRlryEDLLNK---QPQLRQIRQADGQP 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-619 |
6.04e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 393 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 468
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 469 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCREKEIQLESLRQREAEfssag 548
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE----- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538794 549 hsLQDKQSVEEtsgegpEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 619
Cdd:COG4717 182 --LLEQLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
401-652 |
7.40e-08 |
|
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: 56.21 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 401 KTEAlSREKIDLEK-----KLSASEVEVqLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQR 475
Cdd:TIGR01612 1499 KDEA-DKNAKAIEKnkelfEQYKKDVTE-LLNKYSALAIKNKFAKTKKDSEIII---KEIKDAHKKFILEAEKSEQKIKE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 476 IETLERYLADLPTLEDH--------QKQSQQLKDSELKSTELQEKVTELeslLEETQAIcrEKEIQLESLRQREAEFSSA 547
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKsnkaaidiQLSLENFENKFLKISDIKKKINDC---LKETESI--EKKISSFSIDSQDTELKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 548 GHSLQDKQSVeetsgegpeveMESWQKRydslQKIVEKQQQKMDQLRSQVQSLEQEVAQ-----EEGTSQALREEAQRRD 622
Cdd:TIGR01612 1649 GDNLNSLQEF-----------LESLKDQ----KKNIEDKKKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANK 1713
|
250 260 270
....*....|....*....|....*....|....*...
gi 40538794 623 SALQQLRTAVKEL------SVQNQDL--IEKNLTLQEH 652
Cdd:TIGR01612 1714 EEIESIKELIEPTienlisSFNTNDLegIDPNEKLEEY 1751
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
345-635 |
1.66e-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: 54.52 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 345 DKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQ 424
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 425 lireslkvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQ----SQQL 499
Cdd:pfam07888 140 --------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQrdtqVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 500 KDS----ELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGhSLQDKQSVE---------ETSGEGPE 566
Cdd:pfam07888 212 QDTittlTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA-AQRDRTQAElhqarlqaaQLTLQLAD 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40538794 567 VEME------SWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE-AQRRDSALQQLRTAVKEL 635
Cdd:pfam07888 291 ASLAlregraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVElGREKDCNRVQLSESRREL 366
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
401-657 |
2.11e-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: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 401 KTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE------VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQ 474
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 475 RIETLERyladlpTLEDHQKQSQQLKDSELK-STELQEKVTELEslleETQAICREKEIQLESLrqrEAEFSSAghslqD 553
Cdd:TIGR04523 240 EINEKTT------EISNTQTQLNQLKDEQNKiKKQLSEKQKELE----QNNKKIKELEKQLNQL---KSEISDL-----N 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 554 KQSVEETSGEGPEvEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 633
Cdd:TIGR04523 302 NQKEQDWNKELKS-ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260
....*....|....*....|....
gi 40538794 634 ELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQE 404
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
471-635 |
2.53e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 471 EKQQRIETLERYLADLPT----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSS 546
Cdd:PRK02224 472 EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 547 AGHSLQDK-QSVEETSGEGPEV------EMESWQKRYDSLQKIVEkQQQKMDQLRSQVQSLEQEVAQeegtsQALREEaQ 619
Cdd:PRK02224 552 EAEEKREAaAEAEEEAEEAREEvaelnsKLAELKERIESLERIRT-LLAAIADAEDEIERLREKREA-----LAELND-E 624
|
170
....*....|....*.
gi 40538794 620 RRDSaLQQLRTAVKEL 635
Cdd:PRK02224 625 RRER-LAEKRERKREL 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-616 |
2.81e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 413
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVkgrdKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhq 493
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 494 kqSQQLKDSELKSTELQEKVTELESLLEEtqaicrEKEIQ--LESLRQREAEFSSAghsLQDKQSVEETSGEGPEVEMES 571
Cdd:PRK03918 320 --EEEINGIEERIKELEEKEERLEELKKK------LKELEkrLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEK 388
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 40538794 572 WQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 616
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
383-651 |
3.56e-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: 53.36 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRE-NTFLRAQFAQK------TEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhi 455
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANrqrekeKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 456 nnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvteleslLEET 523
Cdd:pfam07888 113 --LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK-------LQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 524 QAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSL 600
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 40538794 601 eqevaqeegtsQALREEAQrrdSALQQLRTAVKELSVQnqdLIEKNLTLQE 651
Cdd:pfam07888 264 -----------AAQRDRTQ---AELHQARLQAAQLTLQ---LADASLALRE 297
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-754 |
3.80e-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: 53.90 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 382 LRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 461
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL--ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 -------CQKESEQNREKQQRIETLERYLADLPTledhqkqsqQLKDSELKSTELQEKVTELESLLEETQAICREKEIQL 534
Cdd:TIGR00606 676 nqsccpvCQRVFQTEAELQEFISDLQSKLRLAPD---------KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 535 ESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQkrydSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEG----- 609
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK----VCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdldr 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 610 TSQALREEAQRRD-------SALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELHQELASCLQ 682
Cdd:TIGR00606 823 TVQQVNQEKQEKQheldtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538794 683 DLQAVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDRYAQD 754
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ 974
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-620 |
3.96e-07 |
|
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: 52.84 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQ---KTEALSREKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHIN 456
Cdd:COG4942 28 ELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 457 NLKKKCQKESEQNREK----QQRIETLERYLADLPTLEDHQKqsQQLKDSELKSTELQEKVTELESLLEETQAICREKEI 532
Cdd:COG4942 108 ELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 533 QLESLRQREAEFSSAGHSLqdkqsveetsgegpevemeswQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 612
Cdd:COG4942 186 ERAALEALKAERQKLLARL---------------------EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 40538794 613 ALREEAQR 620
Cdd:COG4942 245 AAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-657 |
4.97e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 470 REKQQRIETLERYLADLptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFssagh 549
Cdd:COG4913 258 RELAERYAAARERLAEL----EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL----- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 550 slqdKQSVEETSGEgpevEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 629
Cdd:COG4913 329 ----EAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*...
gi 40538794 630 TAVKELSVQNQDLIEKnltLQEHLRQAQ 657
Cdd:COG4913 401 EALEEALAEAEAALRD---LRRELRELE 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
424-655 |
8.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 424 QLIRESLKVALQKHSEE-VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQlkds 502
Cdd:COG4717 41 AFIRAMLLERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 503 ELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFssaghslqdkqsveetsgegpevemESWQKRYDSLQKI 582
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------------------------RELEEELEELEAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 583 VEKQQQKMDQLRSQV-QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSvQNQDLIEKNLTLQEHLRQ 655
Cdd:COG4717 172 LAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-EELEQLENELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
474-659 |
1.02e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 474 QRIETLERYLADLPtledhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQD 553
Cdd:COG1579 17 SELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 554 KQSVEETSGEgpeveMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgtsQALREEAQRRDSALQQLRTAVK 633
Cdd:COG1579 88 NKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
170 180 190
....*....|....*....|....*....|
gi 40538794 634 ELSVQNQDLIEK----NLTLQEHLRQAQPG 659
Cdd:COG1579 160 ELEAEREELAAKippeLLALYERIRKRKNG 189
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
334-656 |
1.09e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 412
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 413 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 492
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 493 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrEKEIQLESLRQREAEfssaghslQDKQSVEETSGEGPEVEMEsw 572
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEE--------RKRKKLELEKEKRDRKRAE-- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 573 QKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeEGTSQALREEAQRRDSalqqlrtavkELSVQNQDLIEKNLTLQEH 652
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEM---EERQKAIYEEERRREA----------EEERRKQQEMEERRRIQEQ 557
|
....
gi 40538794 653 LRQA 656
Cdd:pfam17380 558 MRKA 561
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-676 |
1.16e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 395 RAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVA--LQKHSEEVKKQEERVKGRD--KHINNLKKKCQkES 466
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK--AEEKkkadEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAE-EA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 467 EQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE-------LKSTELQEKVTELESLLEETQAicrEKEIQLESLRQ 539
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkadeAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 540 REA--EFSSAGHSLQDKQSVEETSGEGPEVE---MESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAL 614
Cdd:PTZ00121 1560 AEEkkKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538794 615 REEAQRRDSAlQQLRTAVKELSVQNQDLIEKNltlQEHLRQAQPGSPPSPDTAQLALELHQE 676
Cdd:PTZ00121 1640 KKEAEEKKKA-EELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-635 |
1.42e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 396 AQFAQKTEALSREKIDLEKKLSASEV---------EVQLIRESLKV----ALQKHSEEVKKQEERVKGRDKHINNLKKKC 462
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 463 QKESEQNREK---QQRIETLERYLADLPT-------------------LEDHQKQSQQLKDSELKSTELQEKVTELESLL 520
Cdd:PRK03918 549 EKLEELKKKLaelEKKLDELEEELAELLKeleelgfesveeleerlkeLEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 521 EETQAICREKEIQLESLRQREAEfssaghsLQDKQSVEETsgEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSL 600
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEE-------LEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|....*
gi 40538794 601 EQEVAQeegtsqalREEAQRRDSALQQLRTAVKEL 635
Cdd:PRK03918 700 KEELEE--------REKAKKELEKLEKALERVEEL 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
458-670 |
1.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 458 LKKKCQKESEQNREKQQRIETLerylaDLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESL 537
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPEL-----NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 538 RQREAefssAGHSLQDKQSVEEtsgegpevEMESWQKRYDSLQ---KIVEKQQQKMDQLRSQVQSLEQEVAQE-EGTSQA 613
Cdd:COG4717 122 EKLLQ----LLPLYQELEALEA--------ELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELlEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 614 LREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLA 670
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-653 |
1.98e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQ----------FAQKTEALSREKIDLEKKLSASEVEVQLIR---ESLKVALQKHSEEVKKQEERVK 449
Cdd:PRK02224 287 RLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNeeaESLREDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 450 GRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQLKDselkstELQEKVTELESLLEETQA 525
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnAEDFLEELREERD------ELREREAELEATLRTARE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 526 ICREKEIQLEslrqrEAEFSSAGHSLQDKQSVE------------ETSGEGPEVEMESWQKRYDSLQKIVEKQQQkMDQL 593
Cdd:PRK02224 441 RVEEAEALLE-----AGKCPECGQPVEGSPHVEtieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR-IERL 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 594 RSQVQSLEQEVAQEEGT-------SQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHL 653
Cdd:PRK02224 515 EERREDLEELIAERRETieekrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-657 |
2.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 395 RAQFAQKTEALSR--EKIDLEKKLSASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQ 468
Cdd:PTZ00121 1517 KAEEAKKADEAKKaeEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 469 -----NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESL--LEETQAICREKEIQLESLRQRE 541
Cdd:PTZ00121 1597 vmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKK 1676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 542 AEfsSAGHSLQDKQSVEETSGEGPEVemeswQKRYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEGTSQAL 614
Cdd:PTZ00121 1677 AE--EAKKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELKKaeeenkiKAEEAKKEAEEDKKKAEEA 1749
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 40538794 615 REEAQRRDSALQQLRTAVK---ELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKkaeEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
381-679 |
2.33e-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: 51.49 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 381 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhinnlk 459
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTAR-------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 460 kkcqKESEQNREKQ---QRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQ-EKVTELESLLEETQAICREKEIQLE 535
Cdd:COG3096 499 ----ELLRRYRSQQalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 536 SLRQREAEFSSAGHSLQDKQsvEETSGEGPEvemesWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARI--KELAARAPA-----WLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERD 647
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 616 EEAQRRDSALQQLRtavkelsvqnqdlieknltlqehlRQAQPGSPPSPDTAQLALELHQELAS 679
Cdd:COG3096 648 ELAARKQALESQIE------------------------RLSQPGGAEDPRLLALAERLGGVLLS 687
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-617 |
3.04e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 328 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENTFLRAQFAQKTEALSR 407
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE-------------------LTNSESENSEKQRELEEKQNEIEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 408 EKIDLEKKLSASEVEVQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLP 487
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 488 TLEDH-----QKQSQQLK-----------DSELKSTELQEKVTELESLLEET-------------QAICREKEIQLESLR 538
Cdd:TIGR04523 454 LIIKNldntrESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEKkeleekvkdltkkISSLKEKIEKLESEK 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 539 -QREAEFSSAGHSLQDKQSVE-----ETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 612
Cdd:TIGR04523 534 kEKESKISDLEDELNKDDFELkkenlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
....*
gi 40538794 613 ALREE 617
Cdd:TIGR04523 614 SLEKE 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
334-622 |
3.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKELlidKQRKHISQLEQKVRESElqvHSALLGRPAPfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLE 413
Cdd:PTZ00121 1549 DELKKAEEL---KKAEEKKKAEEAKKAEE---DKNMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 414 KKLSASEV-EVQLIRESLKVALQKHSEEVKKQEErVKGRDKHINNLKKKCQKESEQNREKQQRIETLEryladlptlEDH 492
Cdd:PTZ00121 1618 AKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE---------EDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 493 QKQSQQLKdselKSTELQEKVTELESLLEEtqaicrEKEiQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESW 572
Cdd:PTZ00121 1688 KKAAEALK----KEAEEAKKAEELKKKEAE------EKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 40538794 573 QKrydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRD 622
Cdd:PTZ00121 1757 KK----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-634 |
3.37e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 460
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 KCQKESEQNREKQQRIETLERYLADlptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAiCREKEIQLESLRQR 540
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKAD-----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKK 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 541 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQvqsleqevAQEEGTSQALREEAQR 620
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--------AEEKKKADEAKKKAEE 1402
|
250
....*....|....
gi 40538794 621 RDSALQQLRTAVKE 634
Cdd:PTZ00121 1403 DKKKADELKKAAAA 1416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-657 |
4.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 395 RAQFAQKTEALSREKIDLEKK---LSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ-------- 463
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaeel 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 KESEQNREKQQRIETLERYLADLptledhqKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKE-IQLESLRQREa 542
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMAL-------RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAE- 1629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 543 EFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQ-------VQSLEQEvAQEEGTSQALR 615
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedekkaAEALKKE-AEEAKKAEELK 1708
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 40538794 616 EEAQRRDSALQQLRTAVKELSVQNQDLIEKNltlQEHLRQAQ 657
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEA---EEDKKKAE 1747
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-744 |
5.00e-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: 50.35 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 385 QELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKH---SEEVKKQEERVKgRDKHINNLKKK 461
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLK-KQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 CQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrekeiqlesLRQRE 541
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-----------HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 542 AEFSSAGHSLQDKQSVEETSGEGPEVEMeSWQKRYD---SLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEA 618
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 619 QRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALELHQELASCLQDLQAVCSI---VTQRA 695
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavVLARL 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 40538794 696 QGHDPNLSLLLGIHSAQHPE-TQLDLQKPDV--IKRKLEEVQQLRRDIEDLR 744
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPArQDIDNPGPLTrrMQRGEQTYAQLETSEEDVY 548
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
470-680 |
6.30e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 470 REKQQRIETLERYLADLPtlEDHQKQSQQLKDSELKSTELQEKVTELESLLEET-QAICREKEIQLESLRQREAEFSSAG 548
Cdd:PRK04863 840 RQLNRRRVELERALADHE--SQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRFVQQHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 549 HSLQDKQSVEETSGEGPEvEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQ------------SLEQEVAQEEGTSQALRE 616
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPE-QFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedaaeMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40538794 617 EAQRRDSALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQAQPGSPPSPDTAQLAL-----ELHQELASC 680
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASlkssydaKRQMLQELKQELQDLGVPADSGAEERArarrdELHARLSAN 1072
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-622 |
6.82e-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: 49.79 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 384 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCq 463
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 keSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAE 543
Cdd:pfam01576 422 --SESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40538794 544 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeEGTSQALREEAQRRD 622
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL---EALTQQLEEKAAAYD 569
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-741 |
7.15e-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: 49.72 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 379 VCLLRLQELQREN-----TFLRAQFAQKTEALsREKIDLE----KKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVK 449
Cdd:pfam05483 242 VSLLLIQITEKENkmkdlTFLLEESRDKANQL-EEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 450 GRDKHINNL--KKKCQKEsEQNREKQQRIETLERYLADLPTLEDHQKQSQQ-LKDSE----LKSTELQEKVTELEslleE 522
Cdd:pfam05483 321 IATKTICQLteEKEAQME-ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrLEKNEdqlkIITMELQKKSSELE----E 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 523 TQAICREKEIQLESLRQREAEFSSAghsLQDKQSVEetsgegpevemeswqkrydslqKIVEKQQQKMDQLRSQVQSLEQ 602
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKL---LDEKKQFE----------------------KIAEELKGKEQELIFLLQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 603 EVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEK-NLTLQEHLRQAQpgsppspDTAQLALEL--HQElas 679
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcDKLLLENKELTQ-------EASDMTLELkkHQE--- 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538794 680 clqdlqavcSIVTQRAQGHdpnlSLLLGIHSAQHPETQLD----------LQKPDVIKRKLEEVQQLRRDIE 741
Cdd:pfam05483 521 ---------DIINCKKQEE----RMLKQIENLEEKEMNLRdelesvreefIQKGDEVKCKLDKSEENARSIE 579
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-686 |
7.64e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 330 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREK 409
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 410 IDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR-------------- 475
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 476 ----IETLERYLADLPTL----------------EDHQKQSQQLKD----SELKSTELQEKVTELESLLEETQAICREKE 531
Cdd:COG4717 264 lggsLLSLILTIAGVLFLvlgllallflllarekASLGKEAEELQAlpalEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 532 IQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESwqkrYDSLQKIVEKQQQKmDQLRSQVQSLEQEVAQEEGTS 611
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED----EEELRAALEQAEEY-QELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 612 QALREEAQRRD--SALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELHQELASCLQDLQA 686
Cdd:COG4717 419 EELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLE--------EDGELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
383-540 |
8.25e-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: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQKTEALSREKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKK 461
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLELLEAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 CQKESEQNREKQQRIETLERYLADL--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICREKEI 532
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*...
gi 40538794 533 QLESLRQR 540
Cdd:COG4913 427 EIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
394-651 |
1.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 394 LRAQFAQKTEALSREKI-DLEKKLSASEVEVQLI----------RESLKVALQKHSEevKKQE-ERVKGRDKHINNLKKK 461
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLnGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEE--RREElETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 CQKE----SEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESL 537
Cdd:PRK02224 270 TEREreelAEEVRDLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 538 RQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKivekqqqKMDQLRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270
....*....|....*....|....*....|....
gi 40538794 618 AQRRDSALQQLRTAVKELsvqnQDLIEKNLTLQE 651
Cdd:PRK02224 421 RDELREREAELEATLRTA----RERVEEAEALLE 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
466-642 |
1.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 466 SEQNREKQQRIETLERYLADLptledhqKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFS 545
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 546 SAGHSLQDKQSVEETSGEGPEVEME--SWQKRYDSLQKIVEKQQQKMDQLRSQVQ--------SLEQEVAQEEGTSQALR 615
Cdd:COG3206 254 DALPELLQSPVIQQLRAQLAELEAElaELSARYTPNHPDVIALRAQIAALRAQLQqeaqrilaSLEAELEALQAREASLQ 333
|
170 180
....*....|....*....|....*..
gi 40538794 616 EEAQRRDSALQQLRTAVKELSVQNQDL 642
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV 360
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-678 |
1.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 501 DSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFssaghslqdkQSVEETSGEgpEVEMESWQKRYDSLQ 580
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 581 ---KIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEK-----NLTLQEH 652
Cdd:COG4913 675 aelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEER 754
|
170 180
....*....|....*....|....*.
gi 40538794 653 LRQAQpgspPSPDTAQLALELHQELA 678
Cdd:COG4913 755 FAAAL----GDAVERELRENLEERID 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
383-633 |
1.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRD--KHINNLKK 460
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeaKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 KCQKESEQNREKQQRIEtlERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEiQLESLRQR 540
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAE--EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 541 EAEFSSAGHSLQDKQSVEETSGEGPEVEMEswQKRYDSLQKIVEkQQQKMDQLRSQVqslEQEVAQEEGTSQAlrEEAQR 620
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEE--KKKADEAKKKAE-EAKKADEAKKKA---EEAKKAEEAKKKA--EEAKK 1471
|
250
....*....|...
gi 40538794 621 RDSALQQLRTAVK 633
Cdd:PTZ00121 1472 ADEAKKKAEEAKK 1484
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
330-638 |
2.12e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 330 LNSNEHLLKEKELLIDKQRKHISQLE---QKVR---ESELQVHSALLGRPAPFGDVCLLrLQELQRENTFLRAQFAQKTE 403
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQfenEKVSlklEEEIQENKDLIKENNATRHLCNL-LKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 404 ALSREKIDL----EKKLSASE---VEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQRI 476
Cdd:pfam05483 180 ETRQVYMDLnnniEKMILAFEelrVQAENARLEMHFKLKEDHEKIQHLEEEYK---KEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 477 ETLERYLADLPTLEDHQKQSQQLKDSELK-STELQEKVT-ELESL-------------LEE-----TQAICR---EKEIQ 533
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKeLIEKKDHLTkELEDIkmslqrsmstqkaLEEdlqiaTKTICQlteEKEAQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 534 LESLRQREA-------EFSSAGHSLQDKQSVEETSGEGPE-------VEMESWQKRYDSLQKIVEKQQQKMDQLRS---Q 596
Cdd:pfam05483 337 MEELNKAKAahsfvvtEFEATTCSLEELLRTEQQRLEKNEdqlkiitMELQKKSSELEEMTKFKNNKEVELEELKKilaE 416
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 40538794 597 VQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQ 638
Cdd:pfam05483 417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
378-658 |
2.39e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 378 DVCLLRLQELQRENtFLRAQFAQKtealsREKIDLEKKLSASEVEVQLIRESLKVALQKHSEE---VKKQEERVKGRDKH 454
Cdd:COG5022 745 DNIATRIQRAIRGR-YLRRRYLQA-----LKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPllsLLGSRKEYRSYLAC 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 455 INNLKKKCQKESEQN-REKQQR-------IETLERYLADLPTLEDHQKQS------QQLKDSELKSTELQEKVTELESLL 520
Cdd:COG5022 819 IIKLQKTIKREKKLReTEEVEFslkaevlIQKFGRSLKAKKRFSLLKKETiylqsaQRVELAERQLQELKIDVKSISSLK 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 521 EetQAICREKEI-----QLESLRQREAEFSSAgHSLQDKQSVEET-SGEGPEVEMESwqkrydslQKIVEKQQQKMDQLR 594
Cdd:COG5022 899 L--VNLELESEIielkkSLSSDLIENLEFKTE-LIARLKKLLNNIdLEEGPSIEYVK--------LPELNKLHEVESKLK 967
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 595 SQVQSLEQEVAQEEgtsqALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQP 658
Cdd:COG5022 968 ETSEEYEDLLKKST----ILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
566-753 |
2.43e-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: 47.45 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 566 EVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELsvqNQDLIEK 645
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL---RAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 646 NLTLQEHLRQAQPGSPPSPDTAQLALELHQELASCLQDLQAVcsivtqraqghdpnlslllgihsaqhpeTQLDLQKPDV 725
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL----------------------------APARREQAEE 154
|
170 180
....*....|....*....|....*...
gi 40538794 726 IKRKLEEVQQLRRDIEDLRTTMSDRYAQ 753
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAE 182
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
385-612 |
3.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 385 QELQRENTFLRAQFAQKT-EALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhseevkKQEERVKGRDKHINNLKKKCQ 463
Cdd:COG3206 159 EAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEAALEEFRQKNGLV---------DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 KESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKD------------SELKST---------ELQEKVTELESLL-E 521
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaeleaelAELSARytpnhpdviALRAQIAALRAQLqQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 522 ETQAICREKEIQLESLRQREAEFSsaghslQDKQSVEETSGEGPEVEMEswqkrYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQ------AQLAQLEARLAELPELEAE-----LRRLEREVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 40538794 602 QEVAQEEGTSQ 612
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
537-655 |
4.09e-05 |
|
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: 44.23 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 537 LRQREAEFssaghslqdKQSVEETSGEgPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 616
Cdd:pfam11559 46 QRDRDLEF---------RESLNETIRT-LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKE 115
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 40538794 617 EAQRRDSALQQLRTAvkelsvQNQDLIEKNL---TLQEHLRQ 655
Cdd:pfam11559 116 ELQRLKNALQQIKTQ------FAHEVKKRDReieKLKERLAQ 151
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-749 |
4.79e-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: 47.04 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 384 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLsasEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 463
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKI---ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 KESEQNREKQ----QRIETLERYLADLPTLEDHQKQSQQLKDSELK------STELQEKVTELESLLEETQAICREKEIQ 533
Cdd:pfam15921 303 IIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEkqlvlaNSELTEARTERDQFSQESGNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 534 LESLRQREAEFSSAGHslQDKQSVEETSGEgpEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQ-SLEQEVAQEEGTSQ 612
Cdd:pfam15921 383 LADLHKREKELSLEKE--QNKRLWDRDTGN--SITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 613 ALREEAQ---RRDSALQQLRTAVKELSVQNQDLIEKNLT-------LQEHLRQAQP-GSPPSPDTAQLALELhQELASC- 680
Cdd:pfam15921 459 SLEKVSSltaQLESTKEMLRKVVEELTAKKMTLESSERTvsdltasLQEKERAIEAtNAEITKLRSRVDLKL-QELQHLk 537
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40538794 681 -----LQDLQAVCSIVTQRAQGHDPNLSLLlgihsAQHPE--TQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSD 749
Cdd:pfam15921 538 negdhLRNVQTECEALKLQMAEKDKVIEIL-----RQQIEnmTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
290-634 |
5.35e-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: 47.04 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 290 LELIRLQMEQMQLQNGaicHHPAAFGPSLpiLEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 364
Cdd:pfam15921 564 IEILRQQIENMTQLVG---QHGRTAGAMQ--VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 365 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 433
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 434 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 505
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 506 STELQEKVTELESLLEETQAICREkeiqLESLRQREaEFSSAGHSLQDKQSVEETSGEGpevemeswqkrYDSLQKIVEK 585
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAE----CQDIIQRQ-EQESVRLKLQHTLDVKELQGPG-----------YTSNSSMKPR 862
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 40538794 586 QQQKMDQLRSQ-----VQSLEQEVAQEEGTSQALREEAQRR-DSALQQLRTAVKE 634
Cdd:pfam15921 863 LLQPASFTRTHsnvpsSQSTASFLSHHSRKTNALKEDPTRDlKQLLQELRSVINE 917
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
393-682 |
5.74e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 393 FLRAQFAQK--TEALSREKIDLEKKLSASEVEVQLIRESLKVALqkhseEVKKQEERVKgrdKHINNLKKKCQKESEQNR 470
Cdd:PRK11281 26 FARAASNGDlpTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTL-----ALLDKIDRQK---EETEQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 471 EKQQRIETLERYLADlPTLEDHQKQSQqlkdselksTELQEKVTELESLLEETQAICREKEIQLESLRQR----EAEFSS 546
Cdd:PRK11281 98 QAQAELEALKDDNDE-ETRETLSTLSL---------RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 547 AGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQ---QQKMDQLRSQVQSLEQevaqeegtsqalreeaQRRDs 623
Cdd:PRK11281 168 NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQndlQRKSLEGNTQLQDLLQ----------------KQRD- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40538794 624 aLQQLRTAVKELSVQN-QDLI-EKNLTL-QEHLRQAQpgsppSPDTAQLALE---LHQELASCLQ 682
Cdd:PRK11281 231 -YLTARIQRLEHQLQLlQEAInSKRLTLsEKTVQEAQ-----SQDEAARIQAnplVAQELEINLQ 289
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
426-656 |
7.79e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 426 IRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKcqkESEQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSEL 504
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNKIESArADLEDIKIKINELKDKHD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 505 KSTELQE-----KVTELESLLEE-TQAICREKEIQLESLRQREAEFSSAGHSLQDKqsVEETSGEGPEV---------EM 569
Cdd:PRK01156 547 KYEEIKNrykslKLEDLDSKRTSwLNALAVISLIDIETNRSRSNEIKKQLNDLESR--LQEIEIGFPDDksyidksirEI 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 570 ESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE---EAQRRDSALQQLRTAVKELSVQN---QDLI 643
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRarlESTI 704
|
250
....*....|...
gi 40538794 644 EKNLTLQEHLRQA 656
Cdd:PRK01156 705 EILRTRINELSDR 717
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-635 |
8.24e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 327 ISILNSNEHLLKEKELLIDKQRKHISQLEQKVRE--------SELQVHSALLGRPAPFGDVCLL-----RLQELQRENTF 393
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkEELERLKKRLTGLTPEKLEKELeelekAKEEIEEEISK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 394 LRAQFAQ-KTEALSREK--IDLEK---------KLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKK 461
Cdd:PRK03918 410 ITARIGElKKEIKELKKaiEELKKakgkcpvcgRELTEEHRKELLEEYTA-ELKRIEKELKEIEEKERKLRKELRELEKV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 CQKESEQNREKQ--QRIETLERYLADLpTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQ 539
Cdd:PRK03918 489 LKKESELIKLKElaEQLKELEEKLKKY-NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 540 REAEFSSAGHSLQDK--QSVEETSGEGPevEMESWQKRYDSLQKIvekqqqkmdqlRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:PRK03918 568 LEEELAELLKELEELgfESVEELEERLK--ELEPFYNEYLELKDA-----------EKELEREEKELKKLEEELDKAFEE 634
|
330
....*....|....*...
gi 40538794 618 AQRRDSALQQLRTAVKEL 635
Cdd:PRK03918 635 LAETEKRLEELRKELEEL 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-743 |
8.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 337 LKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRpapfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKL 416
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 417 SASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLE-------RYLADLPTL 489
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEelaeaaaRLLLLLEAE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 490 EDHQKQSQQLKDSELKS---------TELQEKVTELESLLEE-------------------------TQAICREKEIQLE 535
Cdd:COG1196 501 ADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEAalaaalqnivveddevaaaaieylkAAKAGRATFLPLD 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 536 SLRQREAEfSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT--SQA 613
Cdd:COG1196 581 KIRARAAL-AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggSAG 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 614 LREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQpgsppspdTAQLALELHQELASCLQDLQAVcsIVTQ 693
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE--------EEERELAEAEEERLEEELEEEA--LEEQ 729
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 40538794 694 RAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDL 743
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
401-540 |
9.14e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 401 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 480
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538794 481 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRE--KEIQLESLRQR 540
Cdd:PRK12704 117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
406-638 |
1.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 406 SREKI--------DLE---KKLSASEVEVQLIRESLKVALQKHS---EEVKKQEERVKGRDKHINNLKKKCQKESEQNRE 471
Cdd:PRK03918 146 SREKVvrqilgldDYEnayKNLGEVIKEIKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 472 KQQRIETLERYLADLPTLE-DHQKQSQQLKDSELKSTELQEKVTELESLLEETqaicREKEIQLESLRQREAEFSSAGhS 550
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEkELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAEEYIKLS-E 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 551 LQDKQSVEETSGegpEVEMESWQKRYDSLQKIV---EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALrEEAQRRDSALQQ 627
Cdd:PRK03918 301 FYEEYLDELREI---EKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELER 376
|
250
....*....|.
gi 40538794 628 LRTAVKELSVQ 638
Cdd:PRK03918 377 LKKRLTGLTPE 387
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
337-704 |
1.31e-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: 45.49 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 337 LKEKELLIDKQRKHISQLEQKVRESE--LQVHSALLGRPAPFGDVCLLRLQELQRENTFLRaQFAQKTEALsreKIDLEK 414
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKEraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEAL---KLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 415 KLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTL 489
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekvKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 490 EDHQKQSQQLKDSELKSTELQEKV----TELESLLEETQAI---CREKEIQLESLRQR-EAEFSSAGHSLQDK----QSV 557
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVktsrNELNSLSEDYEVLkrnFRNKSEEMETTTNKlKMQLKSAQSELEQTrntlKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 558 EETSGEGPEVEMeswqkrydSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTA----VK 633
Cdd:pfam15921 719 EGSDGHAMKVAM--------GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEknkmAG 790
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 634 ELSV---QNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQlalelHQELASCLQDLQAVCSIVTQRAQGHDPNLSL 704
Cdd:pfam15921 791 ELEVlrsQERRLKEKVANMEVALDKASLQFAECQDIIQ-----RQEQESVRLKLQHTLDVKELQGPGYTSNSSM 859
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
412-641 |
1.36e-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: 45.49 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 412 LEKKLSASEVEVQLIRESLKVALQKHSEEVkkqeERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLED 491
Cdd:pfam15921 431 LEALLKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 492 HQKQSQQLKDSE---------LKSTELQEKVTElESLLEETQAICR-------EKEIQLESLRQREAEFS--------SA 547
Cdd:pfam15921 507 EKERAIEATNAEitklrsrvdLKLQELQHLKNE-GDHLRNVQTECEalklqmaEKDKVIEILRQQIENMTqlvgqhgrTA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 548 GHSLQDKQSVEEtsgegpevEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQ--EEGTS--QALREEAQRRDS 623
Cdd:pfam15921 586 GAMQVEKAQLEK--------EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKlvNAGSErlRAVKDIKQERDQ 657
|
250
....*....|....*...
gi 40538794 624 ALQQLRTAVKELSVQNQD 641
Cdd:pfam15921 658 LLNEVKTSRNELNSLSED 675
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
328-657 |
1.44e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 328 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQ--ELQRENTFLRAQFAQKTEAL 405
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAELRAQLAKKEEEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 406 SREKIDLEKKLSASEVEVQLIREslkvaLQKHSEEVKKQEERVKGRDkhinnlkkkcQKESEQNREKQQRIETLERYLAD 485
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRE-----LEAQISELQEDLESERAAR----------NKAEKQRRDLGEELEALKTELED 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 486 lpTLEDHQKQSqqlkdsELKSTELQEkVTELESLLEETQaicREKEIQLESLRQREaefSSAGHSLQD--------KQSV 557
Cdd:pfam01576 311 --TLDTTAAQQ------ELRSKREQE-VTELKKALEEET---RSHEAQLQEMRQKH---TQALEELTEqleqakrnKANL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 558 EETSgEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSV 637
Cdd:pfam01576 376 EKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
330 340
....*....|....*....|
gi 40538794 638 QNQDLIEKNLTLQEHLRQAQ 657
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQ 474
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
455-651 |
1.55e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 455 INNLKKKCQKESEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKD--SELKS--TELQEKVTELESLLEETQAICREK 530
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAE--KRDELNAQVKELREeaQELREkrDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 531 EIQLESLRQREAEFSSAGHSLQD-KQSVE------ETSGEGPEVEME------SWQKRYDSLQKIVEkQQQKMDQLRSQV 597
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKlRKEIErlewrqQTEVLSPEEEKElvekikELEKELEKAKKALE-KNEKLKELRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 40538794 598 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQE 651
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
383-617 |
2.05e-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: 44.81 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQElQRENtfLRAQFAQKTEALSREKIDLEKKLSASEVEVQLiRESLKVALQKHSEEVK----KQEERVKGRDKHINNL 458
Cdd:pfam10174 454 RLKE-QRER--EDRERLEELESLKKENKDLKEKVSALQPELTE-KESSLIDLKEHASSLAssglKKDSKLKSLEIAVEQK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 459 KKKCQKESEQNReKQQRIETLERyladlpTLEDHQKQSQQL-KDSELKSTELQEKVTELESLLE-----ETQAICREKEI 532
Cdd:pfam10174 530 KEECSKLENQLK-KAHNAEEAVR------TNPEINDRIRLLeQEVARYKEESGKAQAEVERLLGilrevENEKNDKDKKI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 533 -QLESLRQRE-AEFSSAGHSLQDKQSV---------EETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLE 601
Cdd:pfam10174 603 aELESLTLRQmKEQNKKVANIKHGQQEmkkkgaqllEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQ 682
|
250
....*....|....*.
gi 40538794 602 QEVAQEEGTSQALREE 617
Cdd:pfam10174 683 QSLAEKDGHLTNLRAE 698
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
383-636 |
2.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQREntflRAQFAQKTEALSrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLK 459
Cdd:PRK02224 476 RVEELEAE----LEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 460 KKCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselkSTELQEKVTELESL--LEETQAICREKEIQLESL 537
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAEL-------------------NSKLAELKERIESLerIRTLLAAIADAEDEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 538 RQREAEFSSAGHSLQDKQS-----VEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 612
Cdd:PRK02224 612 REKREALAELNDERRERLAekrerKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
250 260 270
....*....|....*....|....*....|
gi 40538794 613 ALREEAQRRDS------ALQQLRTAVKELS 636
Cdd:PRK02224 692 ELEELRERREAlenrveALEALYDEAEELE 721
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
484-672 |
2.25e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 484 ADLPTLEDHQKQSQQLKDSELKS-TELQEKVTELESLLEETQAICREKEIQLESLRQReaefssaghsLQDKqsVEETSG 562
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEaKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA----------LKDL--LTDEGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 563 EGPEVEMESWQKRYDSLQK-IVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEL-SVQNQ 640
Cdd:cd22656 175 AIARKEIKDLQKELEKLNEeYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeKLQGA 254
|
170 180 190
....*....|....*....|....*....|....
gi 40538794 641 -DLIEKNL-TLQEHLRQAqPGSPPSPDTAQLALE 672
Cdd:cd22656 255 wQAIATDLdSLKDLLEDD-ISKIPAAILAKLELE 287
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
395-676 |
2.85e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 395 RAQFAQKT------EALSREKIDLEKKLSA-SEVEVQLIRESLKVALQKHSEEvkkqeervkgrdkhiNNLKKKCQKESE 467
Cdd:PRK10246 369 RAQFSQQTsdreqlRQWQQQLTHAEQKLNAlPAITLTLTADEVAAALAQHAEQ---------------RPLRQRLVALHG 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 468 QNREKQQRIETLERYLADLPTleDHQKQSQQLKDSELKSTELQEKVTELESLLEetqaicREKEIQ-LESLRQReaefss 546
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQNVTQ--EQTQRNAALNEMRQRYKEKTQQLADVKTICE------QEARIKdLEAQRAQ------ 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 547 aghsLQDKQSVEET-SGEGPEV------EMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 619
Cdd:PRK10246 500 ----LQAGQPCPLCgSTSHPAVeayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQ 575
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 40538794 620 RRDSALQQLrTAVKELSVQNQDLIEKNLTLQE-HLRQAQPGSPPSPDTAQLALELHQE 676
Cdd:PRK10246 576 ALTQQWQAV-CASLNITLQPQDDIQPWLDAQEeHERQLRLLSQRHELQGQIAAHNQQI 632
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
403-539 |
2.87e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 403 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 482
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 483 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICREKEIQLESLRQ 539
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
438-563 |
3.43e-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: 43.03 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 438 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 517
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 40538794 518 SLLEETQA---ICREKEIqleSLRQREAEFSSAGHSLQDKQSVEETSGE 563
Cdd:pfam15934 169 KLQEELRTerkILREEVI---ALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
384-519 |
3.81e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 384 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 463
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 464 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 519
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-659 |
3.92e-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: 44.06 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKK-- 460
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 -----KCQK-ESEQNREKQQRIETLERYLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaicrEKEIQL 534
Cdd:pfam12128 364 kaltgKHQDvTAKYNRRRSKIKEQNNRDIAGI-----KDKLAKIREARDRQLAVAEDDLQALESELRE------QLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 535 ESLRQREAEFSSAGHSLQDKQSVEETSgegPEVEMESWQKrydslQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGtsqal 614
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATAT---PELLLQLENF-----DERIERAREEQEAANAEVERLQSELRQARK----- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 40538794 615 reeaqRRDSA----------LQQLRTAVKELSVQnqdLIEKNLTLQEHLRQAQPG 659
Cdd:pfam12128 500 -----RRDQAsealrqasrrLEERQSALDELELQ---LFPQAGTLLHFLRKEAPD 546
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
451-645 |
4.91e-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: 43.66 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 451 RDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---------------LEDHQKQSQQLKdsELKSTELQEKVTE 515
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtalttleeaLSEKERIIERLK--EQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 516 LESLLEETQaicrEKEIQLESLRQREAEFSSAGHSLQDKQSVEETSG-------EGPEVEMESWQKRYDSLQKIVEKQQQ 588
Cdd:pfam10174 470 LESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkdsklKSLEIAVEQKKEECSKLENQLKKAHN 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40538794 589 KMDQLR------SQVQSLEQEVAQEegtsqalREEAQRRDSALQQLRTAVKELSVQNQDLIEK 645
Cdd:pfam10174 546 AEEAVRtnpeinDRIRLLEQEVARY-------KEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
411-592 |
5.32e-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: 42.05 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 411 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 486
Cdd:cd00176 18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 487 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRE---KEIQLESLRQREAEFSSA 547
Cdd:cd00176 96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 40538794 548 GHSLQDKQSveetsgegpEVEMESWQKRYDSLQKIVEKQQQKMDQ 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 ... |
336-754 |
5.35e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 336 LLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKK 415
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 416 LSASEVEVQLIRESLKVALQKHSE---------EVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL 486
Cdd:TIGR00618 496 LLELQEEPCPLCGSCIHPNPARQDidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 487 PTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEfssagHSLQDKQSVEETSGEG 564
Cdd:TIGR00618 576 TQCDNRSKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-----QQCSQELALKLTALHA 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 565 PEVEMESWQKRYDSLQKiveKQQQKmdQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIE 644
Cdd:TIGR00618 651 LQLTLTQERVREHALSI---RVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 645 KNLTLQEHLRQaqpgsppspdtaqlALELHQELASCLQDLQ--AVCSIVTQRAQGHDPNLSLLLGIHSAQHPETQLDLQK 722
Cdd:TIGR00618 726 ASSSLGSDLAA--------------REDALNQSLKELMHQArtVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN 791
|
410 420 430
....*....|....*....|....*....|....*...
gi 40538794 723 PDV------IKRKLEEVQQLRRDIEDLRTTMSDRYAQD 754
Cdd:TIGR00618 792 RLReedthlLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
381-673 |
7.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 381 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 457
Cdd:COG4372 37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 458 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLEsl 537
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 538 rQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKmDQLRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:COG4372 189 -LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL-DALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 40538794 618 AQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLALEL 673
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
412-602 |
7.61e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 412 LEKKLSAS----EVEVQLIR-ESLKVALQKHSEEVKKQEERVKGRDKHINNlkKKCQKESEQNREKQQRIETLERYladl 486
Cdd:COG2433 355 VEKKVPPDvdrdEVKARVIRgLSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAE---- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 487 ptledhqkqsqqlkdselkstelqekVTELESLLEETQAICREKEIQLESLRQREaefssaghslqdKQSVEEtsgegpE 566
Cdd:COG2433 429 --------------------------VEELEAELEEKDERIERLERELSEARSEE------------RREIRK------D 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 40538794 567 VEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQ 602
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
349-652 |
8.16e-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: 42.33 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 349 KHISQLEQKVRESELQVHSALLGRPAPFgDVCLLRLQELQRENTFLRAQFAQKTEALsREKIDLEKKLSASEVEVQLIRE 428
Cdd:cd08915 45 ASIDDLQKPENLPDSIQHSQEIIEEGGL-DNIEQSFKELSKLRQNVEELLQECEELL-EEEAAEDDQLRAKFGTLRWRRP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 429 SLKVALQKHSEEVkkqeervkgrdkhiNNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELkSTE 508
Cdd:cd08915 123 SSDEAAKELYEKV--------------TKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPAL-DPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 509 LQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAghslqdkQSVEETSGEGPEVEMESWQKR----YDSLQKIVE 584
Cdd:cd08915 188 VSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDIL-------PKLITEYKKNGTTEFEDLFEEhlkkFDKDLTYVE 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40538794 585 KQQQKMDQLRSQVQSLEQEVAQEEGTSqalrEEAQRRDSALQQLRTAVKELS--VQN--------QDLIEKNLTLQEH 652
Cdd:cd08915 261 KTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYKKYLelKENlnegskfyNDLIEKVNRLLEE 334
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
399-655 |
8.18e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 399 AQKTEALSREKidLEKKLSASEVEV-QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIE 477
Cdd:TIGR00606 273 ALKSRKKQMEK--DNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 478 TLERyladlpTLEDHQKQSQQlKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSV 557
Cdd:TIGR00606 351 RLQL------QADRHQEHIRA-RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 558 EETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQ-RRDSALQQLRTAV 632
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSsdriLELDQELRKAERELSKaEKNSLTETLKKEV 503
|
250 260
....*....|....*....|...
gi 40538794 633 KELSVQNQDLIEKNLTLQEHLRQ 655
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQ 526
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
400-649 |
8.66e-04 |
|
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: 42.81 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 400 QKTEALSREKIDLEKKLSASEVEVQLIRESLKValqkhseevkkQEERVKGRDKHINNLKKKCQKESEQNrekqQRIETL 479
Cdd:pfam05557 111 NELSELRRQIQRAELELQSTNSELEELQERLDL-----------LKAKASEAEQLRQNLEKQQSSLAEAE----QRIKEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 480 ERYLAdlptledhqkqsQQLKDSEL--KSTELQEKVTELESLLEETQA-------ICREKEI---QLESLRQREAEFSSA 547
Cdd:pfam05557 176 EFEIQ------------SQEQDSEIvkNSKSELARIPELEKELERLREhnkhlneNIENKLLlkeEVEDLKRKLEREEKY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 548 ghslQDKQSVEETSGEGPEVEMESWQK----------RYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE 617
Cdd:pfam05557 244 ----REEAATLELEKEKLEQELQSWVKlaqdtglnlrSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
250 260 270
....*....|....*....|....*....|..
gi 40538794 618 AQRRDSALQQLRTAVKELSVQNQDLIEKNLTL 649
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLL 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
489-620 |
9.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 489 LEDHQKQSQQLKdsELKSTELQEKVTELESLLEETQAIcREKEIQ--LESLRQREAEFSSAGHSLQDKqsveetsgegpE 566
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRE-RRNELQklEKRLLQKEENLDRKLELLEKR-----------E 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538794 567 VEMESWQKRYDSLQKIVEKQQQKMDQLRS-QVQSLEqEVA---QEEGTSQAL---REEAQR 620
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEeQLQELE-RISgltAEEAKEILLekvEEEARH 169
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
466-643 |
1.02e-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: 42.54 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 466 SEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSelkSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFS 545
Cdd:pfam09730 265 SEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGA---LSEQQEKVNRLTENLEAMRGLQASKERQDALDSEKDRDSH 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 546 SAGHS----------LQDKQSVEETSGEGPEVEMESWQKRYdslQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 615
Cdd:pfam09730 342 EDGDYyevdingpeiLECKYRVAVEEAGELREELKALKARY---NTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQ 418
|
170 180 190
....*....|....*....|....*....|..
gi 40538794 616 EEAQRRDSALQQLRTAVKE----LSVQNQDLI 643
Cdd:pfam09730 419 ERIAHLEKELGKTRKVAGEsegsLSVAQDELV 450
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
493-749 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 493 QKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSlqdkqsveetsgegpEVEMESW 572
Cdd:pfam05557 16 NEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE---------------QAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 573 QKRY-DSLQKIVEKQQQKMDQLRSQVQSLEQEVAqeegtsqALREEAQRRDSALQQLRTAVKELSVQNqDLIEKNLTLQE 651
Cdd:pfam05557 81 KKKYlEALNKKLNEKESQLADAREVISCLKNELS-------ELRRQIQRAELELQSTNSELEELQERL-DLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 652 HLRQAQPGSPPSPDTAQLAL-ELHQELASCLQDlqavcSIVTQRAQghdpnlSLLLGIHsaqhpetqlDLQKpdvikrkl 730
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIkELEFEIQSQEQD-----SEIVKNSK------SELARIP---------ELEK-------- 204
|
250
....*....|....*....
gi 40538794 731 eEVQQLRRDIEDLRTTMSD 749
Cdd:pfam05557 205 -ELERLREHNKHLNENIEN 222
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
430-654 |
1.33e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 41.91 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 430 LKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQSQQLKDSELKste 508
Cdd:pfam03999 7 LHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDALSEENDKEQRiLQSIADLRAEAAILCLYMRNRLLHEERDPFEPK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 509 lqekvtELESLLEETQAICREKEIQLESLRQREAEFSSAGHslQDKQSVEETSGEG--------PEVE-MESWQKRYDSL 579
Cdd:pfam03999 84 ------KGMSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLE--QLQQLCEELGEEPlpllidplPSLEeLESFRKHLENL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 580 QKIVEKQQQKMDQLRSQVQSL------------EQEVAQEEGTSQAL-REEAQRRDSALQQLRTAVKELSVQNQDLIEKN 646
Cdd:pfam03999 156 RNEKERRLEEVNELKKQIKLLmeeldlvpgtdfEEDLLCESEDNFCLsRENIDKLRKLIKQLEEQKAEREEKIDDLREKI 235
|
....*...
gi 40538794 647 LTLQEHLR 654
Cdd:pfam03999 236 LELWNRLQ 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
455-635 |
1.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 455 INNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELE---SLLEETQAICREKE 531
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 532 IQLESLRQREAEFSSAGHSLQDKQSVEETsgegpevEMESWQKRYDSLQKIVE-KQQQKMDQLRSQVQSLEQEVAQEEGT 610
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 40538794 611 SQALREEAQRRDSALQQLRTAVKEL 635
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
533-757 |
1.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 533 QLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQ--QQKMDQLRSQVQSLEQEVAQEEGT 610
Cdd:COG4913 611 KLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 611 SQALREEAQRRDSALQQLRTAVKELsvqnQDLIEKNLTLQEHLRQAQpgsppspdtaqlalelhQELASCLQDLQAVCSI 690
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEEL----DELKGEIGRLEKELEQAE-----------------EELDELQDRLEAAEDL 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 691 VtqrAQGHDPNLSLLLGIHSAQHPETQLDLQKPDVIKRKLEEVQQLRRDIEDLRTTMSDRYAQDMGE 757
Cdd:COG4913 743 A---RLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD 806
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
396-657 |
1.59e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 396 AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQ-EERVKGRDK---HINNL-------KKKCQK 464
Cdd:pfam00038 14 ASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQlDTLTVERARlqlELDNLrlaaedfRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 465 ESEQNREKQQRIETLERYLADLpTLE--DHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQ--------------AIC 527
Cdd:pfam00038 94 ELNLRTSAENDLVGLRKDLDEA-TLArvDLEAKIESLKEElAFLKKNHEEEVRELQAQVSDTQvnvemdaarkldltSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 528 REKEIQLESLRQReaefssaghslqDKQSVEETsgegpevemesWQKRYDSLQKIVEKQ-------QQKMDQLRSQVQSL 600
Cdd:pfam00038 173 AEIRAQYEEIAAK------------NREEAEEW-----------YQSKLEELQQAAARNgdalrsaKEEITELRRTIQSL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538794 601 EQEVAQEEGTSQAL----REEAQRRDSALQQLRTAVKELSVQNQDLIEknlTLQEHLRQAQ 657
Cdd:pfam00038 230 EIELQSLKKQKASLerqlAETEERYELQLADYQELISELEAELQETRQ---EMARQLREYQ 287
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
396-657 |
1.80e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 396 AQFAQKTEALSREKIDLEKKLSASEVevqlIRESLKVALQkhseevkkqeervkgrdkhinnLKKKCQKESEQNREKQQR 475
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQA----AHSQFEQAYQ----------------------LVRKIAGEVSRSEAWDVA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 476 IETLERYladlptlEDHQKQSQQLKdselkstELQEKVTELESLLEETQaicrekeiQLESLRQReaefssaghsLQDKQ 555
Cdd:PRK04863 499 RELLRRL-------REQRHLAEQLQ-------QLRMRLSELEQRLRQQQ--------RAERLLAE----------FCKRL 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 556 SVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREeAQrrdSALQQLRTAVKEL 635
Cdd:PRK04863 547 GKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA-AQ---DALARLREQSGEE 622
|
250 260
....*....|....*....|..
gi 40538794 636 SVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:PRK04863 623 FEDSQDVTEYMQQLLERERELT 644
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
385-540 |
1.86e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 385 QELQRENTFLRAQFAQKT---EALSREKIDLEKKLSASEVEVQLIRESLKVAlQKHSEEVKKQEERVKGRDKHINNLKKk 461
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLENY-EKDKQSLKNLKARLKVLEKELKDLKW- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 462 cqkeseQNREKQQRIETLERylaDLPTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEetqaicrEKEIQLESLRQ 539
Cdd:pfam13851 107 ------EHEVLEQRFEKVER---ERDELYDKFEAAIQdvQQKTGLKNLLLEKKLQALGETLE-------KKEAQLNEVLA 170
|
.
gi 40538794 540 R 540
Cdd:pfam13851 171 A 171
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
427-624 |
1.89e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 427 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ---KESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQL 499
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEaisQASRKLRETQNTLNQLNKQIDELNAsiakLEQQQAAQERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 500 KDSELKSTELQEKVTELESLL--EETQaicREKEIQ-------------LESLRQREAEFSSAGHSLQDKQSVEET---- 560
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILsgEESQ---RGERILayfgylnqarqetIAELKQTREELAAQKAELEEKQSQQKTllye 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 561 ---SGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAlREEAQRRDSA 624
Cdd:PRK11637 203 qqaQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKA-RAEREAREAA 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
493-653 |
1.97e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 493 QKQSQQLKDSEL-KSTELQEKV-TELESLLEETQAICREKEIQLESLrQREAEFSSAGHSLQ-----DKQSVEETSGEgP 565
Cdd:pfam01576 3 QEEEMQAKEEELqKVKERQQKAeSELKELEKKHQQLCEEKNALQEQL-QAETELCAEAEEMRarlaaRKQELEEILHE-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 566 EVEMESWQKRYDSLQKIVEKQQQkmdqlrsQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEK 645
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQ-------HIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE 153
|
....*...
gi 40538794 646 NLTLQEHL 653
Cdd:pfam01576 154 RKLLEERI 161
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
328-543 |
2.17e-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: 41.48 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 328 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 388
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 389 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 460
Cdd:COG5185 348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 461 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELES----LLEETQAICRE 529
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESrvstLKATLEKLRAK 507
|
250
....*....|....
gi 40538794 530 KEIQLESLRQREAE 543
Cdd:COG5185 508 LERQLEGVRSKLDQ 521
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
470-677 |
2.46e-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: 41.48 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 470 REKQQRIETLERyladlpTLEDHQKQSQQLKDselKSTELQEKVTELESLL--------EETQAICREKEIQLESLRQRE 541
Cdd:COG3096 839 AALRQRRSELER------ELAQHRAQEQQLRQ---QLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 542 AEFSSAGHSLQDKQSVEETSGEGPEvEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLE----QEVAQEEGTSQALRE- 616
Cdd:COG3096 910 AFIQQHGKALAQLEPLVAVLQSDPE-QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEk 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 617 --------EAQRRDsALQQLRTAVKELSVQNQDLIE-------KNLTLQEHLRQ-AQPGSPPSPDTAQLAL----ELHQE 676
Cdd:COG3096 989 lrarleqaEEARRE-AREQLRQAQAQYSQYNQVLASlkssrdaKQQTLQELEQElEELGVQADAEAEERARirrdELHEE 1067
|
.
gi 40538794 677 L 677
Cdd:COG3096 1068 L 1068
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
405-637 |
2.96e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 405 LSREKIDlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYla 484
Cdd:pfam02029 125 LGRYKEE-ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQK-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 485 dlptlEDHQKQSQQLKDSELKSTELQEKVTELESLL----EETQAICREKEIQLESLRQREAEFSSAGHSlQDKQSVEET 560
Cdd:pfam02029 202 -----RGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQsqerEEEAEVFLEAEQKLEELRRRRQEKESEEFE-KLRQKQQEA 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 561 sgegpEVEMESWQKRYDSLQKIVEKQQQKMDQlrsqvQSLEQEVAQEEGTSQaLREEAQRRDSALQQLRTAVKELSV 637
Cdd:pfam02029 276 -----ELELEELKKKREERRKLLEEEEQRRKQ-----EEAERKLREEEEKRR-MKEEIERRRAEAAEKRQKLPEDSS 341
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
473-743 |
3.06e-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: 40.98 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 473 QQRIETLERYLADLPTLEDHqkqsqqLKDSELKSTELQEKVTELESLLEEtQAICREKEIQlESLRQREAEFSSAGHSLQ 552
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFG------YKSDETLIASRQEERQETSAELNQ-LLRTLDDQWK-EKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 553 DKQSveetsgegpEVE-MESWQKRYDSLQKIVEKQQQKM-DQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQlrt 630
Cdd:pfam12128 319 KDRS---------ELEaLEDQHGAFLDADIETAAADQEQlPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE--- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 631 avkelsvQNQDLIEKNLTLQEHLRQAQpgsppspdtaqlalelHQELASCLQDLQAVCSIVTQRAQGHDPNLS------- 703
Cdd:pfam12128 387 -------QNNRDIAGIKDKLAKIREAR----------------DRQLAVAEDDLQALESELREQLEAGKLEFNeeeyrlk 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 40538794 704 -----LLLGIHSAQH-PETQLDL-QKPDVIKRKLEEVQQLRRDIEDL 743
Cdd:pfam12128 444 srlgeLKLRLNQATAtPELLLQLeNFDERIERAREEQEAANAEVERL 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
503-656 |
3.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 503 ELKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGE--GPEVEMESWQKRYDSLQ 580
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQlaEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 581 KIVEKQQQKM---------DQLRSQVQSLEQEVAQEEGTS-------QALREE--------AQRRDSALQQLRTAVKELS 636
Cdd:COG3206 247 AQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYtpnhpdvIALRAQiaalraqlQQEAQRILASLEAELEALQ 326
|
170 180
....*....|....*....|
gi 40538794 637 VQNQDLIEKNLTLQEHLRQA 656
Cdd:COG3206 327 AREASLQAQLAQLEARLAEL 346
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
424-657 |
3.49e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 424 QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKDSE 503
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ--SREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 504 LKSTELQEKVTELESLLEETQAICREKEIQLESLRQREAEfssaghslqdkqsveetsgegPEVEMEswqkrydslqKIV 583
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE---------------------RETELE----------RMK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40538794 584 EKQQQKMDQLRSQvqslEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQAQ 657
Cdd:pfam07888 157 ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
383-660 |
3.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 383 RLQELQRENTFLRAQFAQKTEAL--SREKIDLEKKLsASEVEVqLIRESLKVALQKHSEEVKKQEER---VKGRDKHINN 457
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLeqAKEGLSALNRL-LPRLNL-LADETLADRVEEIREQLDEAEEAkrfVQQHGNALAQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 458 LKK-------------KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSElKSTELQEKVTELESLLEETQ 524
Cdd:PRK04863 923 LEPivsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLA-KNSDLNEKLRQRLEQAEQER 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 525 AICREKeiqlesLRQREAEFSSAGHSLQDKQSveetsgegpevemeswqkRYDSLQKIVEKQQQKMDQLRSQVQS--LEQ 602
Cdd:PRK04863 1002 TRAREQ------LRQAQAQLAQYNQVLASLKS------------------SYDAKRQMLQELKQELQDLGVPADSgaEER 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 603 EVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDL--IEKNLTLQEHLRQAQPGS 660
Cdd:PRK04863 1058 ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLrkLERDYHEMREQVVNAKAG 1117
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-744 |
3.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 508 ELQEKVTELESLLEETQAIcREKEIQLESLRQREAEFSSAGHSLQDKQSVEETSGegpevemeswqkrydslqkiVEKQQ 587
Cdd:COG4913 229 ALVEHFDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR--------------------LWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 588 QKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNL-TLQEHLRQAQpgsPPSPDT 666
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIeRLERELEERE---RRRARL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40538794 667 AQLALELHQELASCLQDLQAVCSIVTQRAQGHDPNLSLLlgihsaqhpETQLDLQKpDVIKRKLEEVQQLRRDIEDLR 744
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL---------EEALAEAE-AALRDLRRELRELEAEIASLE 432
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
334-621 |
4.06e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 334 EHLLKEKELLidkQRKhISQLEQKVRESELQVHSALLGRpapfgdvclLRLQELQRENTFLRAQFAQKTEALSREKIDLE 413
Cdd:PLN02939 159 EKILTEKEAL---QGK-INILEMRLSETDARIKLAAQEK---------IHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 414 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKgrdkhinNLKKKCQKESEQNREkqqrietLERYLADlptledhq 493
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQ-FLKAELIEVAETEERVF-------KLEKERSLLDASLRE-------LESKFIV-------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 494 KQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESlrqreaefssaGHSLQDKQSVEETSGEGPEVEMESWQ 573
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQ-----------NQDLRDKVDKLEASLKEANVSKFSSY 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 40538794 574 KrYDSLQ---KIVEKQQQKMDQ-LRSQVQSLEQEVAQEEGTSQALREEAQRR 621
Cdd:PLN02939 352 K-VELLQqklKLLEERLQASDHeIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-522 |
4.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 327 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 401
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 402 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 458
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40538794 459 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 522
Cdd:PRK03918 693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
321-627 |
4.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 321 LEPAQWISILNSNEHLLKEKELL-IDKQRKHISQLEQKVreselQVHSALLGRPAPFGDVCLLRLQELQRENT---FLRA 396
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIdEDIDGNHEGKAEAKA-----HVGQDEGLKPSYKDFDFDAKEDNRADEATeeaFGKA 1100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 397 QFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE--------RVK-GRDKHINNLKKKCQKESE 467
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDakrveiarKAEdARKAEEARKAEDAKKAEA 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 468 QNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLE----ETQAICREKEIQLESLRQREAE 543
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 544 FSSAGHSLQDKQSVEETSgEGPEVEMESWQKRYDSLQKIVEKqqQKMDQLRSQVqslEQEVAQEEGTSQAlrEEAQRRDS 623
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEK--KKADEAKKKA---EEAKKADEAKKKA--EEAKKKAD 1332
|
....
gi 40538794 624 ALQQ 627
Cdd:PTZ00121 1333 AAKK 1336
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-522 |
4.69e-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: 40.39 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 328 SILNSNEH---LLKEKELLIDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENtflraqfaqktEA 404
Cdd:TIGR04523 579 SLKKKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSLEKE-------------------LEKAKKEN-----------EK 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 405 LSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKESEQNREKqqRIETLERYlA 484
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKELSLHYKK--YITRMIRI-K 704
|
170 180 190
....*....|....*....|....*....|....*...
gi 40538794 485 DLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 522
Cdd:TIGR04523 705 DLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
382-656 |
5.95e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 382 LRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIR---ESLKVALQKHSEEVKKQEERVKGRDKHINNL 458
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 459 KKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICREKEIQLESLR 538
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEEL--QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 539 QREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEA 618
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270
....*....|....*....|....*....|....*...
gi 40538794 619 QRRDSALQQLRTAVKELSVQNQDLIEKNLTLQEHLRQA 656
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
427-543 |
6.01e-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: 39.14 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 427 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKS 506
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRI 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 40538794 507 TELQEKVTELESLLEETQAICREKEIQLESLRQREAE 543
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
573-753 |
6.46e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 573 QKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVA--QEEGTSQALREEAQRRDSALQQLRTAVKELSVQNQDLIEKNLTLQ 650
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 651 EHLRQAQPGSPPSPDTAQLalelhQELASCLQDLQAvcsivtqraqghdpNLSLLLGIHSAQHPEtqldlqkpdvikrkl 730
Cdd:COG3206 247 AQLGSGPDALPELLQSPVI-----QQLRAQLAELEA--------------ELAELSARYTPNHPD--------------- 292
|
170 180
....*....|....*....|...
gi 40538794 731 eeVQQLRRDIEDLRTTMSDRYAQ 753
Cdd:COG3206 293 --VIALRAQIAALRAQLQQEAQR 313
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
496-642 |
7.69e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 496 SQQL--KDSELKstELQEKVTELESLLeetqAICREKEIQLE-SLRQREAEFSSAgHSLQD--KQSVEETSGEGPEVEme 570
Cdd:PRK09039 45 SREIsgKDSALD--RLNSQIAELADLL----SLERQGNQDLQdSVANLRASLSAA-EAERSrlQALLAELAGAGAAAE-- 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40538794 571 swqKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAqeegtsqALREEAQRRDSALQQLRTAVKELSVQNQDL 642
Cdd:PRK09039 116 ---GRAGELAQELDSEKQVSARALAQVELLNQQIA-------ALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| Mrs2_Mfm1p-like |
cd12823 |
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like ... |
351-538 |
8.25e-03 |
|
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like family; A eukaryotic subfamily belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This functionally diverse subfamily includes the inner mitochondrial membrane Mg2+ transporters Saccharomyces cerevisiae Mfm1p/Lpe10p, Mrs2p, and human MRS2/ MRS2L. It also includes a family of Arabidopsis thaliana proteins (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of two EcCorA_ZntB-like family transporters: Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213357 Cd Length: 323 Bit Score: 39.15 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 351 ISQLEQKVRESELQVHSALLGRPAPFG----DVCLL-RLQELQRENTFLRAQFAQKTEALSREKI--------DLEKKLS 417
Cdd:cd12823 85 LEELQRRLASSNGSESESGGEDSLPFEfralEAALEeVCSHLEAELKRLEPEALPLLDELTDKIStsnlerllPLKRRLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 418 ASEVEVQLIRESLkvalqkhsEEVKKQEERVKGRdkhinNL-KKKCQKESEQNREKQQRIETLErYLadlptLEDHQKQS 496
Cdd:cd12823 165 ELETRVQKVRDAL--------EELLDDDEDMADM-----YLtDKAAGPERLESSRKEDDHEEVE-ML-----LEAYLQQV 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 40538794 497 QqlkdselkstELQEKVTELESLLEETQAICrekEIQLESLR 538
Cdd:cd12823 226 D----------ELLNKLEELREYIDDTEELI---NLILDSRR 254
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
398-655 |
8.33e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.02 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 398 FAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEErvkgrdkhinnLKKKCQKESEQNREKQQRIE 477
Cdd:pfam15905 29 FRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKE-----------LEKEIRALVQERGEQDKRLQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 478 TLEryladlptlEDHQKQSQQLKDSELKSTELQEKVTELESLLEET-------QAICREKEIQlESLRQREAEFSSAGHS 550
Cdd:pfam15905 98 ALE---------EELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellKAKFSEDGTQ-KKMSSLSMELMKLRNK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 551 LQDKQSVEETSGEGPEVEMESwqkrydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRT 630
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQV-------TQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260
....*....|....*....|....*...
gi 40538794 631 AVKELSVQNQDLIEKN---LTLQEHLRQ 655
Cdd:pfam15905 241 YKLDIAQLEELLKEKNdeiESLKQSLEE 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-651 |
8.82e-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: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 411 DLEKKLSASEVEV---QLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESeqnrekqQRIETLERYLADLP 487
Cdd:TIGR04523 37 QLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 488 TLEDHQKQSQQLKDSELKSTELQEK------------VTELESLLEETQAICREKEIQLESLRQREAEFSSAGHSLQ--- 552
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQkni 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 553 DKQSVEETSGEGPEVEMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQRRDSALQQL 628
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEinekTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260
....*....|....*....|...
gi 40538794 629 RTAVKELSVQNQDLIEKNLTLQE 651
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQ 292
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
381-676 |
9.40e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.29 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 381 LLRLQ--ELQRENTFL---RAQFAQKTEALSREKIDLEKK---LSASEVEVQLIRESLKVaLQKHSEEVKKQEERV---K 449
Cdd:pfam05622 63 LLQKQleQLQEENFRLetaRDDYRIKCEELEKEVLELQHRneeLTSLAEEAQALKDEMDI-LRESSDKVKKLEATVetyK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 450 GRDKHINNLKKKCQKESEQNREKQQRI----ETLERYLADLPTLEDHQKQSQQLK---DSELKSTELQEkvTELESLLEE 522
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLEERNAEYMQRTlqleEELKKANALRGQLETYKRQVQELHgklSEESKKADKLE--FEYKKLEEK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 523 TQAICREKE---IQLESLRQREAEFSsAGHSLQDKQSVEETSGEGPEVEMESWQKRYDSLQkIVEKQQQKmdQLRSQVQS 599
Cdd:pfam05622 220 LEALQKEKErliIERDTLRETNEELR-CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAE-IREKLIRL--QHENKMLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 600 LEQEVAQEE--GTSQALREEAQRRdsaLQQLRTavkELSVQNQDLIEKNLTLQEHLRQAQPGSPPSPDTAQLA--LELHQ 675
Cdd:pfam05622 296 LGQEGSYRErlTELQQLLEDANRR---KNELET---QNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKqkLEEHL 369
|
.
gi 40538794 676 E 676
Cdd:pfam05622 370 E 370
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
568-656 |
9.84e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.18 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538794 568 EMESWQKRYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT-----SQALREEAQRRDSALQQL-RTAVKELSVQNQD 641
Cdd:smart00935 12 ESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATlseaaREKKEKELQKKVQEFQRKqQKLQQDLQKRQQE 91
|
90
....*....|....*
gi 40538794 642 LIEKnltLQEHLRQA 656
Cdd:smart00935 92 ELQK---ILDKINKA 103
|
|
| |
