|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-662 |
2.40e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 487
Cdd:COG1196 231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 488 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 568 EAEFSSAGHSLQDKQSVEetsgegpevemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQR 647
Cdd:COG1196 381 LEELAEELLEALRAAAEL--------------AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250
....*....|....*
gi 1622825703 648 RDSALQQLRTAVKEQ 662
Cdd:COG1196 447 AAEEEAELEEEEEAL 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
410-667 |
1.66e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQREntflrAQFAQKTEALSREKIDLEKKLSASEVE-VQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:COG1196 201 QLEPLERQ-----AEKAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEkvtELESLLEETQAICRDRETQLESLRQRE 568
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEE---ELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 569 AEFSSAGHSLQDKQSVEETSgegpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRR 648
Cdd:COG1196 351 EELEEAEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250
....*....|....*....
gi 1622825703 649 DSALQQLRTAVKEQHSTQR 667
Cdd:COG1196 427 EEALAELEEEEEEEEEALE 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-669 |
1.88e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 366 EKELLIDKQRKHISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFAQkteaLSREKIDLEKKLSa 445
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEK------------ALAELRKELEELEEELEQ----LRKELEELSRQIS- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 446 sEVEVQLIRESLKValQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQ 525
Cdd:TIGR02168 730 -ALRKDLARLEAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL--KEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 526 LKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAEFSSAGHSLQDKQSVEETSgegpevemeswQK 601
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelSEDIESLAAEIEELEELIEEL-----------ES 873
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825703 602 QYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTA-----VKEQHSTQRLS 669
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRlegleVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-661 |
3.59e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 419 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 495
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 496 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 575
Cdd:TIGR02168 742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 576 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEK-------QQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRR 648
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250
....*....|...
gi 1622825703 649 DSALQQLRTAVKE 661
Cdd:TIGR02168 900 SEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-664 |
2.52e-11 |
|
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: 67.02 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 481
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 482 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 547
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 548 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 627
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622825703 628 EQEVAQEEGTSQALREE---AQRRDSALQQLRTAVKEQHS 664
Cdd:TIGR02169 433 EAKINELEEEKEDKALEikkQEWKLEQLAADLSKYEQELY 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-627 |
8.16e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGP 592
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270
....*....|....*....|....*....|....*
gi 1622825703 593 EVEMESWQKQYDSLqKIVEKQQQKMDQLRSQVQSL 627
Cdd:TIGR02168 495 ERLQENLEGFSEGV-KALLKNQSGLSGILGVLSEL 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-662 |
1.20e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 426 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 502
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 503 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQ 582
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 583 SVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQeegtsqaLREEAQRRDSALQQLRTAVKEQ 662
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-------LQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-632 |
4.10e-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: 63.12 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 352 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 426
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 427 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 507 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 584
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622825703 585 EETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVA 632
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-656 |
5.60e-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: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 309 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 388
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 389 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 469 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 548
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSgegpevemESWQKQYDSLQKIVEKQQQKMDQLRsqvqsLE 628
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL--------LEAEADYEGFLEGVKAALLLAGLRG-----LA 523
|
330 340
....*....|....*....|....*...
gi 1622825703 629 QEVAQEEGTSQALREEAQRRDSALQQLR 656
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNI 551
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-667 |
1.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 446 SEVEVQLirESLK----VALQ----KHSEEVKKQEERVKgrdkHINNLKKKCQKESEQNREKQQRIETLErylADLPTLE 517
Cdd:COG1196 196 GELERQL--EPLErqaeKAERyrelKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELE---AELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 518 -DHQKQSQQLKDSELKSTELQEKVTELESLLEETqaicrdrETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEM 596
Cdd:COG1196 267 aELEELRLELEELELELEEAQAEEYELLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622825703 597 ESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQHSTQR 667
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
374-616 |
2.54e-09 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 59.44 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 374 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 446
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 447 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 519
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 520 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQReaefssaghslqdkqsvEETSGEGPEVEME 597
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE-----------------YEEKEQTLNAELE 310
|
250
....*....|....*....
gi 1622825703 598 SWQKQYDSLQKIVEKQQQK 616
Cdd:pfam15905 311 ELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-630 |
2.73e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 305 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 382
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 383 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 462
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 463 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT-LEDHQKQSQQLKDSELKSTELQEKVT 541
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKeRDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 542 ELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSV-----EETSGEGP-----EVEMESWQKQYDSLQKIVE 611
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveEEIRALEPvnmlaIQEYEEVLKRLDELKEKRA 996
|
330
....*....|....*....
gi 1622825703 612 KQQQKMDQLRSQVQSLEQE 630
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-655 |
8.46e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 411 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADLPT--------LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 558
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKqlnqlkseISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 559 TQLESLRQreaefssaghSLQDKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTS 638
Cdd:TIGR04523 342 EQISQLKK----------ELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
250
....*....|....*..
gi 1622825703 639 QALREEAQRRDSALQQL 655
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELL 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-667 |
1.13e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQREntflrAQFAQKTEALSREKIDLEKKLSASEVEVQLI-RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR02168 201 QLKSLERQ-----AEKAERYKELKAELRELELALLVLRLEELREeLEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADLptleDHQKQ--SQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLrq 566
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRL----EQQKQilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 567 reaefssaghslqdkqsveetsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 646
Cdd:TIGR02168 350 --------------------------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260
....*....|....*....|.
gi 1622825703 647 RRDSALQQLRTAVKEQHSTQR 667
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIE 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-661 |
1.16e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 479 DKHINNLKKKCQKeSEQNREKQQRIETLERYLA--DLPTLEDHQKQSQ--------QLKDSELKSTELQEKVTELESLLE 548
Cdd:TIGR02168 199 ERQLKSLERQAEK-AERYKELKAELRELELALLvlRLEELREELEELQeelkeaeeELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 628
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190
....*....|....*....|....*....|...
gi 1622825703 629 QEVAQEEGTSQALREEAQRRDSALQQLRTAVKE 661
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-649 |
1.29e-08 |
|
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: 58.29 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 293 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 370
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 371 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 422
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 423 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 486
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 487 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 567 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE--------------VA 632
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLS 446
|
410
....*....|....*..
gi 1622825703 633 QEEGTSQALREEAQRRD 649
Cdd:pfam10174 447 EKERIIERLKEQRERED 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-646 |
1.61e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 420 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 495
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 496 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCRDRETQLESLRQREAEfssag 575
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE----- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622825703 576 hsLQDKQSVEEtsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 646
Cdd:COG4717 182 --LLEQLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-635 |
3.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 440
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 520
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 521 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQdkqsvEETSGEgpevEMESWQ 600
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-----EEHRKE----LLEEYT 458
|
250 260 270
....*....|....*....|....*....|....*
gi 1622825703 601 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE 635
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
410-665 |
5.77e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRE-NTFLRAQFAQK------TEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhi 482
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANrqrekeKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 483 nnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvteleslLEET 550
Cdd:pfam07888 113 --LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK-------LQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 551 QAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSL 627
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622825703 628 eqeVAQEEGTSQAL---REEAQRRDSALQQLRTAVKEQHST 665
Cdd:pfam07888 264 ---AAQRDRTQAELhqaRLQAAQLTLQLADASLALREGRAR 301
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
451-669 |
5.90e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 451 QLIRESLKVALQKHSEE-VKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQlkds 529
Cdd:COG4717 41 AFIRAMLLERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 530 ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKqsveetsgegpEVEMESWQKQYDSLQKI 609
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEL-----------EAELAELQEELEELLEQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622825703 610 V-EKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQHSTQRLS 669
Cdd:COG4717 186 LsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
361-634 |
9.07e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQeLQRENTFLRA-----QFAQKT-EALSR 434
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMS-LQRSMSTQKAleedlQIATKTiCQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 435 EKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE-------KQQRIETLE 507
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 508 RYLADLPTLEDHQKQSQQLKDsELKSTE------LQEKVTELESLLEETQAI----------CRDRETQLESLRQREAEF 571
Cdd:pfam05483 412 KILAEDEKLLDEKKQFEKIAE-ELKGKEqeliflLQAREKEIHDLEIQLTAIktseehylkeVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 572 SSAGH--SLQDKQSVEETSGEGPEV-----EMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQE 634
Cdd:pfam05483 491 TAHCDklLLENKELTQEASDMTLELkkhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
421-646 |
1.43e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 55.06 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 421 LRAQFAQKTEALSREKIDLEKKLSASEVEVQLiresLKVALQKHSEEVKKQEERVKGRDKHiNNLKKKCQKESEQNREkq 500
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMSTDALEQEI----LQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARRQ-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 501 qrIETLERYLADLPTLEDHQKQSQqLKDSELKSTELQEKVTELEslLEE-----TQAICRDR------------------ 557
Cdd:PRK10929 153 --LNEIERRLQTLGTPNTPLAQAQ-LTALQAESAALKALVDELE--LAQlsannRQELARLRselakkrsqqldaylqal 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 558 ETQLESLRQREAEfssagHSLQDKQSVEETSGEGPEVEMESWQKQYDsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGT 637
Cdd:PRK10929 228 RNQLNSQRQREAE-----RALESTELLAEQSGDLPKSIVAQFKINRE-LSQALNQQAQRMDLIASQQRQAASQTLQVRQA 301
|
....*....
gi 1622825703 638 SQALREEAQ 646
Cdd:PRK10929 302 LNTLREQSQ 310
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
493-662 |
1.57e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 493 SEQNREKQQRIETLERYLADLptledhqKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 572
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 573 SAGHSLQDKQSVEETSGEgpEVEMESwqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEG----TSQALREEAQRR 648
Cdd:COG3206 254 DALPELLQSPVIQQLRAQ--LAELEA---ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrilaSLEAELEALQAR 328
|
170
....*....|....
gi 1622825703 649 DSALQQLRTAVKEQ 662
Cdd:COG3206 329 EASLQAQLAQLEAR 342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
497-667 |
1.67e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 497 REKQQRIETLERYLADLptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFssagh 576
Cdd:COG4913 258 RELAERYAAARERLAEL----EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL----- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 577 slqdKQSVEETSGEgpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 656
Cdd:COG4913 329 ----EAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170
....*....|.
gi 1622825703 657 TAVKEQHSTQR 667
Cdd:COG4913 401 EALEEALAEAE 411
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
372-668 |
2.21e-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: 53.75 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 372 DKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQ 451
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 452 lireslkvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREK-QQRIETLERYLADLPTLEDHQKQ----SQQL 526
Cdd:pfam07888 140 --------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQrdtqVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 527 KDS----ELKSTELQEKVTELESLLEETQAIcRDR----ETQLESLRqreAEFSSAGhSLQDKQSVE---------ETSG 589
Cdd:pfam07888 212 QDTittlTQKLTTAHRKEAENEALLEELRSL-QERlnasERKVEGLG---EELSSMA-AQRDRTQAElhqarlqaaQLTL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 590 EGPEVEME------SWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE-AQRRDSALQQL---RTAV 659
Cdd:pfam07888 287 QLADASLAlregraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVElGREKDCNRVQLsesRREL 366
|
....*....
gi 1622825703 660 KEQHSTQRL 668
Cdd:pfam07888 367 QELKASLRV 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-652 |
2.50e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 427
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 428 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL--------QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN 496
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 497 REKqqrIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGH 576
Cdd:TIGR02169 832 EKE---IQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 577 SLQDKQSVEETsgegpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEE---------GTSQALREEAQR 647
Cdd:TIGR02169 900 ELERKIEELEA--------------QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVEE 965
|
....*
gi 1622825703 648 RDSAL 652
Cdd:TIGR02169 966 EIRAL 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
427-658 |
2.96e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 427 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 507 ERYLADLPTLEDHQKQSQQLK----DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSsaghSLQDKQ 582
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 583 SVEETSGEGPE------VEMESWQKQYDSLQkiVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLR 656
Cdd:PRK03918 355 EELEERHELYEeakakkEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
..
gi 1622825703 657 TA 658
Cdd:PRK03918 433 KA 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
498-667 |
6.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 498 EKQQRIETLERYLADLPT----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSS 573
Cdd:PRK02224 472 EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 574 AGhslqdkqsvEETSGEGPEVEMESwqkqyDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeegTSQALREEAQRRDSALQ 653
Cdd:PRK02224 552 EA---------EEKREAAAEAEEEA-----EEAREEVAELNSKLAELKERIESLERIR-----TLLAAIADAEDEIERLR 612
|
170
....*....|....
gi 1622825703 654 QLRTAVKEQHSTQR 667
Cdd:PRK02224 613 EKREALAELNDERR 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-643 |
7.15e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 440
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVkgrdKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhq 520
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 521 kqSQQLKDSELKSTELQEKVTELESLLEETQAICRDretqLESLRQREAEFSSAghsLQDKQSVEETSGEGPEVEMESWQ 600
Cdd:PRK03918 320 --EEEINGIEERIKELEEKEERLEELKKKLKELEKR----LEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622825703 601 KQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 643
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
408-656 |
9.76e-07 |
|
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: 52.26 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 408 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhinnlk 486
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTAR-------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 487 kkcqKESEQNREKQ---QRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQ-EKVTELESLLEETQAICRDRETQLE 562
Cdd:COG3096 499 ----ELLRRYRSQQalaQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 563 SLRQREAEFSSAGHSLQDKQsvEETSGEGPEvemesWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 642
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARI--KELAARAPA-----WLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERD 647
|
250
....*....|....
gi 1622825703 643 EEAQRRDSALQQLR 656
Cdd:COG3096 648 ELAARKQALESQIE 661
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
428-660 |
1.19e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 428 KTEAlSREKIDLEK-----KLSASEVEVqLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQR 502
Cdd:TIGR01612 1499 KDEA-DKNAKAIEKnkelfEQYKKDVTE-LLNKYSALAIKNKFAKTKKDSEIII---KEIKDAHKKFILEAEKSEQKIKE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 503 IETLERYLADLPTLEDH--------QKQSQQLKDSELKSTELQEKVTELeslLEETQAIcrDRETQLESLRQREAEFSSA 574
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKsnkaaidiQLSLENFENKFLKISDIKKKINDC---LKETESI--EKKISSFSIDSQDTELKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 575 GHSLQDKQSVeetsgegpeveMESWQKQydslQKIVEKQQQKMDQLRSQVQSLEQEVAQ-----EEGTSQALREEAQRRD 649
Cdd:TIGR01612 1649 GDNLNSLQEF-----------LESLKDQ----KKNIEDKKKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANK 1713
|
250
....*....|.
gi 1622825703 650 SALQQLRTAVK 660
Cdd:TIGR01612 1714 EEIESIKELIE 1724
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
361-662 |
1.45e-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: 51.66 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 439
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 440 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 519
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 520 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 595
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 596 MESWQK---QYDSLQKIVEKQQQkmDQLRSQVQSLEQEVAQEEGTSQalrEEAQRRDSALQQLRTAVKEQ 662
Cdd:pfam17380 501 LEERKQamiEEERKRKLLEKEME--ERQKAIYEEERRREAEEERRKQ---QEMEERRRIQEQMRKATEER 565
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
427-668 |
1.77e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 427 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 507 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 570
Cdd:PRK02224 320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 571 FSSAGHSLQD----KQSVEETSGE--GPEVEMESWQKqydSLQKIVEKQQQ---------------------KMDQLRSQ 623
Cdd:PRK02224 400 FGDAPVDLGNaedfLEELREERDElrEREAELEATLR---TARERVEEAEAlleagkcpecgqpvegsphveTIEEDRER 476
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622825703 624 VQSLEQEVAQeegtsqaLREEAQRRDSALQQLRTAVKEQHSTQRL 668
Cdd:PRK02224 477 VEELEAELED-------LEEEVEEVEERLERAEDLVEAEDRIERL 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-644 |
1.92e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 411 LQELQRENtflrAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEERVKG----RDKHINNLK 486
Cdd:TIGR04523 372 IEKLKKEN----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKEtiikNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 487 KKCQ------KESEQNREKQ-QRIETLER-YLADLPTLEDHQKQSQQlKDSELKS-----TELQEKVTELE---SLLEET 550
Cdd:TIGR04523 447 NQDSvkeliiKNLDNTRESLeTQLKVLSRsINKIKQNLEQKQKELKS-KEKELKKlneekKELEEKVKDLTkkiSSLKEK 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 551 QAICRDRETQLES-LRQREAEFSSAGHSLqdKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQ 629
Cdd:TIGR04523 526 IEKLESEKKEKESkISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
250
....*....|....*
gi 1622825703 630 EVAQEEGTSQALREE 644
Cdd:TIGR04523 604 EIEEKEKKISSLEKE 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-668 |
2.24e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 487
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 488 KCQKESEQNREKQQRIETLERYLADlptleDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrdretQLESLRQR 567
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKAD-----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK--------KADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 568 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEvAQEEGTSQALREEAQR 647
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEE 1402
|
250 260
....*....|....*....|.
gi 1622825703 648 RDSALQQLRTAVKEQHSTQRL 668
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEA 1423
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
472-660 |
2.97e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 472 EERVKGRDKHINNLKKKcqkESEQNREKQQRIETLeryladLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQ 551
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKK---NGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 552 AicrDRETQLESLrQREAEFSSAGHS----LQDKQSVEETSGEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQ---V 624
Cdd:PHA02562 265 A---KIKSKIEQF-QKVIKMYEKGGVcptcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEIMDEFNEQskkL 339
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622825703 625 QSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 660
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
423-655 |
3.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 423 AQFAQKTEALSREKIDLEKKLSASEV---------EVQLIRESLKV----ALQKHSEEVKKQEERVKGRDKHINNLKKKC 489
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 490 QKESEQNREK---QQRIETLERYLADLptledhQKQSQQLKDSELKstELQEKVTELESLLE---ETQAICRDRETQLES 563
Cdd:PRK03918 549 EKLEELKKKLaelEKKLDELEEELAEL------LKELEELGFESVE--ELEERLKELEPFYNeylELKDAEKELEREEKE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 564 LRQREAEFSSAGHSLQD-KQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 642
Cdd:PRK03918 621 LKKLEEELDKAFEELAEtEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
250
....*....|...
gi 1622825703 643 EEAQRRDSALQQL 655
Cdd:PRK03918 701 EELEEREKAKKEL 713
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
411-649 |
4.09e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 411 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCq 490
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 491 keSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAE 570
Cdd:pfam01576 422 --SESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825703 571 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVaqeEGTSQALREEAQRRD 649
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL---EALTQQLEEKAAAYD 569
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
365-661 |
4.77e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 365 KEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLE---K 441
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 442 KLSASEVEVQLIRE---SLKVALQKHSEEVKKQEERVKGRDKHINNLKK----------KCQKESEQNREK----QQRIE 504
Cdd:PRK02224 350 DADDLEERAEELREeaaELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREErdelREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 505 TLErylADLPTLEDHQKQSQQL-------------KDSELKST--ELQEKVTELESLL---EETQAICRDRETQLESLRQ 566
Cdd:PRK02224 430 ELE---ATLRTARERVEEAEALleagkcpecgqpvEGSPHVETieEDRERVEELEAELedlEEEVEEVEERLERAEDLVE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 567 REAEFSsaghSLQDKQsveetsgegpevemESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ 646
Cdd:PRK02224 507 AEDRIE----RLEERR--------------EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
330
....*....|....*...
gi 1622825703 647 R---RDSALQQLRTAVKE 661
Cdd:PRK02224 569 EareEVAELNSKLAELKE 586
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-567 |
4.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSREKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKK 488
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLELLEAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADL--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRET 559
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*...
gi 1622825703 560 QLESLRQR 567
Cdd:COG4913 427 EIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-649 |
4.98e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELlidKQRKHISQLEQKVRESElqvHSALLGRPAPfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLE 440
Cdd:PTZ00121 1549 DELKKAEEL---KKAEEKKKAEEAKKAEE---DKNMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 441 KKLSASEV-EVQLIRESLKVALQKHSEEVKKQEErVKGRDKHINNLKKKCQKESEQNREKQQRIETLEryladlptlEDH 519
Cdd:PTZ00121 1618 AKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE---------EDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 520 QKQSQQLKdselKSTELQEKVTELESLLEEtqaicrdRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESW 599
Cdd:PTZ00121 1688 KKAAEALK----KEAEEAKKAEELKKKEAE-------EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622825703 600 QKqydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRD 649
Cdd:PTZ00121 1757 KK----IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-660 |
6.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 466 EEVKKQEERVKGRDKHINNLKKKCQKESEQ-------NREKQQ--------RIETLERYL----ADLPTLEDHQKQSQQL 526
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKaeryqalLKEKREyegyellkEKEALERQKeaieRQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 527 KD-----------------------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQs 583
Cdd:TIGR02169 260 ISelekrleeieqlleelnkkikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 584 veetsgEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLE-------QEVAQEE--------------GTSQALR 642
Cdd:TIGR02169 339 ------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYRekleklkreinelkRELDRLQ 412
|
250
....*....|....*...
gi 1622825703 643 EEAQRRDSALQQLRTAVK 660
Cdd:TIGR02169 413 EELQRLSEELADLNAAIA 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
412-639 |
9.67e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 412 QELQRENTFLRAQFAQKT-EALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhseevkKQEERVKGRDKHINNLKKKCQ 490
Cdd:COG3206 159 EAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEAALEEFRQKNGLV---------DLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 491 KESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKD------------SELKST---------ELQEKVTELESLL-E 548
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlaeleaelAELSARytpnhpdviALRAQIAALRAQLqQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 549 ETQAICRDRETQLESLRQREAEFSsaghslQDKQSVEETSGEGPEVemeswQKQYDSLQKIVEKQQQKMDQLRSQVQSLE 628
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQ------AQLAQLEARLAELPEL-----EAELRRLEREVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 1622825703 629 QEVAQEEGTSQ 639
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-661 |
1.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 422 RAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVA--LQKHSEEVKKQEERVKGRD--KHINNLKKKCQkES 493
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKK--AEEKkkadEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAE-EA 1482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 494 EQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE-------LKSTELQEKVTELESLLEETQAicrDRETQLESLRQ 566
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkadeAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 567 REA--EFSSAGHSLQDKQSVEETSGEGPEVE---MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAL 641
Cdd:PTZ00121 1560 AEEkkKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260
....*....|....*....|
gi 1622825703 642 REEAQRRDSAlQQLRTAVKE 661
Cdd:PTZ00121 1640 KKEAEEKKKA-EELKKAEEE 1658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-662 |
1.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKlsASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNL 485
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--ADEAkkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 486 KKKCQKESEQNREKQQRIETLERylADLPTLEDHQKQSQQLKDSEL-KSTELQEKVTELESLLEETQAICRDRETQLESL 564
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 565 RQ----REAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKqydslqKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQA 640
Cdd:PTZ00121 1647 KKaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
250 260
....*....|....*....|..
gi 1622825703 641 LREEAQRRDSALQQLRTAVKEQ 662
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEED 1742
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
317-666 |
1.66e-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: 48.19 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 317 LELIRLQMEQMQLQNGAicHHPAAFAPslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 391
Cdd:pfam15921 564 IEILRQQIENMTQLVGQ--HGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 392 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 460
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 461 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 532
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 533 STELQEKVTELESLLEETQ---AICRDretqlesLRQREaEFSSAGHSLQDKQSVEETSGEGpevemeswqkqYDSLQKI 609
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASlqfAECQD-------IIQRQ-EQESVRLKLQHTLDVKELQGPG-----------YTSNSSM 859
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825703 610 VEKQQQKMDQLRSQ-----VQSLEQEVAQEEGTSQALREEAQRR-DSALQQLRTAVKEQHSTQ 666
Cdd:pfam15921 860 KPRLLQPASFTRTHsnvpsSQSTASFLSHHSRKTNALKEDPTRDlKQLLQELRSVINEEPTVQ 922
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-667 |
1.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 422 RAQFAQKTEALSR--EKIDLEKKLSASEV----EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQ 495
Cdd:PTZ00121 1517 KAEEAKKADEAKKaeEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 496 -----NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREAE 570
Cdd:PTZ00121 1597 vmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 571 FSSAGHSLQDKQSVEETSGEGPEVEMESwQKQYDSLQKIVEKQQQKMDQLRS-------QVQSLEQEVAQEEGTSQALRE 643
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKaeeenkiKAEEAKKEAEEDKKKAEEAKK 1751
|
250 260
....*....|....*....|....
gi 1622825703 644 EAQRRDSaLQQLRTAVKEQHSTQR 667
Cdd:PTZ00121 1752 DEEEKKK-IAHLKKEEEKKAEEIR 1774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
528-659 |
2.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 528 DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSS-AGHS--LQDKQSVEEtsgegpevEMESWQKQYD 604
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSwdEIDVASAER--------EIAELEAELE 678
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825703 605 SLQK---IVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAV 659
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
412-668 |
3.21e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 412 QELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKH---SEEVKKQEERVKgRDKHINNLKKK 488
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLK-KQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQRE 568
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 569 AEFSSagHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQ-- 646
Cdd:TIGR00618 349 TLHSQ--EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGql 426
|
250 260
....*....|....*....|....*
gi 1622825703 647 ---RRDSALQQLRTAVKEQHSTQRL 668
Cdd:TIGR00618 427 ahaKKQQELQQRYAELCAAAITCTA 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-661 |
4.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 309 ELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRES 388
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 389 ELQVHSALLGRPAPFgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEkklsasEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG4717 176 QEELEELLEQLSLAT----EEELQDLAEELEELQQRLAELEEELEEAQEELE------ELEEELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 469 KKQE------------------------------------------ERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:COG4717 246 KEARlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 507 ERY-------LADLPTLEDHQKQSQQL---KDSELKSTELQEKVTELESLLEETQAICRD----RETQLESLRQREAEFS 572
Cdd:COG4717 326 AALglppdlsPEELLELLDRIEELQELlreAEELEEELQLEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 573 SAGHSLQDKQSVEETSGEgpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgTSQALREEAQRRDSAL 652
Cdd:COG4717 406 ELEEQLEELLGELEELLE--ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE-EDGELAELLQELEELK 482
|
....*....
gi 1622825703 653 QQLRTAVKE 661
Cdd:COG4717 483 AELRELAEE 491
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
533-661 |
8.07e-05 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 44.92 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 533 STELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEgpEVEMESWQKQYDSLQKIVEK 612
Cdd:pfam13949 132 SPSVEEQVAKLRELLNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQE--EQLFEEELEKYDPLQNRLEQ 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622825703 613 QQQKMDQLRSQVQSLEQEVAQEegtSQALREEAQRRDSALQQLRTAVKE 661
Cdd:pfam13949 210 NLHKQEELLKEITEANNEFLQD---KRVDSEKQRQREEALQKLENAYDK 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
491-662 |
8.12e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 491 KESEQNREKQQRIETLERYLADLPTLEDHQKQ-----SQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLR 565
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrldelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 566 Q-REAEFSSAGHSLQDKQSVEETSGEgpevEMESWQKQYDSL-QKIVEKQQQKMDQLRSQVQSLE---QEVAQEEGTSQA 640
Cdd:TIGR02169 751 QeIENVKSELKELEARIEELEEDLHK----LEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEarlREIEQKLNRLTL 826
|
170 180
....*....|....*....|..
gi 1622825703 641 LREEAQRRDSALQQLRTAVKEQ 662
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQ 848
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-667 |
8.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 489
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 490 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 569
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 570 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKIVEkQQQKMDQLRSQVqslEQEVAQEEGTSQAlrEEAQRR 648
Cdd:PTZ00121 1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAE-EKKKADEAKKKA---EEAKKADEAKKKA--EEAKKA 1459
|
250
....*....|....*....
gi 1622825703 649 DSALQQLRTAVKEQHSTQR 667
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKK 1478
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
511-660 |
9.85e-05 |
|
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: 45.05 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 511 ADLPTLEDHQKQSQQLKDSELKS-TELQEKVTELESLLEETQAICRDRETQLESLRQReaefssaghsLQDKqsVEETSG 589
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEaKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA----------LKDL--LTDEGG 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 590 EGPEVEMESWQKQYDSLQK-IVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVK 660
Cdd:cd22656 175 AIARKEIKDLQKELEKLNEeYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
421-661 |
1.06e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 421 LRAQFAQKTEALSREKI-DLEKKLSASEVEVQLI----------RESLKVALQKHSEevKKQE-ERVKGRDKHINNLKKK 488
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLnGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEE--RREElETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKE----SEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 564
Cdd:PRK02224 270 TEREreelAEEVRDLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 565 RQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE 644
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
250
....*....|....*..
gi 1622825703 645 AQRRDSALQQLRTAVKE 661
Cdd:PRK02224 428 EAELEATLRTARERVEE 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
435-662 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 435 EKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKKKCQKESEQNREKQQRIETLERYLADLp 514
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD-ALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREELGER- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 515 tLEDHQKQSQQLKDSE--LKSTELQEKVTELESLleeTQAICRDRETqLESLRQREAEFSSAGHSLQDKQSVEETSgegp 592
Cdd:COG3883 92 -ARALYRSGGSVSYLDvlLGSESFSDFLDRLSAL---SKIADADADL-LEELKADKAELEAKKAELEAKLAELEAL---- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 593 EVEMESWQKQydsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQ 662
Cdd:COG3883 163 KAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
364-663 |
1.27e-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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 364 LKEKELLIDKQRKHISQLEQKVRESE--LQVHSALLGRPAPFGDVCLLRLQELQRENTFLRaQFAQKTEALsreKIDLEK 441
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKEraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEAL---KLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 442 KLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTL 516
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekvKLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 517 EDHQKQSQQLKDSELKSTELQEKV----TELESLLEETQAICRDRETQLESLR----QREAEFSSAGHSLQDK----QSV 584
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTrntlKSM 718
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825703 585 EETSGEGPEVEMeswqkqydSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDsalQQLRTAVKEQH 663
Cdd:pfam15921 719 EGSDGHAMKVAM--------GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKN 786
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
478-661 |
1.45e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 478 RDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---------------LEDHQKQSQQLKdsELKSTELQEKVTE 542
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtalttleeaLSEKERIIERLK--EQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 543 LESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSVEETSG-------EGPEVEMESWQKQYDSLQKIVEKQQQ 615
Cdd:pfam10174 470 LESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkdsklKSLEIAVEQKKEECSKLENQLKKAHN 545
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 616 KMDQLR------SQVQSLEQEVAQEegtsqalREEAQRRDSALQQLRTAVKE 661
Cdd:pfam10174 546 AEEAVRtnpeinDRIRLLEQEVARY-------KEESGKAQAEVERLLGILRE 590
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
410-564 |
1.53e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEErVKGRDKHINNLKKKC 489
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKE-YEALQKEIESLKRRI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825703 490 QKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDselKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAEL--EAELAELEAELEE---KKAELDEELAELEAELEELEA---EREELAAKI 172
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
423-654 |
1.54e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 423 AQFAQKTEALSREKIDLEKKLSAS-------EVEVQLIR------------ESLKVALQKHSEEvKKQEERVKGRDKHIN 483
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAqaahsqfEQAYQLVRkiagevsrseawDVARELLRRLREQ-RHLAEQLQQLRMRLS 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 484 NLkkkcqkesEQNREKQQRietLERYLADLptledHQKQSQQLKDSElkstelqekvtELESLLEETQAICRDRETQLES 563
Cdd:PRK04863 524 EL--------EQRLRQQQR---AERLLAEF-----CKRLGKNLDDED-----------ELEQLQEELEARLESLSESVSE 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 564 LRQREAEFSsagHSLQD-KQSVEETSGEGPEvemesWQKQYDSLQKIVE------KQQQKMDQLRSQVQSLEQEVAQEEG 636
Cdd:PRK04863 577 ARERRMALR---QQLEQlQARIQRLAARAPA-----WLAAQDALARLREqsgeefEDSQDVTEYMQQLLERERELTVERD 648
|
250
....*....|....*...
gi 1622825703 637 TSQALREEAQRRDSALQQ 654
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
430-566 |
1.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 430 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 509
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825703 510 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
365-574 |
1.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 365 KEKELL--IDKQRKHISQLEQKVRESELQVhsALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKK 442
Cdd:COG4942 49 EEKALLkqLAALERRIAALARRIRALEQEL--AALEA----------ELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 443 LSASEVEVQLIRESLKVALQKhseeVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQ 522
Cdd:COG4942 117 GRQPPLALLLSPEDFLDAVRR----LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL--EEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 523 SQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSA 574
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
376-660 |
2.12e-04 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 43.87 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 376 KHISQLEQKVRESELQVHSALLGRPAPFgDVCLLRLQELQRENTFLRAQFAQKTEALsREKIDLEKKLSASEVEVQLIRE 455
Cdd:cd08915 45 ASIDDLQKPENLPDSIQHSQEIIEEGGL-DNIEQSFKELSKLRQNVEELLQECEELL-EEEAAEDDQLRAKFGTLRWRRP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 456 SLKVALQKHSEEVkkqeervkgrdkhiNNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELkSTE 535
Cdd:cd08915 123 SSDEAAKELYEKV--------------TKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPAL-DPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 536 LQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAghslqdkQSVEETSGEGPEVEMES-WQKQ---YDSLQKIVE 611
Cdd:cd08915 188 VSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDIL-------PKLITEYKKNGTTEFEDlFEEHlkkFDKDLTYVE 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622825703 612 KQQQKMDQLRSQVQSLEQEVAQEEGTSqalrEEAQRRDSALQQLRTAVK 660
Cdd:cd08915 261 KTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYK 305
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
410-644 |
2.30e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQElQRENtfLRAQFAQKTEALSREKIDLEKKLSASEVEVQLiRESLKVALQKH-----SEEVKKQ----------EER 474
Cdd:pfam10174 454 RLKE-QRER--EDRERLEELESLKKENKDLKEKVSALQPELTE-KESSLIDLKEHasslaSSGLKKDsklksleiavEQK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 475 VKGRDKHINNLKKKCQKESEQ--NREKQQRIETLERylaDLPTLEDHQKQSQQ--------LKDSELKSTELQEKVTELE 544
Cdd:pfam10174 530 KEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQ---EVARYKEESGKAQAeverllgiLREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 545 SLleeTQAICRDRETQLESLRQREAEFSSAGHSLqdkqsVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQV 624
Cdd:pfam10174 607 SL---TLRQMKEQNKKVANIKHGQQEMKKKGAQL-----LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARL 678
|
250 260
....*....|....*....|
gi 1622825703 625 QSLEQEVAQEEGTSQALREE 644
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAE 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
490-663 |
2.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 490 QKESEQNREK-QQRIETLERYLADlpTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQRE 568
Cdd:COG4942 22 AAEAEAELEQlQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 569 AEFSsagHSLQDKQSVEETSGEGPEVEM----ESWQKQYDS---LQKIVEKQQQKMDQLRSQVQSLEQevaqeegtsqaL 641
Cdd:COG4942 100 EAQK---EELAELLRALYRLGRQPPLALllspEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAA-----------L 165
|
170 180
....*....|....*....|..
gi 1622825703 642 REEAQRRDSALQQLRTAVKEQH 663
Cdd:COG4942 166 RAELEAERAELEALLAELEEER 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
310-669 |
2.62e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 310 LSTCRQQLELI--RLQmEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLK---EKELLIDKQ-------RKH 377
Cdd:TIGR00618 302 VTQIEQQAQRIhtELQ-SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRdahEVATSIREIscqqhtlTQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 378 ISQLEQKVR--ESELQVHSALLgrpapfgdvclLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRE 455
Cdd:TIGR00618 381 IHTLQQQKTtlTQKLQSLCKEL-----------DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 456 SLKVALQKHSEEVKKQEeRVKGRDKHINNLKKKCQKESEQNREKQQRIETL----------------ERYLADLPT---- 515
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQ-SLKEREQQLQTKEQIHLQETRKKAVVLARLLELqeepcplcgscihpnpARQDIDNPGpltr 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 516 -----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQ------AICRDRETQ-LESLRQREAEFSsagHSLQDKQS 583
Cdd:TIGR00618 529 rmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEdIPNLQNITVRLQ---DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 584 VEETSGEGPEVEMESWQKQYDSLQKIVEKQQ--QKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKE 661
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKM 685
|
....*...
gi 1622825703 662 QHSTQRLS 669
Cdd:TIGR00618 686 QSEKEQLT 693
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
410-665 |
2.63e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQREntflRAQFAQKTEALSrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLK 486
Cdd:PRK02224 476 RVEELEAE----LEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 487 KKCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselkSTELQEKVTELESL--LEETQAICRDRETQLESL 564
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAEL-------------------NSKLAELKERIESLerIRTLLAAIADAEDEIERL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 565 RQREAEFSSAGHSLQDKQS-----VEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQ 639
Cdd:PRK02224 612 REKREALAELNDERRERLAekrerKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
250 260 270
....*....|....*....|....*....|..
gi 1622825703 640 ALREEAQRRDS------ALQQLRTAVKEQHST 665
Cdd:PRK02224 692 ELEELRERREAlenrveALEALYDEAEELESM 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
501-661 |
2.69e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 501 QRIETLERYLADLPtledhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 580
Cdd:COG1579 17 SELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 581 KQSVEETSGEgpeveMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEgtsQALREEAQRRDSALQQLRTAVK 660
Cdd:COG1579 88 NKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELE 159
|
.
gi 1622825703 661 E 661
Cdd:COG1579 160 E 160
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
494-654 |
3.27e-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: 42.43 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 494 EQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSE-LKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEF 571
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHeERVEALNELGEQLIEEGhPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 572 SSAGHSLQ---DKQSVEETSGEGPEVE-MESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTS--------- 638
Cdd:cd00176 113 RDADDLEQwleEKEAALASEDLGKDLEsVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEieekleeln 192
|
170
....*....|....*....
gi 1622825703 639 ---QALREEAQRRDSALQQ 654
Cdd:cd00176 193 erwEELLELAEERQKKLEE 211
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
471-663 |
3.54e-04 |
|
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: 43.79 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 471 QEERVKGRDKHINNLKKKCQKESEQNREKQQRIE---TLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLL 547
Cdd:COG5185 273 NAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 548 EETQAICRDRETQLES---LRQREAEFSSAGHSLqdkqsveETSGEGPEVEMESWQKQYDSLQKIVEK----QQQKMDQL 620
Cdd:COG5185 353 TENLEAIKEEIENIVGeveLSKSSEELDSFKDTI-------ESTKESLDEIPQNQRGYAQEILATLEDtlkaADRQIEEL 425
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622825703 621 RSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQH 663
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEA 468
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
411-546 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 411 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 491 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 546
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
454-667 |
3.61e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 454 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ---KESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQL 526
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEaisQASRKLRETQNTLNQLNKQIDELNAsiakLEQQQAAQERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 527 KDSELKSTELQEKVTELESLL--EETQAICR----------DRETQLESLRQREAEFSSAGHSLQDKQSVEET------- 587
Cdd:PRK11637 126 LAAQLDAAFRQGEHTGLQLILsgEESQRGERilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTllyeqqa 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 588 SGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQAlREEAQRRDSAlqqlRTAVKEQHSTQR 667
Cdd:PRK11637 206 QQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKA-RAEREAREAA----RVRDKQKQAKRK 280
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
438-619 |
4.16e-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: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 438 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 513
Cdd:cd00176 18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 514 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRD---RETQLESLRQREAEFSSA 574
Cdd:cd00176 96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622825703 575 GHSLQDKQSveetsgegpEVEMESWQKQYDSLQKIVEKQQQKMDQ 619
Cdd:cd00176 176 GHPDADEEI---------EEKLEELNERWEELLELAEERQKKLEE 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-663 |
5.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 357 LNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTFLRAQFAQKTEALSREK 436
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 437 IDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN-------------------- 496
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 497 -------------------------------REKQQRIETLERyLADLPTLED--HQKQSQQLKDSELKSTELQEKVTEL 543
Cdd:COG4717 264 lggsllsliltiagvlflvlgllallflllaREKASLGKEAEE-LQALPALEEleEEELEELLAALGLPPDLSPEELLEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 544 ESLLEETQAICRDRETQLESLRQREAEfssaghslQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQ 623
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELE--------QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622825703 624 VQSLEQEVaqEEGTSQALREEAQRRDSALQQLRTAVKEQH 663
Cdd:COG4717 415 LGELEELL--EALDEEELEEELEELEEELEELEEELEELR 452
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
439-629 |
5.46e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 439 LEKKLSAS----EVEVQLIR-ESLKVALQKHSEEVKKQEERVKGRDKHINNlkKKCQKESEQNREKQQRIETLERYLAdl 513
Cdd:COG2433 355 VEKKVPPDvdrdEVKARVIRgLSIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVE-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 514 ptledhqkqsqqlkdselkstELQEKVTELESLLEEtqaicrdRETQLESLRQREaefssaghslqdKQSVEEtsgegpE 593
Cdd:COG2433 431 ---------------------ELEAELEEKDERIER-------LERELSEARSEE------------RREIRK------D 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622825703 594 VEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQ 629
Cdd:COG2433 465 REISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
449-667 |
5.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 449 EVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLadlptledhQKQSQQLKD 528
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL---------EQARSELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 529 SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQK 608
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825703 609 IVEKQQQKMDQLRSQVQSLEQEVAQEEgtSQALREEAQRRDSALQQLRTAVKEQHSTQR 667
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQA--LDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
465-590 |
5.95e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 41.87 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 465 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 544
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622825703 545 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 590
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
564-658 |
6.87e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.76 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 564 LRQREAEFssaghslqdKQSVEETSGEgPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 643
Cdd:pfam11559 46 QRDRDLEF---------RESLNETIRT-LEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKE 115
|
90
....*....|....*
gi 1622825703 644 EAQRRDSALQQLRTA 658
Cdd:pfam11559 116 ELQRLKNALQQIKTQ 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
411-661 |
7.55e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 411 LQELQRENTFLRAQFAQKTEALSREKIDLEKKLsasEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKI---ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 491 KESEQNREKQ----QRIETLERYLADLPTLEDHQKQSQQLKDSELK------STELQEKVTELESLLEETQAICRDRETQ 560
Cdd:pfam15921 303 IIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEkqlvlaNSELTEARTERDQFSQESGNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 561 LESLRQREAEFSSAGHslQDKQSVEETSGEgpEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ-SLEQEVAQEEGTSQ 639
Cdd:pfam15921 383 LADLHKREKELSLEKE--QNKRLWDRDTGN--SITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNE 458
|
250 260
....*....|....*....|....*
gi 1622825703 640 ALREEAQ---RRDSALQQLRTAVKE 661
Cdd:pfam15921 459 SLEKVSSltaQLESTKEMLRKVVEE 483
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
409-667 |
8.13e-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: 42.73 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 409 LRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL--ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 -------CQKESEQNREKQQRIETLERYLADLPT----LEDHQKQSQQLKD-----SELKSTELQEKVTELESLLEETQA 552
Cdd:TIGR00606 676 nqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDklksTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNKLQK 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 553 ICRD----------RETQLESLRqreAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQ-----------KQYDSLQKIVE 611
Cdd:TIGR00606 756 VNRDiqrlkndieeQETLLGTIM---PEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdldRTVQQVNQEKQ 832
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 612 KQQQKMDQLRSQVQSLEQEVAQEEGTSQALR--------------EEAQRRDSALQQLRTAVKEQHSTQR 667
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktnelkseklqigTNLQRRQQFEEQLVELSTEVQSLIR 902
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
410-666 |
9.49e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSREKIDLE-------KKLSASEVEVQLIRESLkvalQKHSEEVKKQEERVKGRDKHI 482
Cdd:pfam07111 152 QLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAELLRKQL----SKTQEELEAQVTLVESLRKYV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 483 NNLKKKCQKESEQNREKQQRIETLERYLAD----LPTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRD- 556
Cdd:pfam07111 228 GEQVPPEVHSQTWELERQELLDTMQHLQEDradlQATVELLQVRVQSLTHMlALQEEELTRKIQPSDSLEPEFPKKCRSl 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 557 ----RETQLESLRQREAEfssaghSLQDKQSVEETSGEGPEVEME--SWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE 630
Cdd:pfam07111 308 lnrwREKVFALMVQLKAQ------DLEHRDSVKQLRGQVAELQEQvtSQSQEQAILQRALQDKAAEVEVERMSAKGLQME 381
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622825703 631 VAQEEgtsQALREEAQRRDSALQQLRTAVKEQHSTQ 666
Cdd:pfam07111 382 LSRAQ---EARRRQQQQTASAEEQLKFVVNAMSSTQ 414
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
439-664 |
1.27e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 439 LEKKLSASEVEVQLIRESLKVALQKHSEEVkkqeERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLED 518
Cdd:pfam15921 431 LEALLKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 519 HQKQSQQLKDSE---------LKSTELQEKVTElESLLEETQAICR-------DRETQLESLRQREAEFS--------SA 574
Cdd:pfam15921 507 EKERAIEATNAEitklrsrvdLKLQELQHLKNE-GDHLRNVQTECEalklqmaEKDKVIEILRQQIENMTqlvgqhgrTA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 575 GHSLQDKQSVEEtsgegpevEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQE----VAQEEGTSQALREEAQRRDS 650
Cdd:pfam15921 586 GAMQVEKAQLEK--------EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQ 657
|
250
....*....|....
gi 1622825703 651 ALQQLRTAVKEQHS 664
Cdd:pfam15921 658 LLNEVKTSRNELNS 671
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-567 |
1.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 454 RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---LEDHQKQSQQLK--- 527
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeYEALQKEIESLKrri 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622825703 528 -DSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG1579 106 sDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
453-666 |
1.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 453 IRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKcqkESEQNREKQQRIETLERYLADL-PTLEDHQKQSQQLKDSEL 531
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNKIESArADLEDIKIKINELKDKHD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 532 KSTELQE-----KVTELESLLEE-TQAICRDRETQLESLRQREAEFSSAGHSLQDKqsVEETSGEGPEV---------EM 596
Cdd:PRK01156 547 KYEEIKNrykslKLEDLDSKRTSwLNALAVISLIDIETNRSRSNEIKKQLNDLESR--LQEIEIGFPDDksyidksirEI 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825703 597 ESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE---EAQRRDSALQQLRTAVKEQHSTQ 666
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANR 697
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
445-665 |
1.78e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 445 ASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLADlpTLEDHQK 521
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREetfARTALKNARLDLRRLFDEKQSEKD--KKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 522 QSQQLKDSELKSTELQEKVTELE--SLLEETQAICRDRETQ-LESLRQREAEFSSAGHSLQDKQSVEETsgeGPEVEMES 598
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKhqAWLEEQKEQKREARTEkQAYWQVVEGALDAQLALLKAAIAARRS---GAKAELKA 751
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825703 599 WQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQHST 665
Cdd:pfam12128 752 LETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSN 818
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
428-567 |
1.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 428 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 507
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 508 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 567
Cdd:PRK12704 117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-643 |
2.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 354 ISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKT-EAL 432
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYE--------------------EAKAKKEELERLKKRLTGLTpEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 433 SREKIDLEKKlsasevevqliRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNRE--KQQRIETLERYL 510
Cdd:PRK03918 390 EKELEELEKA-----------KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 511 ADLPTLEdhqkqsQQLKDSELKSTELQEKVTELESLLEETQAICRDRET--QLESLRqreaefssaghslqdkqsvEETS 588
Cdd:PRK03918 459 AELKRIE------KELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELE-------------------EKLK 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622825703 589 GEGPEvEMESWQKQYdslqkivEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALRE 643
Cdd:PRK03918 514 KYNLE-ELEKKAEEY-------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-662 |
2.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 408 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 484
Cdd:COG4372 37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 485 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicRDRETQLESL 564
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 565 RqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE 644
Cdd:COG4372 189 L-KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250
....*....|....*...
gi 1622825703 645 AQRRDSALQQLRTAVKEQ 662
Cdd:COG4372 268 LVEKDTEEEELEIAALEL 285
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
427-667 |
2.07e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 427 QKTEALSREKIDLEKKLSASEVEVQLIRESLKValqkhseevkkQEERVKGRDKHINNLKKKCQKESEQNrekqQRIETL 506
Cdd:pfam05557 111 NELSELRRQIQRAELELQSTNSELEELQERLDL-----------LKAKASEAEQLRQNLEKQQSSLAEAE----QRIKEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 507 ERYLAdlptledhqkqsQQLKDSEL--KSTELQEKVTELESLLE----------ETQAICRDRETQLESLRQREAEFSSA 574
Cdd:pfam05557 176 EFEIQ------------SQEQDSEIvkNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRKLEREEKY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 575 ghslQDKQSVEETSGEGPEVEMESWQKQY----------DSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREE 644
Cdd:pfam05557 244 ----REEAATLELEKEKLEQELQSWVKLAqdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
250 260
....*....|....*....|...
gi 1622825703 645 AQRRDSALQQLRTAVKEQHSTQR 667
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVR 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-667 |
2.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 420 FLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHS-EEVKKQEERVKGRDKHINNLkkkcQKESEQNRE 498
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEEL----EEELQLEEL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 499 KQQRIETLERYLA-DLPTLEDHQKQSQQLKdselkstELQEKVTELESLLEEtqaicrdretqleslrqrEAEFSSAGHS 577
Cdd:COG4717 369 EQEIAALLAEAGVeDEEELRAALEQAEEYQ-------ELKEELEELEEQLEE------------------LLGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 578 LQDKQSVEETSGEgPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQ--VQSLEQEVAQEEGTSQALREEAQRRDSALQQL 655
Cdd:COG4717 424 ALDEEELEEELEE-LEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELL 502
|
250
....*....|..
gi 1622825703 656 RTAVKEQHSTQR 667
Cdd:COG4717 503 EEAREEYREERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
500-668 |
2.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 500 QQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAIcRDRETQLESLRQREAEfssaghslq 579
Cdd:COG4913 609 RAKLAALEAELAEL--EEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAE--------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 580 dKQSVEETSGEgpeveMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQeegtSQALREEAQRRDSALQQLRTAV 659
Cdd:COG4913 677 -LERLDASSDD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLE 746
|
....*....
gi 1622825703 660 KEQHSTQRL 668
Cdd:COG4913 747 LRALLEERF 755
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
420-666 |
2.71e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 420 FLRAQFAQK--TEALSREKIDLEKKLSASEVEVQLIRESLKVALqkhseEVKKQEERVKgrdKHINNLKKKCQKESEQNR 497
Cdd:PRK11281 26 FARAASNGDlpTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTL-----ALLDKIDRQK---EETEQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 498 EKQQRIETLERYLADlPTLEDHQKQSQqlkdselksTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAEFSS 573
Cdd:PRK11281 98 QAQAELEALKDDNDE-ETRETLSTLSL---------RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 574 AGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQ---QQKMDQLRSQVQSLEQevAQEEGTSqalrEEAQRRDS 650
Cdd:PRK11281 168 NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQndlQRKSLEGNTQLQDLLQ--KQRDYLT----ARIQRLEH 241
|
250
....*....|....*.
gi 1622825703 651 ALQQLRTAVKEQHSTQ 666
Cdd:PRK11281 242 QLQLLQEAINSKRLTL 257
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
516-647 |
2.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 516 LEDHQKQSQQLKdsELKSTELQEKVTELESLLEETqaiCRDRETQL----ESLRQREAEFSSAGHSLQDKqsveetsgeg 591
Cdd:PRK12704 44 LEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKE---LRERRNELqkleKRLLQKEENLDRKLELLEKR---------- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825703 592 pEVEMESWQKQYDSLQKIVEKQQQKMDQLRS-QVQSLEqEVA---QEEGTSQAL---REEAQR 647
Cdd:PRK12704 109 -EEELEKKEKELEQKQQELEKKEEELEELIEeQLQELE-RISgltAEEAKEILLekvEEEARH 169
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
410-655 |
3.05e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEAL--SREKIDLEKKLsASEVEVqLIRESLKVALQKHSEEVKKQEER---VKGRDKHINN 484
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLeqAKEGLSALNRL-LPRLNL-LADETLADRVEEIREQLDEAEEAkrfVQQHGNALAQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 485 LKK-------------KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSElKSTELQEKvteLESLLEETQ 551
Cdd:PRK04863 923 LEPivsvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLA-KNSDLNEK---LRQRLEQAE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 552 AicrDRETQLESLRQREAEFSSAGHSLQDKQSveetsgegpevemeswqkQYDSLQKIVEKQQQKMDQLRSQVQS--LEQ 629
Cdd:PRK04863 999 Q---ERTRAREQLRQAQAQLAQYNQVLASLKS------------------SYDAKRQMLQELKQELQDLGVPADSgaEER 1057
|
250 260
....*....|....*....|....*.
gi 1622825703 630 EVAQEEGTSQALREEAQRRDSALQQL 655
Cdd:PRK04863 1058 ARARRDELHARLSANRSRRNQLEKQL 1083
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
422-665 |
3.12e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 422 RAQFAQKTEALSREKIDLEKKLSASEVEvqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ------KESEQ 495
Cdd:pfam03528 132 RAQWNQYRESAEREIADLRRRLSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTeaedkiKELEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 496 NR----------EKQQRIEtLERYLADLPT-----LEDHQKQSQQLKDSELKSTELQEKVTEL--------ESLLEETQA 552
Cdd:pfam03528 207 SKmkelnhyleaEKSCRTD-LEMYVAVLNTqksvlQEDAEKLRKELHEVCHLLEQERQQHNQLkhtwqkanDQFLESQRL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 553 ICRDR---ETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVE-------KQQQKMDQLRS 622
Cdd:pfam03528 286 LMRDMqrmESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVetsaplsNVEEQINSAHG 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622825703 623 QVQSLEQEVAQEEGTSQALRE----EAQRRDSALQQLRTAVKEQHST 665
Cdd:pfam03528 366 SVHSLDTDVVLGAGDSFNKQEdpfkEGLRRAQSTDSLGSSSSLQHKF 412
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
410-658 |
3.94e-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: 40.59 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKK-- 487
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 488 -----KCQK-ESEQNREKQQRIETLERYLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaicrDRETQL 561
Cdd:pfam12128 364 kaltgKHQDvTAKYNRRRSKIKEQNNRDIAGI-----KDKLAKIREARDRQLAVAEDDLQALESELRE------QLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 562 ESLRQREAEFSSAGHSLQDKQSVEETSgegPEVEMEswQKQYDSLqkiVEKQQQKMDQLRSQVQSLEQEVAQEEGtsqal 641
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATAT---PELLLQ--LENFDER---IERAREEQEAANAEVERLQSELRQARK----- 499
|
250
....*....|....*..
gi 1622825703 642 reeaqRRDSALQQLRTA 658
Cdd:pfam12128 500 -----RRDQASEALRQA 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
497-648 |
3.97e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 497 REKQQRIETLERYLADLPtlEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRetqLESLRQREAEFSSAGH 576
Cdd:PRK04863 840 RQLNRRRVELERALADHE--SQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA---DR---VEEIREQLDEAEEAKR 911
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 577 SLQDKQsveetsgegpeVEMESWQKQYDSLQKivekQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRR 648
Cdd:PRK04863 912 FVQQHG-----------NALAQLEPIVSVLQS----DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRR 968
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-662 |
4.14e-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: 39.52 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 511 ADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAghsLQDKQSVEETSge 590
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKY-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825703 591 gpEVEMESW--QKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDSALQQLRTAVKEQ 662
Cdd:COG1579 79 --EEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
361-648 |
4.15e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 361 EHLLKEKELLidkQRKhISQLEQKVRESELQVHSALLGRpapfgdvclLRLQELQRENTFLRAQFAQKTEALSREKIDLE 440
Cdd:PLN02939 159 EKILTEKEAL---QGK-INILEMRLSETDARIKLAAQEK---------IHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKgrdkhinNLKKKCQKESEQNREkqqrietLERYLADlptledhq 520
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQ-FLKAELIEVAETEERVF-------KLEKERSLLDASLRE-------LESKFIV-------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 521 KQSQQLKDSELKSTELQEKVTELESLLEETQaicrDRETQLESLRQREaefssagHSLQDKQSVEETSGEGPEVEMESWQ 600
Cdd:PLN02939 283 AQEDVSKLSPLQYDCWWEKVENLQDLLDRAT----NQVEKAALVLDQN-------QDLRDKVDKLEASLKEANVSKFSSY 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622825703 601 KqYDSLQ---KIVEKQQQKMDQ-LRSQVQSLEQEVAQEEGTSQALREEAQRR 648
Cdd:PLN02939 352 K-VELLQqklKLLEERLQASDHeIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
493-665 |
4.40e-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: 40.23 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 493 SEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSelkSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 572
Cdd:pfam09730 265 SEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGA---LSEQQEKVNRLTENLEAMRGLQASKERQDALDSEKDRDSH 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 573 SAGHS----------LQDKQSVEETSGEGPEVEMESWQKQYdslQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALR 642
Cdd:pfam09730 342 EDGDYyevdingpeiLECKYRVAVEEAGELREELKALKARY---NTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQ 418
|
170 180
....*....|....*....|...
gi 1622825703 643 EEAQRRDSALQQLRTAVKEQHST 665
Cdd:pfam09730 419 ERIAHLEKELGKTRKVAGESEGS 441
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
410-669 |
5.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 410 RLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEvevQLIRESLKVALQKHSE-EVKKQEERVKGRDKHINNLKKK 488
Cdd:PRK04863 787 RIEQLRAE----REELAERYATLSFDVQKLQRLHQAFS---RFIGSHLAVAFEADPEaELRQLNRRRVELERALADHESQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 CQKESEQNREKQQRIETLERYLADLPTLEDhqkqsqqlkdselksTELQEKVTELESLLEETQAICRDRETQLESLRQRE 568
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALNRLLPRLNLLAD---------------ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 569 AEFSsaghSLQdkqsveetsgEGPEvEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQ------------SLEQEVAQEEG 636
Cdd:PRK04863 925 PIVS----VLQ----------SDPE-QFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyedaaeMLAKNSDLNEK 989
|
250 260 270
....*....|....*....|....*....|....*
gi 1622825703 637 TSQALREEAQRRDSALQQLRTAvKEQHS--TQRLS 669
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQA-QAQLAqyNQVLA 1023
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
490-654 |
5.68e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 490 QKESEQNREKQQRiETLERYLADL----------PTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRET 559
Cdd:pfam12128 208 DDGVVPPKSRLNR-QQVEHWIRDIqaiagimkirPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 560 QLES-LRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKI-VEK---QQQKMDQLRSQVQSLEQEVAQE 634
Cdd:pfam12128 287 ELNQlLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETaaaDQEQLPSWQSELENLEERLKAL 366
|
170 180
....*....|....*....|
gi 1622825703 635 EGTSQALREEAQRRDSALQQ 654
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKE 386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
482-661 |
6.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 482 INNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELE---SLLEETQAICRDRE 558
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 559 TQLESLRQREAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKIVE-KQQQKMDQLRSQVQSLEQEVAQEEGT 637
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....
gi 1622825703 638 SQALREEAQRRDSALQQLRTAVKE 661
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEE 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-549 |
7.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 354 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 428
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 429 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 485
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825703 486 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 549
Cdd:PRK03918 693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
499-658 |
7.15e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 499 KQQRIETLERYLADlptledhQKQSQQLKDSELKSTELQEKVtELESLLEE--------TQAICRDRETQLESLrQREAE 570
Cdd:pfam05667 241 RKRKRTKLLKRIAE-------QLRSAALAGTEATSGASRSAQ-DLAELLSSfsgssttdTGLTKGSRFTHTEKL-QFTNE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 571 FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQALREEAQRRDS 650
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
|
....*...
gi 1622825703 651 ALQQLRTA 658
Cdd:pfam05667 392 TLDLLPDA 399
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
423-661 |
8.28e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 38.75 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 423 AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQ-EERVKGRDK---HINNL-------KKKCQK 491
Cdd:pfam00038 14 ASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQlDTLTVERARlqlELDNLrlaaedfRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 492 ESEQNREKQQRIETLERYLADLpTLE--DHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQ--------------AIC 554
Cdd:pfam00038 94 ELNLRTSAENDLVGLRKDLDEA-TLArvDLEAKIESLKEElAFLKKNHEEEVRELQAQVSDTQvnvemdaarkldltSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 555 RDRETQLESLRQReaefssaghslqDKQSVEETsgegpevemesWQKQYDSLQKIVEKQ-------QQKMDQLRSQVQSL 627
Cdd:pfam00038 173 AEIRAQYEEIAAK------------NREEAEEW-----------YQSKLEELQQAAARNgdalrsaKEEITELRRTIQSL 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622825703 628 EQEVAQEEGTSQAL----REEAQRRDSALQQLRTAVKE 661
Cdd:pfam00038 230 EIELQSLKKQKASLerqlAETEERYELQLADYQELISE 267
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
412-567 |
8.52e-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: 37.96 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 412 QELQRENTFLRAQFAQKT---EALSREKIDLEKKLSASEVEVQLIRESLKVAlQKHSEEVKKQEERVKGRDKHINNLKKk 488
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLENY-EKDKQSLKNLKARLKVLEKELKDLKW- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 489 cqkeseQNREKQQRIETLERylaDLPTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEEtqaicrdRETQLESLRQ 566
Cdd:pfam13851 107 ------EHEVLEQRFEKVER---ERDELYDKFEAAIQdvQQKTGLKNLLLEKKLQALGETLEK-------KEAQLNEVLA 170
|
.
gi 1622825703 567 R 567
Cdd:pfam13851 171 A 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-549 |
8.81e-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: 39.23 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 355 SILNSNEH---LLKEKELLIDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENtflraqfaqktEA 431
Cdd:TIGR04523 579 SLKKKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSLEKE-------------------LEKAKKEN-----------EK 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 432 LSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKESEQNREKqqRIETLERYlA 511
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKELSLHYKK--YITRMIRI-K 704
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622825703 512 DLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 549
Cdd:TIGR04523 705 DLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
355-648 |
9.58e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.17 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 355 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 415
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 416 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 487
Cdd:COG5185 348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELESLLEETQAicrdretQ 560
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESRVSTLKA-------T 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825703 561 LESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYdsLQKIVEKQQQKMDQLRSQVQSLEQEVAQEEGTSQA 640
Cdd:COG5185 501 LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN--LIPASELIQASNAKTDGQAANLRTAVIDELTQYLS 578
|
....*...
gi 1622825703 641 LREEAQRR 648
Cdd:COG5185 579 TIESQQAR 586
|
|
| |
