|
Name |
Accession |
Description |
Interval |
E-value |
| Spc110_C |
pfam18520 |
Spindle pole body component 110 C-terminal domain; This is the C-terminal domain found in ... |
785-835 |
3.16e-18 |
|
Spindle pole body component 110 C-terminal domain; This is the C-terminal domain found in Spc110 proteins. Spc110 is a spindle pole body component (SPB) protein. The N-terminus is shown to bind to gamma-tubulin small complex (g-TuSC) while this C-terminal domain is essential for calmodulin-binding. The C-terminus of Spc110 is anchored to the SPB via a conserved PACT domain.
Pssm-ID: 375946 Cd Length: 52 Bit Score: 78.91 E-value: 3.16e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 334351095 785 SPGHIPTFKAVALLVLACVRMKQTAVRCRWDEHRIRYLRNKMAIDDDRITW 835
Cdd:pfam18520 2 RRRRRLKFKTVALMVLACVRMKRVALKRRWDEQRLRYLQRKIALDDDRISW 52
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-629 |
2.19e-16 |
|
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: 83.92 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 92 DNDNDNAHDSGKETDDVVKNLMGNLKENAPASNPLKEQQEQLHKLNTDNYNLRLKCNSLLKFLHNVTDQ----------- 160
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEklniqknidki 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 161 -GELTKSLGLLDEIHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQepvtevdhtacqrELSYVQNQLEKTTLQLNTYR 239
Cdd:TIGR04523 193 kNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-------------EINEKTTEISNTQTQLNQLK 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 240 DEvahlEDKTIRIQEDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDrakiqrLMNQLHEFDHKGSQSLLDLERQ 319
Cdd:TIGR04523 260 DE----QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD------WNKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 320 LEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRdnvKNNNSSNFEIGELKHAKASLDDKVRNLTEE 399
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK---KENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 400 RHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQV------IENTTKNSER 473
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLkvlsrsINKIKQNLEQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 474 TSQRIKDKETQIQKLESELQFCKQQLKDGSRRlQAEEERCRETFESELQNLEMK-NGFERTKLEREITLLKEERVALIET 552
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKK-ISSLKEKIEKLESEKKEKESKiSDLEDELNKDDFELKKENLEKEIDE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 553 HDRELELWKSKCDAL---NKENDILVRQ---EIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKD 626
Cdd:TIGR04523 566 KNKEIEELKQTQKSLkkkQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
...
gi 334351095 627 ELK 629
Cdd:TIGR04523 646 EVK 648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
280-559 |
5.02e-14 |
|
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: 76.63 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 280 SLVNKESELEEDRAKIQRLMNQLHEfdhkgsqslldLERQLEMKRDSISSLEKEVRALTHDRVHLETRI----KDREIEN 355
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAE-----------LEKALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 356 AKIQSELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAF 435
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 436 DSLRQELQTTKTQLEETRKTAQQLQTQvIENTTKNSERTSQRIKDKETQIQKLESELQfCKQQLKDGSRRLQAEEERCRE 515
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIEELESELE-ALLNERASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 334351095 516 TFESELQNLEMKNGFERTKLEREITLLKEERVALIETHDRELEL 559
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-676 |
7.28e-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: 66.24 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 350 DREIENAKiqSELERLRDNVKNNNSSNFEIGelkhakasldDKVRNLTEERHNLnQRISALRKECDEWK-----SKYQRN 424
Cdd:TIGR02169 169 DRKKEKAL--EELEEVEENIERLDLIIDEKR----------QQLERLRREREKA-ERYQALLKEKREYEgyellKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 425 ESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSR 504
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 505 RLQAEEERCRETFE------SELQNLEMKNG---FERTKLEREITLLKEERVAL---IETHDRELELWKSKCDALNKEND 572
Cdd:TIGR02169 316 ELEDAEERLAKLEAeidkllAEIEELEREIEeerKRRDKLTEEYAELKEELEDLraeLEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 573 ILVRqEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSAIND 652
Cdd:TIGR02169 396 KLKR-EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340
....*....|....*....|....
gi 334351095 653 DEQKTKYNTmkqrllvELKSLQDE 676
Cdd:TIGR02169 475 KEEYDRVEK-------ELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-686 |
8.66e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 227 QLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQhqleIQMLRSDVNNL--NVSLVNKESELEEDRAKIQRLMNQLHE 304
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEER----IEELKKEIEELeeKVKELKELKEKAEEYIKLSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 305 FDHKGSQSLLDLERQ---LEMKRDSISSLEKEVRALTHDRVHLETRI-----KDREIENAK-IQSELERLRDNVKNNNSS 375
Cdd:PRK03918 308 ELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLeeleeRHELYEEAKaKKEELERLKKRLTGLTPE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 376 NF--EIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQR----NESLDSNHRKAF--------DSLRQE 441
Cdd:PRK03918 388 KLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELleeytaelKRIEKE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 442 LQTTKTQLEETRKTAQQLQTQVienttkNSERTSQRIKDKETQIQKLESELQ-FCKQQLKDGSRRLQAEEERCREtFESE 520
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVL------KKESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIK-LKGE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 521 LQNLEmkngferTKLEREITLLKEERVALIETHDRELELwkskcdalNKENDILVRQEIGDLDGVKRKLsQQLDKLQEK- 599
Cdd:PRK03918 541 IKSLK-------KELEKLEELKKKLAELEKKLDELEEEL--------AELLKELEELGFESVEELEERL-KELEPFYNEy 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 600 --LTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEyLKSKQSAINDDEQKTKYNTMkQRLLVELKSLQDEN 677
Cdd:PRK03918 605 leLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEYEELREEY-LELSRELAGLRAEL 682
|
....*....
gi 334351095 678 LSLERKLLE 686
Cdd:PRK03918 683 EELEKRREE 691
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-652 |
1.18e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 200 NAAENKQEPVT-EVDHTACQRElsYVQNQLEKTTLQLNTY---RDEVAHLEDKTIRIQEDQRAKE---EQHQLEIQMLRS 272
Cdd:PRK02224 209 NGLESELAELDeEIERYEEQRE--QARETRDEADEVLEEHeerREELETLEAEIEDLRETIAETErerEELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 273 DVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQslldLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDRE 352
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE----LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 353 IENAKIQSELERLRDNVKNNNSS----NFEIGELKHAKA-------SLDDKVRNLTEERHNLNQRISALRKECDEWKSKY 421
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEieelEEEIEELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 422 QRNESL--------------DSNH-------RKAFDSLRQELQTTKTQLEETRKTAQQLQTQV-----IENTTKNSERTS 475
Cdd:PRK02224 443 EEAEALleagkcpecgqpveGSPHvetieedRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedrIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 476 QRIKDKETQIQKLE---SELQFCKQQLKDGSRRLQAEEERCRETFESELQNLEMKNGfERTKLEREITLLK--EERVALI 550
Cdd:PRK02224 523 ELIAERRETIEEKReraEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-KLAELKERIESLEriRTLLAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 551 ETHDRELELWKSKCDALNKENDiLVRQEIGDLDGVKRKLSQQLD-----KLQEKLTTAEGERGDLAEKLIKLQHSKDSYK 625
Cdd:PRK02224 602 ADAEDEIERLREKREALAELND-ERRERLAEKRERKRELEAEFDearieEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
490 500
....*....|....*....|....*..
gi 334351095 626 DELKRVSSKLEYLskEYLKSKQSAIND 652
Cdd:PRK02224 681 AEIGAVENELEEL--EELRERREALEN 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-511 |
1.41e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 219 RELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRL 298
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 299 MNQLHEFDHKG---SQSLLDLERQLEMKRDSISSLEKEVRAL-------THDRVHLETRIKDREIENAKIQSELERLRDN 368
Cdd:TIGR02168 774 EEELAEAEAEIeelEAQIEQLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLEDLEEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 369 VKNNNSsnfEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQ 448
Cdd:TIGR02168 854 IESLAA---EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334351095 449 LEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKD-GSRRLQAEEE 511
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElGPVNLAAIEE 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-514 |
1.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 185 QQYLELKAKLIQVEANAAENKQEpvtevdhtACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKE---E 261
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElelE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 262 QHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDhkgsQSLLDLERQLEMKRDSISSLEKEVRALTHDR 341
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 342 VHLETRIKDREIENAKIQSELERLRDnvknnnssnfEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKY 421
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAE----------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 422 QRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFckQQLKD 501
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLE 508
|
330
....*....|...
gi 334351095 502 GSRRLQAEEERCR 514
Cdd:COG1196 509 GVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-524 |
1.71e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 219 RELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQ----EDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAK 294
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 295 IQRLMNQLHEFDHKgsqsLLDLERQlemkrdsISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVknnNS 374
Cdd:TIGR02168 276 VSELEEEIEELQKE----LYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL---AE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 375 SNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYqrnesldSNHRKAFDSLRQELQTTKTQLEETRK 454
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334351095 455 TAQQLQTQVIENTTKNSE----RTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCREtFESELQNL 524
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-AERELAQL 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
216-687 |
5.41e-10 |
|
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: 63.27 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 216 ACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEqhqleiqmLRSDVNNLNVSLVNKESELEEDRAKI 295
Cdd:pfam01576 9 AKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE--------LCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 296 QRLM-------NQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDn 368
Cdd:pfam01576 81 ESRLeeeeersQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 369 vknnnssnfEIGELKHAKASLDDKVRNLTEERHNLNQRISAL----------RKECDEWKSKYQRnESLDSNHRKAfdSL 438
Cdd:pfam01576 160 ---------RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkkeekgRQELEKAKRKLEG-ESTDLQEQIA--EL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 439 RQELQTTKTQLEETRKTAQQLQTQVIENTTKNSErTSQRIKDKETQIQKLESELQFCK-------QQLKDGSRRLQAEEE 511
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNN-ALKKIRELEAQISELQEDLESERaarnkaeKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 512 RCRETFESELQNLEMkngfeRTKLEREITLLK-----EERV-------------ALIETHDRELE--------LWKSKcD 565
Cdd:pfam01576 307 ELEDTLDTTAAQQEL-----RSKREQEVTELKkaleeETRSheaqlqemrqkhtQALEELTEQLEqakrnkanLEKAK-Q 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 566 ALNKENDIL------VRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLS 639
Cdd:pfam01576 381 ALESENAELqaelrtLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 334351095 640 KEyLKSKQSAINDDEQKTKYNT-MKQRLLVELKSLQDENLSLERKLLEQ 687
Cdd:pfam01576 461 KD-VSSLESQLQDTQELLQEETrQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-649 |
8.81e-10 |
|
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: 62.78 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 256 QRAKEEqhqLEIQMLRSDVNNLNVSLVNKESE-LEEDRAKIQR---LMNQLHEFDHKG-SQSLLDLERQLEMKRDSISSL 330
Cdd:TIGR02169 173 EKALEE---LEEVEENIERLDLIIDEKRQQLErLRREREKAERyqaLLKEKREYEGYElLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 331 EKEVralthdrvhletrikdreienAKIQSELERLRDnvknnnssnfEIGELKHAKASLDDKVRNLTEERHNlnqrisAL 410
Cdd:TIGR02169 250 EEEL---------------------EKLTEEISELEK----------RLEEIEQLLEELNKKIKDLGEEEQL------RV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 411 RKECDEWKSKYQRnesldsnhrkafdsLRQELQTTKTQLEETRKTAQQLQTQvIENTTKNSERTSQRIKDKETQIQKLES 490
Cdd:TIGR02169 293 KEKIGELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRRDKLTE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 491 ELQFCKQQLKDGSRRLQAEEERCRETFEselqnlemkngfERTKLEREITLLKEERVALIETHDRELELWKSKCDALNKe 570
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRD------------ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334351095 571 ndilVRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSA 649
Cdd:TIGR02169 425 ----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
220-676 |
1.53e-09 |
|
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: 61.67 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 220 ELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKE-EQHQLEIQMLRSDVNNLNVSLVNKESELE--EDRAKIQ 296
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEiiQEQARNQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 297 R--LMNQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNV----- 369
Cdd:pfam15921 312 NsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkrek 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 370 -------KNNNSSNFEIGE---LKHAKASLDDkvRNLTEERhnLNQRISALRKECD-----EWKSKYQRNESLDSnhrka 434
Cdd:pfam15921 392 elslekeQNKRLWDRDTGNsitIDHLRRELDD--RNMEVQR--LEALLKAMKSECQgqmerQMAAIQGKNESLEK----- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 435 FDSLRQELQTTKTQLeetRKTAQQLQTQVIenTTKNSERT----SQRIKDKE-------TQIQKLESELQFCKQQLKdgs 503
Cdd:pfam15921 463 VSSLTAQLESTKEML---RKVVEELTAKKM--TLESSERTvsdlTASLQEKEraieatnAEITKLRSRVDLKLQELQ--- 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 504 rRLQAEEERCRETfESELQNLEMkngfERTKLEREITLLK---EERVALIETHDRELELWKSKCDALNKE-NDilVRQEI 579
Cdd:pfam15921 535 -HLKNEGDHLRNV-QTECEALKL----QMAEKDKVIEILRqqiENMTQLVGQHGRTAGAMQVEKAQLEKEiND--RRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 580 GDLDGVKRKLSQQLDKLQEKLTTAEGERGDL----AEKL---IKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSAIND 652
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLravKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
490 500
....*....|....*....|....
gi 334351095 653 DEQktkYNTMKQRLLVELKSLQDE 676
Cdd:pfam15921 687 SEE---METTTNKLKMQLKSAQSE 707
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-519 |
2.78e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 283 NKESELEEDRAKIQRLMNQLHEFdhkgSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSEL 362
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 363 ERLRDNVKNNNSSNFEIGELKHAK-----ASLDDKVRNLteerHNLNQRISALRKECDEWKSKYQRNESLdsnhRKAFDS 437
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRL----QYLKYLAPARREQAEELRADLAELAAL----RAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 438 LRQELQTTKTQLEETRKTAQQLQTQvienttknSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCRETF 517
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAE--------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 334351095 518 ES 519
Cdd:COG4942 244 PA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
287-686 |
4.91e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 287 ELEEDRAKIQRLMNQLHEFDhKGSQSLLDLERQLEMKRDSISSL-------EKEVRALTHDRVHLETRIKDREIENAKIQ 359
Cdd:PRK03918 142 ESDESREKVVRQILGLDDYE-NAYKNLGEVIKEIKRRIERLEKFikrteniEELIKEKEKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 360 SELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNhRKAFDSLR 439
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 440 QELQTTKTQLEETRKTAQQL--QTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLK--DGSRRLQAEEERCR- 514
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLeeEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 515 -------ETFESELQNLEMKngfeRTKLEREITLLKEE------RVALIETHDRELELWKSKCDALNKE------NDILV 575
Cdd:PRK03918 380 rltgltpEKLEKELEELEKA----KEEIEEEISKITARigelkkEIKELKKAIEELKKAKGKCPVCGRElteehrKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 576 R--QEIGDLDGVKRKLSQQLDKLQEKLTTAEGERG---------DLAEKLIKLQHSKDSY-KDELKRVSSKLEYLSKEY- 642
Cdd:PRK03918 456 EytAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLi 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 334351095 643 -LKSKQSAINDD-EQKTKYNTMKQRLLVELKSLQDENLSLERKLLE 686
Cdd:PRK03918 536 kLKGEIKSLKKElEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
394-666 |
5.17e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 394 RNLTEERHNLNQRISALRKECDEWKSKYQRNESLdsnhrkaFDSLRQELQTTKTQLEETRKTAQQLQtqvienttKNSER 473
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLE--------QEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 474 TSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCREtFESELQNLEMKNGFERTK-LEREITLLKEER------ 546
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-LEEALNDLEARLSHSRIPeIQAELSKLEEEVsriear 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 547 -----VALIETHDRELELWKSKCDALNKENDI-----LVRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIK 616
Cdd:TIGR02169 814 lreieQKLNRLTLEKEYLEKEIQELQEQRIDLkeqikSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 334351095 617 LqhskdsyKDELKRVSSKLEYLSKEYLKSKQsaiNDDEQKTKYNTMKQRL 666
Cdd:TIGR02169 894 L-------EAQLRELERKIEELEAQIEKKRK---RLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-519 |
3.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 216 ACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKtirIQEDQRAKEEQHQlEIQMLRSDVNNLNVSLVNKESELEEDRA-- 293
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEED---LSSLEQEIENVKS-ELKELEARIEELEEDLHKLEEALNDLEArl 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 294 ------KIQRLMNQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLrd 367
Cdd:TIGR02169 789 shsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-- 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 368 nvknnnssNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELqttkT 447
Cdd:TIGR02169 867 --------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----S 934
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334351095 448 QLEETRKTAQQL--QTQVIENTTKNSERTSQRIKDKET----QIQKLESELQFCKqQLKDGSRRLQAEEERCRETFES 519
Cdd:TIGR02169 935 EIEDPKGEDEEIpeEELSLEDVQAELQRVEEEIRALEPvnmlAIQEYEEVLKRLD-ELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
254-656 |
6.51e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 254 EDQRAKEEQHQLEIQMLRSDVNNlnvSLVNKESELEEDRAKiqRLMNQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKE 333
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRG---SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 334 VRALTHdrvHLETRikdREIEnaKIQSELERLRDnvknnnssnfEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKE 413
Cdd:PRK02224 240 DEVLEE---HEERR---EELE--TLEAEIEDLRE----------TIAETEREREELAEEVRDLRERLEELEEERDDLLAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 414 CDewkskyqrnesLDSNHRKAFDSLRQELQTTKTQLEET---RKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLES 490
Cdd:PRK02224 302 AG-----------LDDADAEAVEARREELEDRDEELRDRleeCRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 491 ELQFCKQQLKDGSRRLqaeeercrETFESELQNLEMKNGFERTKLEREITLLKEERVALIETHDRELEL---WKSKCDAL 567
Cdd:PRK02224 371 ELEEAREAVEDRREEI--------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatLRTARERV 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 568 NKENDILVR-------QEIGDLDGVKR--KLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSyKDELKRVSSKLEyL 638
Cdd:PRK02224 443 EEAEALLEAgkcpecgQPVEGSPHVETieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERRE-D 520
|
410
....*....|....*...
gi 334351095 639 SKEYLKSKQSAINDDEQK 656
Cdd:PRK02224 521 LEELIAERRETIEEKRER 538
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
321-534 |
7.71e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 56.09 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 321 EMKRDSISSLEKE----VRALtHDR--VHLE---TRIKDREIENA-----KIQSELERLRDNVKNNNSSNFEIGELKHAK 386
Cdd:PRK05771 5 RMKKVLIVTLKSYkdevLEAL-HELgvVHIEdlkEELSNERLRKLrslltKLSEALDKLRSYLPKLNPLREEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 387 A------------SLDDKVRNLTEERHNLNQRISALRKECDE---WK------SKYQRNESLD----SNHRKAFDSLRQE 441
Cdd:PRK05771 84 LeelikdveeeleKIEKEIKELEEEISELENEIKELEQEIERlepWGnfdldlSLLLGFKYVSvfvgTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 442 LQTTKTQLEETRKT----------------AQQLQ-TQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSR 504
Cdd:PRK05771 164 SDVENVEYISTDKGyvyvvvvvlkelsdevEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
250 260 270
....*....|....*....|....*....|
gi 334351095 505 RLQAEEERCRETFESELQNLEMKNGFERTK 534
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLKTD 273
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
158-686 |
2.52e-07 |
|
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: 54.46 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 158 TDQGELTKSL-GLLDEIHEWKQKHYTLNQQY-LELKAKLIQVEANAAENKQEPVTEvdHTACQRELSYVQNQL-EKTTLQ 234
Cdd:pfam12128 354 SELENLEERLkALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDKLAKIREARDRQ--LAVAEDDLQALESELrEQLEAG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 235 LNTYRDE----VAHLEDKTIRIQEDQRAKEEQHQLEIqmlrsdvnnlNVSLVNK-ESELEEDRAKIQRLMNQLHEFD--- 306
Cdd:pfam12128 432 KLEFNEEeyrlKSRLGELKLRLNQATATPELLLQLEN----------FDERIERaREEQEAANAEVERLQSELRQARkrr 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 307 HKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVH-LETRIKDREIENAKIQSELERLRDNVKNNNSSNFEIGELKHA 385
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLY 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 386 KASLDDK---VRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQ 462
Cdd:pfam12128 582 GVKLDLKridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 463 VIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKdgsrrlQAEEERCRETFESELQNLEMKNGFERTKlEREITLL 542
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQ------AWLEEQKEQKREARTEKQAYWQVVEGAL-DAQLALL 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 543 KEERVALIETHDRELelwkskcDALNKENDILVRQEIGDLDGVKrKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHS-- 620
Cdd:pfam12128 735 KAAIAARRSGAKAEL-------KALETWYKRDLASLGVDPDVIA-KLKREIRTLERKIERIAVRRQEVLRYFDWYQETwl 806
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334351095 621 --KDSYKDELKRVSSKLEYLSKEYLKSKQSAINDDEQKTKYNTMKQRLLVELkslqDENLSLERKLLE 686
Cdd:pfam12128 807 qrRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL----SENLRGLRCEMS 870
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
438-688 |
3.98e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 438 LRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERcRETF 517
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-LEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 518 ESELQNLEmkngFERTKLEREITLLKEERVALIETHDRELELWKSkcdalNKENDILVRQEIGDLDGVKRKLSQQLDKLQ 597
Cdd:COG1196 273 RLELEELE----LELEEAQAEEYELLAELARLEQDIARLEERRRE-----LEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 598 EKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSAINDDEQKTKYNTMKQRLLVELKSLQDEN 677
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250
....*....|.
gi 334351095 678 LSLERKLLEQR 688
Cdd:COG1196 424 EELEEALAELE 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
227-688 |
6.62e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 227 QLEKTTLQLNTYRDEVAHLED--KTIRIQEDQRAKEEQHQlEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHE 304
Cdd:COG4913 256 PIRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 305 fdhKGSQSLLDLERQLEmkrdsisSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVKNN-NSSNFEIGELK 383
Cdd:COG4913 335 ---NGGDRLEQLEREIE-------RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALlEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 384 HAKASLDDKVRNLTEERHNLNQRISALRkecdewkskyQRNESLDSNHRKAFDSLRQELQTTKTQLE------------- 450
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLE----------RRKSNIPARLLALRDALAEALGLDEAELPfvgelievrpeee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 451 -------------------------------ETRKTAQQLQTQVIENTTKNSERTS-------QRIKDKETQIQK-LESE 491
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLVYERVRTGLPDPERPRldpdslaGKLDFKPHPFRAwLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 492 L--QF---C---KQQLKDGSRRLQAE----EERCRetFESELQNLEMKN---GFERTK----LEREITLLKEERVAL--- 549
Cdd:COG4913 555 LgrRFdyvCvdsPEELRRHPRAITRAgqvkGNGTR--HEKDDRRRIRSRyvlGFDNRAklaaLEAELAELEEELAEAeer 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 550 IETHDRELELWKSKCDALNK-------ENDIL-VRQEIGDLDGVKRKLS----------QQLDKLQEKLTTAEGERGDLA 611
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdEIDVAsAEREIAELEAELERLDassddlaaleEQLEELEAELEELEEELDELK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 612 EKLIKLQHSKDSYKDELKRVSSKLEYLSK-------EYLKSKQSAINDDEQktkYNTMKQRLLVELKSLQDENLSLERKL 684
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERFAAALGDAV---ERELRENLEERIDALRARLNRAEEEL 789
|
....
gi 334351095 685 LEQR 688
Cdd:COG4913 790 ERAM 793
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-689 |
1.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 161 GELTKSLGLLDEIHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQEPvTEVDHTACQRELSYVQNQLEKTTLQLNTYRD 240
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 241 EVAHLEDKTIRIQED-QRAKEEQHQLE--IQMLRSDVNNLNVSLVNKESELEEDR--------------AKIQRLMNQLH 303
Cdd:TIGR02168 275 EVSELEEEIEELQKElYALANEISRLEqqKQILRERLANLERQLEELEAQLEELEskldelaeelaeleEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 304 EFDHKGS----------QSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVKNNN 373
Cdd:TIGR02168 355 SLEAELEeleaeleeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 374 ---------SSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQT 444
Cdd:TIGR02168 435 lkelqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 445 TKT------QLEETRKTAQQLQTQVieNTTKNSERTSQRIKDKETQIQKLES------------ELQFCKQQLKDGSRRL 506
Cdd:TIGR02168 515 QSGlsgilgVLSELISVDEGYEAAI--EAALGGRLQAVVVENLNAAKKAIAFlkqnelgrvtflPLDSIKGTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 507 QAEEERC-------RETFESELQNLeMKNGFERTK----LEREITLLKEER-VALIETHDRELELW---------KSKCD 565
Cdd:TIGR02168 593 ILKNIEGflgvakdLVKFDPKLRKA-LSYLLGGVLvvddLDNALELAKKLRpGYRIVTLDGDLVRPggvitggsaKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 566 ALNKENDIL-VRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLK 644
Cdd:TIGR02168 672 ILERRREIEeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 334351095 645 SKQSAINDDEQKTKYNTMKQRLLVELKSLQDENLSLERKLLEQRG 689
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-543 |
1.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 161 GELTKSL-GLLDEIHEWKQKHytlnQQYLELKAKLIQVEANAAENKQEPVTEVdhtacQRELSYVQNQLEKTTLQLNTYR 239
Cdd:PRK03918 341 EELKKKLkELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGLTPEKL-----EKELEELEKAKEEIEEEISKIT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 240 DEVAHLEDktiRIQEDQRAKEEqhqLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQsLLDLERQ 319
Cdd:PRK03918 412 ARIGELKK---EIKELKKAIEE---LKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK-LRKELRE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 320 LEMKRDSISSLEKEvRALTHDRVHLETRIKDREIENA--------KIQSELERLRDNVKNNNSSNFEIGELKHAKASLDD 391
Cdd:PRK03918 485 LEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 392 KVRNLTEERHNLNQRISALRKEC-DEWKSKYQR--------NESLDSNHR-----KAFDSLRQELQTTKTQLEETRKTAQ 457
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESvEELEERLKElepfyneyLELKDAEKElereeKELKKLEEELDKAFEELAETEKRLE 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 458 QLQTQVIENTTKNSERTSQRIKDKETqiqKLESELQFCKQQLKdgsrrlqaEEERCRETFESELQNLEMKNGfERTKLER 537
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYL---ELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELE-EREKAKK 711
|
....*.
gi 334351095 538 EITLLK 543
Cdd:PRK03918 712 ELEKLE 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-638 |
3.70e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 169 LLDEIHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQEpVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDK 248
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 249 TIRIQEDQRAKEEQHQ---LEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFD---HKGSQSLLDLERQLEM 322
Cdd:COG1196 297 LARLEQDIARLEERRReleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEaelAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 323 KRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVKNNNS----SNFEIGELKHAKASLDDKVRNLTE 398
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEalaeLEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 399 ERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVI-------------- 464
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligveaay 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 465 -------------ENTTKNSERTSQRI---KDKE---------TQIQKLESELQFCKQQLKDGSRRLQAEEERCRETFES 519
Cdd:COG1196 537 eaaleaalaaalqNIVVEDDEVAAAAIeylKAAKagratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 520 ELQN-----------LEMKNGFERT---------------------------------KLEREITLLKEERVALIETHDR 555
Cdd:COG1196 617 VLGDtllgrtlvaarLEAALRRAVTlagrlrevtlegeggsaggsltggsrrellaalLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 556 ELELWKSKCDALNKENDILVRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKL 635
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
...
gi 334351095 636 EYL 638
Cdd:COG1196 777 EAL 779
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
188-688 |
3.77e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 188 LELKAKLIQVEANAAENKQEPVTEVDHTACQRELSYVQ-----NQLEKTTLQLNTYRDEVAHLEDKTIRIQED-QRAKEE 261
Cdd:pfam05483 211 LEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQitekeNKMKDLTFLLEESRDKANQLEEKTKLQDENlKELIEK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 262 QHQLEiqmlrSDVNNLNVSL---VNKESELEEDRAKIQRLMNQLHEfdhkgsqsllDLERQLEMKRDSISSLEKEVRALT 338
Cdd:pfam05483 291 KDHLT-----KELEDIKMSLqrsMSTQKALEEDLQIATKTICQLTE----------EKEAQMEELNKAKAAHSFVVTEFE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 339 HDRVHLETRIKDREIENAKIQSELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWK 418
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 419 SKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTS-------------QRIKDKETQI 485
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllenkeltQEASDMTLEL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 486 QKLESELQFCKQQLKDGSRR---LQAEEERCRETFESELQNLEMKNGFERTKLEREitllkEERVALIE----THDRELE 558
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS-----EENARSIEyevlKKEKQMK 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 559 LWKSKCDALNKE------NDILVRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGErgdLAEKLIKLQHSKDSYKDELKRVS 632
Cdd:pfam05483 591 ILENKCNNLKKQienknkNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEIEDKK 667
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 334351095 633 SKLEYLSKEYLKSKQSAINDDEQKTKYNTMKQRLLVELKSLQDENLSLERKLLEQR 688
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
278-684 |
9.18e-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: 49.25 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 278 NVSLVNKESELEEDRAKIQRLMNQLHEFDHKgsqsLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAK 357
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENE----LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 358 IqSELERLRDNVKNNnssnfeigelkhaKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDS 437
Cdd:TIGR04523 220 I-SELKKQNNQLKDN-------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 438 LRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCRETF 517
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 518 ESELQNLEmkngfertKLEREITLLKEERVALiETHDRELELWKSKCDALNKENDilvrQEIGDLDGVKRKLSQQLDKLQ 597
Cdd:TIGR04523 366 EEKQNEIE--------KLKKENQSYKQEIKNL-ESQINDLESKIQNQEKLNQQKD----EQIKKLQQEKELLEKEIERLK 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 598 EKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQsainDDEQKTKYNTMKQRllvELKSLQDEN 677
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ----NLEQKQKELKSKEK---ELKKLNEEK 505
|
....*..
gi 334351095 678 LSLERKL 684
Cdd:TIGR04523 506 KELEEKV 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-630 |
1.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 219 RELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQHQLeiQMLRSDVNNLNVSLVNKESELEEDRAKIQRL 298
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 299 MNQLHEFDHKgSQSLLDLERQLEMKRDSIS-SLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVKNNNSSNF 377
Cdd:COG4717 159 RELEEELEEL-EAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 378 EIGELKHAK---------------ASLDDKVRNLTEERHNLNQRISALRkecdEWKSKYQRNESLDSNHRKAFDSLRQEL 442
Cdd:COG4717 238 AAALEERLKearlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLL----ALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 443 QTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQfCKQQLKDGSRRLQAEEERCRETFESELQ 522
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 523 NLEmkngfERTKLEREITLLKEErvalIETHDRELElwkskcDALNKENDILVRQEIGDLDGVKRKLSQQLDKLQEKLTT 602
Cdd:COG4717 393 QAE-----EYQELKEELEELEEQ----LEELLGELE------ELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430
....*....|....*....|....*....|
gi 334351095 603 AEGERGDLAE--KLIKLQHSKDSYKDELKR 630
Cdd:COG4717 458 LEAELEQLEEdgELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
429-624 |
1.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 429 SNHRKAFDSLRQELQTTKTQ---LEETRKTAQQLQTQVIENTTKNSERT-------SQRIKDKETQIQKLESELQFCKQQ 498
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAalrlwfaQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 499 LkdgsRRLQAEEERCRETfESELQNLEMKNGFER-TKLEREITLLKEERvaliETHDRELELWKSKCDALN--------- 568
Cdd:COG4913 311 L----ERLEARLDALREE-LDELEAQIRGNGGDRlEQLEREIERLEREL----EERERRRARLEALLAALGlplpasaee 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334351095 569 -KENDILVRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSY 624
Cdd:COG4913 382 fAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
192-532 |
3.75e-05 |
|
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: 47.73 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 192 AKLIQVEANAAENKQEPVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQHQLEIQMLR 271
Cdd:TIGR00606 784 AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 272 SDVNNLNVSLVnkesELEEDRAKIQRLMNQLHEFdhkgSQSLLDLERQLEMKRDSISSLEKevrALTHDRVHLETRIKDR 351
Cdd:TIGR00606 864 SKTNELKSEKL----QIGTNLQRRQQFEEQLVEL----STEVQSLIREIKDAKEQDSPLET---FLEKDQQEKEELISSK 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 352 EIENAKIQSELERLRDNVKNnnssnfEIGELKHAKASLDD-KVRNLTEERHNLNQRISALrKECDEWKSKYQRNESLdsn 430
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKN------IHGYMKDIENKIQDgKDDYLKQKETELNTVNAQL-EECEKHQEKINEDMRL--- 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 431 HRKAFDSLRQELQTTKTQLeETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEE 510
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDNL-TLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYE 1081
|
330 340
....*....|....*....|..
gi 334351095 511 ERcRETFESELQNLEMKNGFER 532
Cdd:TIGR00606 1082 KE-IKHFKKELREPQFRDAEEK 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-512 |
4.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 325 DSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVknnNSSNFEIGELKHAKASLDDKVRNLTEERHNLN 404
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 405 QRISALRKECDEWKSKYQRNESLD-----------SNHRKAFDSLRQELQTTKTQLEETRKTAQQLQtQVIENTTKNSER 473
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELA-ALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 334351095 474 TSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEER 512
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
254-423 |
4.11e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 254 EDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEfdHKGSQSLLDLERQLEMKRDSISSLEKE 333
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN--VRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 334 VRAlthdrvhLETRIKDREIENAKIQSELERLRDnvknnnssnfeigELKHAKASLDDKVRNLTEERHNLNQRISALRKE 413
Cdd:COG1579 112 ILE-------LMERIEELEEELAELEAELAELEA-------------ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
170
....*....|.
gi 334351095 414 CDE-WKSKYQR 423
Cdd:COG1579 172 IPPeLLALYER 182
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
185-651 |
4.18e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 185 QQYLELKAKLIQVEANAAENKQEPVTEVDHTacQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQHQ 264
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEEL--EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 265 LE-----------------IQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQSL---LDLERQLEMKR 324
Cdd:pfam15921 395 LEkeqnkrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLekvSSLTAQLESTK 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 325 DSissLEKEVRALTHDRVHLE----------TRIKDREIENAKIQSELERLRDNVknnnssNFEIGELKHAKASlDDKVR 394
Cdd:pfam15921 475 EM---LRKVVEELTAKKMTLEssertvsdltASLQEKERAIEATNAEITKLRSRV------DLKLQELQHLKNE-GDHLR 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 395 NLTEERHNLNQRISALRKECDEWKSKYQRNESLDSNH--------------RKAFDSLRQELQTTK-------TQLEETR 453
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtagamqvekaqlEKEINDRRLELQEFKilkdkkdAKIRELE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 454 KTAQQLQTQVIENTTKNSERTsQRIKDKETQIQKLESELQFCKQQLKDgsrrLQAEEERCRETFESELQNLEMKNGFERT 533
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNS----LSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 534 KLEREITLLKEERVALIETHDRELELWKSkcdALNKENDILVRQeiGDLDGVKRKLSqqldKLQEKLTTAEGERGDLAEK 613
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKV---AMGMQKQITAKR--GQIDALQSKIQ----FLEEAMTNANKEKHFLKEE 770
|
490 500 510
....*....|....*....|....*....|....*...
gi 334351095 614 LIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSAIN 651
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
460-649 |
4.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 460 QTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCRETfESELQNLEMK---NGFERTKLE 536
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAALEAElaeLEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 537 REITLLKEERVALIETHDR-----ELELWKSKCDALNKENDILV--------RQEIGDLDGVKRKLSQQLDKLQEKLTTA 603
Cdd:COG4942 97 AELEAQKEELAELLRALYRlgrqpPLALLLSPEDFLDAVRRLQYlkylaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334351095 604 EGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKQSA 649
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
195-346 |
5.47e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 195 IQVEANAAENKQEPVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLE------DKTIRIQEDQ--RAKEEQHQL- 265
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeleekDERIERLERElsEARSEERREi 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 266 ----EIQMLRSDVNNLNVSLVNKESELEEDRAKIQRlMNQLHEFDHKGSQSLLDLERQLemKRDSISSLEKEVRALTHDR 341
Cdd:COG2433 462 rkdrEISRLDREIERLERELEEERERIEELKRKLER-LKELWKLEHSGELVPVKVVEKF--TKEAIRRLEEEYGLKEGDV 538
|
....*
gi 334351095 342 VHLET 346
Cdd:COG2433 539 VYLRD 543
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
232-587 |
6.06e-05 |
|
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: 46.66 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 232 TLQLNTYRDEVAHLEDKTIRIQEDQRaKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFdhkGSQ 311
Cdd:pfam17380 264 TMTENEFLNQLLHIVQHQKAVSERQQ-QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 312 SLLDLERQLEMKRDSISSLEKEVRALTHDRVHLE-TRIKD-------REIENAKIQSELERLRDNVKNNNSSNFEIGELK 383
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRElerlqmeRQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 384 HAKASL--------DDKVRNLTEERHNLNQRIsalRKECDEWKSKYQRNESLDSNHRKAFDSLRQElqttktqlEETRKT 455
Cdd:pfam17380 420 VEMEQIraeqeearQREVRRLEEERAREMERV---RLEEQERQQQVERLRQQEEERKRKKLELEKE--------KRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 456 AQQLQTQVIEnttKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERCREtfeselqnLEMKngfERTKL 535
Cdd:pfam17380 489 AEEQRRKILE---KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ--------QEME---ERRRI 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 334351095 536 EREITLLKEERVALiETHDRELELWKSKCDALNKENDILVRQEIGDLDGVKR 587
Cdd:pfam17380 555 QEQMRKATEERSRL-EAMEREREMMRQIVESEKARAEYEATTPITTIKPIYR 605
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
254-398 |
1.06e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.13 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 254 EDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKE 333
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEE 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334351095 334 VRaltHDRVHLETRIKDREienakiqSELERLRDNVKNNNSSNFEIGElkhakasLDDKVRNLTE 398
Cdd:pfam09787 130 LR---RSKATLQSRIKDRE-------AEIEKLRNQLTSKSQSSSSQSE-------LENRLHQLTE 177
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-449 |
1.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 183 LNQQYLELKAKLIQVEANAAENKQ-----------EPVTEVDHTAcqrELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIR 251
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVE---TIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 252 IQEDQRAKEEqhqleIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQ---SLLDLERQLEMKRDSIS 328
Cdd:PRK02224 501 AEDLVEAEDR-----IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkreAAAEAEEEAEEAREEVA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 329 SLEKEVRALTHDRVHLEtRIKDREIENAKIQSELERLRDNVKNNNSSNFE----IGELKHAKASL--------------- 389
Cdd:PRK02224 576 ELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDErrerLAEKRERKRELeaefdearieeared 654
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334351095 390 -----------DDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNESLDsNHRKAFDSLRQE---LQTTKTQL 449
Cdd:PRK02224 655 keraeeyleqvEEKLDELREERDDLQAEIGAVENELEELEELRERREALE-NRVEALEALYDEaeeLESMYGDL 727
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
440-600 |
1.48e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 440 QELQTTKTQLEETRKT---AQQLQtQVIENTTKNSERTSQRIKDKE---------TQIQKLESELQFCKQQLKDGSRRLQ 507
Cdd:PRK10929 48 EALQSALNWLEERKGSlerAKQYQ-QVIDNFPKLSAELRQQLNNERdeprsvppnMSTDALEQEILQVSSQLLEKSRQAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 508 AEEERCRETFESELQNLEMKNGFER--TKLEREI---------------TLLKEERVALIETHDrELELwkSKCDALNke 570
Cdd:PRK10929 127 QEQDRAREISDSLSQLPQQQTEARRqlNEIERRLqtlgtpntplaqaqlTALQAESAALKALVD-ELEL--AQLSANN-- 201
|
170 180 190
....*....|....*....|....*....|.
gi 334351095 571 ndilvRQEIGDLDG-VKRKLSQQLDKLQEKL 600
Cdd:PRK10929 202 -----RQELARLRSeLAKKRSQQLDAYLQAL 227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
196-473 |
1.52e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 196 QVEANAAENKQEPVTEVDHTACQRELSYVQNQLEK----TTLQLNTYRDEVAHL---EDKTIRIQEDQRAKEEQHQLEIQ 268
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdMTLELKKHQEDIINCkkqEERMLKQIENLEEKEMNLRDELE 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 269 MLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRI 348
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 349 KDREIENAKIQSELERLR---DNVKNNNSSNFEI---------GELKHAKASLDDKVRNLTE------------------ 398
Cdd:pfam05483 632 NAYEIKVNKLELELASAKqkfEEIIDNYQKEIEDkkiseekllEEVEKAKAIADEAVKLQKEidkrcqhkiaemvalmek 711
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334351095 399 ERHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSER 473
Cdd:pfam05483 712 HKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
321-545 |
1.57e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 321 EMKRDSISSleKEVRALTHDRVHLETRIKDREIE-NAKIQSELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEE 399
Cdd:pfam05557 17 EKKQMELEH--KRARIELEKKASALKRQLDRESDrNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 400 RHNL----NQRISALRKECDEWKSKYQRNESldsnhrkAFDSLRQELQTTKTQLEETRKTAQQLqTQVIENTtknsERTS 475
Cdd:pfam05557 95 KESQladaREVISCLKNELSELRRQIQRAEL-------ELQSTNSELEELQERLDLLKAKASEA-EQLRQNL----EKQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 476 QRIKDKETQIQKLESELQFcKQQLKDGSRRLQAEEERCREtFESELQNLEMKNGFERTkLEREITLLKEE 545
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQS-QEQDSEIVKNSKSELARIPE-LEKELERLREHNKHLNE-NIENKLLLKEE 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
225-413 |
2.30e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 225 QNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQ----------HQLEIQMLRSDVNNLNVSLVNKESELEEDRAK 294
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraLEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 295 IQRLMNQLHEFDHKG-------SQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRD 367
Cdd:COG4942 106 LAELLRALYRLGRQPplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334351095 368 N----VKNNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKE 413
Cdd:COG4942 186 EraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-528 |
3.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 361 ELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWK--SKYQRNESLDSNHRKAFDSL 438
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 439 R---QELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERcRE 515
Cdd:COG4717 152 EerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE-LE 230
|
170
....*....|...
gi 334351095 516 TFESELQNLEMKN 528
Cdd:COG4717 231 QLENELEAAALEE 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
285-525 |
3.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 285 ESELEEDRAKIQRLMNQLHEFdhKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRvhletrikdreienAKIQSELER 364
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL--------------AEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 365 LRDNVKNNNSSNFEIGElkhakaslDDKVRNLTEERHNLNQRISALRkecdewkskyqrnESLDSNHRKAfDSLRQELQT 444
Cdd:COG3206 245 LRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELS-------------ARYTPNHPDV-IALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 445 TKTQL-EETRKTAQQLQTQVienttknsERTSQRIKDKETQIQKLESELQFcKQQLKDGSRRLQAEEERCRETFESELQN 523
Cdd:COG3206 303 LRAQLqQEAQRILASLEAEL--------EALQAREASLQAQLAQLEARLAE-LPELEAELRRLEREVEVARELYESLLQR 373
|
..
gi 334351095 524 LE 525
Cdd:COG3206 374 LE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
291-458 |
3.88e-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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 291 DRAKIQRLMnQLHEFDHKgsqsLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVK 370
Cdd:COG1579 2 MPEDLRALL-DLQELDSE----LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 371 ------NNNSSNFEIGELKHAKASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRNEsldsnhrKAFDSLRQELQT 444
Cdd:COG1579 77 kyeeqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDE 149
|
170
....*....|....
gi 334351095 445 TKTQLEETRKTAQQ 458
Cdd:COG1579 150 ELAELEAELEELEA 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
385-641 |
4.16e-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: 43.60 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 385 AKASLDDKVRNLTEERHNLNQRISALRKEcdewkskyqrnesldsnhrkaFDSLRQELQTTKTQLEETRKTAQQLQTQVi 464
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE---------------------EKALLKQLAALERRIAALARRIRALEQEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 465 enttknsERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEEERcretfeSELQNLEMKNGFERtkLEREITLLK- 543
Cdd:COG4942 79 -------AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ------PPLALLLSPEDFLD--AVRRLQYLKy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 544 --EERVALIETHDRELELWKSKCDALNKENDILvRQEIGDLDGVKRKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSK 621
Cdd:COG4942 144 laPARREQAEELRADLAELAALRAELEAERAEL-EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|
gi 334351095 622 DSYKDELKRVSSKLEYLSKE 641
Cdd:COG4942 223 EELEALIARLEAEAAAAAER 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
388-646 |
4.47e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 388 SLDDKVRNLTEERHNLN--QRISALRKECDEwksKYQRNESLDSNHRKAFDSLRQELQTTKTqLEETRKTAQQLQT-QVI 464
Cdd:PRK05771 13 TLKSYKDEVLEALHELGvvHIEDLKEELSNE---RLRKLRSLLTKLSEALDKLRSYLPKLNP-LREEKKKVSVKSLeELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 465 ENTTKNSERTSQRIKDKETQIQKLESELqfckqqlkdgsRRLQAEEERCR--ETFESELQNLemkNGFERTK-------- 534
Cdd:PRK05771 89 KDVEEELEKIEKEIKELEEEISELENEI-----------KELEQEIERLEpwGNFDLDLSLL---LGFKYVSvfvgtvpe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 535 -LEREITLLKEERVALIETHDRELE---LWKSKcDALNKENDIL-----VRQEIGDldgvKRKLSQQLDKLQEKLTTAEG 605
Cdd:PRK05771 155 dKLEELKLESDVENVEYISTDKGYVyvvVVVLK-ELSDEVEEELkklgfERLELEE----EGTPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 334351095 606 ERGDLAEKLIKLqhsKDSYKDELKRVsskLEYLSKEYLKSK 646
Cdd:PRK05771 230 ERESLLEELKEL---AKKYLEELLAL---YEYLEIELERAE 264
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
160-411 |
5.00e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 160 QGELTKSLGLLDEIHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQEPVTEVDHT-------ACQRELSYVQNQLEKTT 232
Cdd:PRK11281 62 QQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrQLESRLAQTLDQLQNAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 233 LQLNTYRDEVAHLEDKTIRIQedqrAKEEQHQLEIQMLRsdvNNLNVSLVNKESELEEDRAKI---QRLMNQLHEFDHK- 308
Cdd:PRK11281 142 NDLAEYNSQLVSLQTQPERAQ----AALYANSQRLQQIR---NLLKGGKVGGKALRPSQRVLLqaeQALLNAQNDLQRKs 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 309 --GSQSLLDL-ERQLEMKRDSISSLEKEVRALthdrvhletrikdREIENAK--IQSE-----LERLRDNVKNNNSS--- 375
Cdd:PRK11281 215 leGNTQLQDLlQKQRDYLTARIQRLEHQLQLL-------------QEAINSKrlTLSEktvqeAQSQDEAARIQANPlva 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 334351095 376 -----NFEIGE-LKHAKASLDDKVR----------NLTEERHNLNQRISALR 411
Cdd:PRK11281 282 qeleiNLQLSQrLLKATEKLNTLTQqnlrvknwldRLTQSERNIKEQISVLK 333
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
188-688 |
5.07e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 188 LELKAKLIQVEANAAENKQEPVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQRAKEEQHQLEI 267
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 268 QMLRSDVNNLNVSLVNKESELEEDRAKIQRLMnqLHEFDHKGSQSLLDLERQLEMKRDSISSL--EKEVRALTHDRVHLE 345
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAHAKKQQELQQRYAELCAAaiTCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 346 trikdreiENAKIQSELERLRDNVKNNNSSNFEIGELK-HAKASLDDKVRNLTEERHNLNQRISAL------RKECDEWK 418
Cdd:TIGR00618 463 --------ESAQSLKEREQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 419 SKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLqTQVIENTTKNSERTSQRIKDketqIQKLESELQFCKQQ 498
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDIPNLQNITVR----LQDLTEKLSEAEDM 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 499 LKDGSRR--LQAEEERCRETFESELQNLEMKNGFERTKLEREITLL--KEERVALIETHDRELELWKSKCDALNKENDiL 574
Cdd:TIGR00618 610 LACEQHAllRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQS-E 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 575 VRQEIGDLDGVKRKLSqQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDELKRVSSKLEYLSKEYLKSKqsaINDDE 654
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQT-LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR---TEAHF 764
|
490 500 510
....*....|....*....|....*....|....
gi 334351095 655 QKTKYNTMKQRLLVELKSLQdENLSLERKLLEQR 688
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLA-AEIQFFNRLREED 797
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
270-688 |
6.00e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 270 LRSDVNNLNVSLVNKESELEEDRAKIQRLMnqlhefDHKGSQS--LLDLERQLEMKRDSISSLEKEVRALTHdrvhlETR 347
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLT------EEKSTLAgeIRDLKDMLDVKERKINVLQKKIENLQE-----QLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 348 IKDREIENAKiqselERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEERhnlnqrisalrkecdewkskyqrnESL 427
Cdd:pfam10174 412 DKDKQLAGLK-----ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR------------------------ERE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 428 DSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKdKETQIQKLESELqfckQQLKDGSRRLQ 507
Cdd:pfam10174 463 DRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAV----EQKKEECSKLE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 508 AEEERCRETFESELQNLEMKNGFErtKLEREITLLKEERVALIETHDRELELWKskcDALNKENDilVRQEIGDLDG-VK 586
Cdd:pfam10174 538 NQLKKAHNAEEAVRTNPEINDRIR--LLEQEVARYKEESGKAQAEVERLLGILR---EVENEKND--KDKKIAELESlTL 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 587 RKLSQQLDKLQEKLTTAEGERGDLAEKLIKLQHSKDSYKDelKRVSSKLEYLSKEYLKSKQSAindDEQKTKYNTMKQRL 666
Cdd:pfam10174 611 RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQEL---DATKARLSSTQQSL 685
|
410 420
....*....|....*....|...
gi 334351095 667 lvELKSLQDENLSLE-RKLLEQR 688
Cdd:pfam10174 686 --AEKDGHLTNLRAErRKQLEEI 706
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
436-614 |
6.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 436 DSLRQELQTTKTQLEETRKTAQQLQTQVienttknsERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRL-QAEEERCR 514
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARL--------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 515 ETFESELQNLEMkngfERTKLEREITLLKEErvalIETHDRELELWKSKCDALNKEndilvrqeigdLDGVKRKLSQQLD 594
Cdd:COG1579 92 EALQKEIESLKR----RISDLEDEILELMER----IEELEEELAELEAELAELEAE-----------LEEKKAELDEELA 152
|
170 180
....*....|....*....|
gi 334351095 595 KLQEKLTTAEGERGDLAEKL 614
Cdd:COG1579 153 ELEAELEELEAEREELAAKI 172
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
451-618 |
8.43e-04 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 451 ETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESEL--------QFCKQQLKDGSRRLQAEEERCR----ETFE 518
Cdd:pfam07902 125 EIVESAEGIATRISEDTDKKLALINETISGIRREYQDADRQLsssyqagiEGLKATMASDKIGLQAEIQASAqglsQRYD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 519 SELQNLEMKngFERTK------LEREITLLKEERVALIETHDRELELWKSKCDALNKENDILVRQEIGDLDGVKRKLSQQ 592
Cdd:pfam07902 205 NEIRKLSAK--ITTTSsgtteaYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQSTAYQISQEISNREGAVSRVQQD 282
|
170 180
....*....|....*....|....*.
gi 334351095 593 LDKLQEKLTTAEGERGDLAEKLIKLQ 618
Cdd:pfam07902 283 LDSYQRRLQDAEKNYSSLTQTVKGLQ 308
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-453 |
1.12e-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: 42.70 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 86 LNGQSADNDNDNAHDSGKETDDVVKNLMGNLKENAPASNPLKEQQEQLHKLNTDNYNLRLKCNSLLKFLHNVTDQgeltk 165
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK----- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 166 slgLLDEIHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQE-PVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAH 244
Cdd:TIGR04523 375 ---LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 245 LE---DKTIRIQEDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDHKGSqSLLDLERQLE 321
Cdd:TIGR04523 452 KEliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-SLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 322 MKrdsISSLEKEVRALTHDRVHLETRIKDREIENAK--IQSELERLRDNVKNNNSSNFEIGELKHAKAsldDKVRNLTEE 399
Cdd:TIGR04523 531 SE---KKEKESKISDLEDELNKDDFELKKENLEKEIdeKNKEIEELKQTQKSLKKKQEEKQELIDQKE---KEKKDLIKE 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 334351095 400 RHNLNQRISALRKECDEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETR 453
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
130-548 |
1.14e-03 |
|
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: 42.65 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 130 QEQLHKLNTDNYNLRLKCNSLLKFLHNVTDQGELTKSLGLLDE-IHEWKQKHYTLNQQYLELKAKLIQVEANAAENKQEP 208
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 209 VTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKtirIQEDQRAKEEQHQLEIQMLRsdvnnLNVSLVNKESEL 288
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM---LACEQHALLRKLQPEQDLQD-----VRLHLQQCSQEL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 289 EEDRAKIQRLMNQL--HEFDHKGSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHL----------ETRIKDREIENA 356
Cdd:TIGR00618 642 ALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLaqcqtllrelETHIEEYDREFN 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 357 KIQSELERLRDNVKNNNSSNFEIgeLKHAKASLDDKVRNLTEERHNLNQRISALRKECDEwkskYQRNESLDSNHRKAFD 436
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQS--LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE----LSHLAAEIQFFNRLRE 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 437 SLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKET---QIQKLESELQFCKQQlKDGSRRLQAEEERC 513
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQ-LAQLTQEQAKIIQL 874
|
410 420 430
....*....|....*....|....*....|....*
gi 334351095 514 RETFESELQNLEMKNGFERTKLEREITLLKEERVA 548
Cdd:TIGR00618 875 SDKLNGINQIKIQFDGDALIKFLHEITLYANVRLA 909
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
432-618 |
1.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 432 RKAFDSLRQELQTTKTQLEETRKTAQQLQTQ-VIENTTKNSERTSQRIKDKETQIQKLESELQFCKQQLKDGSRRLQAEE 510
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKnGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 511 ERCRETFES-ELQNLemkngfeRTKLEREITLLKEERVALIETHDRELELwKSKCDALNKENDILVRQEIGDLDGVKRKL 589
Cdd:COG3206 254 DALPELLQSpVIQQL-------RAQLAELEAELAELSARYTPNHPDVIAL-RAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180
....*....|....*....|....*....
gi 334351095 590 SQQLDKLQEKLTTAEGERGDLAEKLIKLQ 618
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
169-547 |
1.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 169 LLDEIHEWKQKHYTLNQQYLELKAKLIQVEAnaAENKQEPVTEVDhtACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDK 248
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELE--ALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 249 TIRIQEDQRAKEEQHQL-------EIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFdhKGSQSLLDLERQLE 321
Cdd:COG4717 169 EAELAELQEELEELLEQlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 322 MKRDSI--------------------------------------SSLEKEVRALTHDRVHLETRIKDREIENAKIQSELE 363
Cdd:COG4717 247 EARLLLliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 364 RLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLTEER--HNLNQRISALRKEC-----DEWKSKYQRNEsldsnhrkAFD 436
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAgvedeEELRAALEQAE--------EYQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 437 SLRQELQTTKTQLEETRKTAQQLQTQVIENTTKN-SERTSQRIKDKETQIQKLESELQFCKQQLKD--GSRRLQAEEERc 513
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELEEeLEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQE- 477
|
410 420 430
....*....|....*....|....*....|....*..
gi 334351095 514 RETFESELQNLE---MKNGFERTKLEREITLLKEERV 547
Cdd:COG4717 478 LEELKAELRELAeewAALKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-558 |
1.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 172 EIHEWKQKHYTLNQQYLELKAKLIQVEaNAAENKQEPVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIR 251
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 252 IQEDQRAKEEQHQlEIQMLRSDVNNL-NVSLVNKESELEEDRAKIQRLMNQLHEfdhkgsqslldLERQLEMKRDSISSL 330
Cdd:COG4717 158 LRELEEELEELEA-ELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAE-----------LEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 331 EKEVRALTHDRVHLETRIKDREIEN-AKIQSELERLRDNVKNNNSSNFEIGELKHAKASL----------DDKVRNLTEE 399
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLlLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllarEKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 400 RHNLNQRISALRKEcdEWKSKYQRNESLDSNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKN--------S 471
Cdd:COG4717 306 ELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagveD 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 472 ERTSQRIKDKETQIQKLESELQFCKQQLKD-GSRRLQAEEERCRETFESELQNLEMkngfERTKLEREITLLKEERvALI 550
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEE----ELEELEEELEELREEL-AEL 458
|
....*...
gi 334351095 551 ETHDRELE 558
Cdd:COG4717 459 EAELEQLE 466
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
220-513 |
1.83e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 220 ELSYVQNQLEKTTLQLNTYRDEVAHLEDKTIRIQEDQ---RAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEedrakiq 296
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELeelVARLAKLEAALREAEAAKEELRIELRDKTAQAE------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 297 rlmnqlhefdhkgsqsllDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRDNVKN-NNSS 375
Cdd:pfam19220 122 ------------------ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRlQALS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 376 NFEIGELkhakASLDDKVRNLTEERHNLNQRISALRKECDEWKSKYQRN----ESLDSNHRKAFDSLRQELQTTKTQLEE 451
Cdd:pfam19220 184 EEQAAEL----AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAeaqlEEAVEAHRAERASLRMKLEALTARAAA 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334351095 452 TRKTAQQLQTQVIENTtkNSERTSQRiKDKETQIQK---------LESELQFCKQQLKDGSRRLQAEEERC 513
Cdd:pfam19220 260 TEQLLAEARNQLRDRD--EAIRAAER-RLKEASIERdtlerrlagLEADLERRTQQFQEMQRARAELEERA 327
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
318-726 |
2.63e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 318 RQLEMKRDSISSLEKEVRALthdrvhlETRIKDREIENAKIQsELERLRDNVKNNNSSNFEIGELKHAKASLDDKVRNLT 397
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKAL-------ETLRQVRQTQGQKVQ-EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 398 EERHNLNQRISALRKECDEWKSKYQRNEsldsNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERT--- 474
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvre 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 475 -SQRIKDKETQIQKLESELQFCKQQ-----LKDGSRRLQAEEERCR-ETFESELQNLEMK---NGFERTK-LEREItllK 543
Cdd:TIGR00606 317 kERELVDCQRELEKLNKERRLLNQEktellVEQGRLQLQADRHQEHiRARDSLIQSLATRlelDGFERGPfSERQI---K 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 544 EERVALIETHDRELELWKSKCDALnKENDILVRQEIGDLDGVKRKLSQQLDKLQEKLttaEGERGDLAEKLIKLQHSKDS 623
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADL-QSKERLKQEQADEIRDEKKGLGRTIELKKEIL---EKKQEELKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 624 YKDELKrvsskleyLSKEYLKSKQsaindDEQKTKYNTMKQRLLVELKSLQDENLSLERKLL---EQRGSSSRSQESSSR 700
Cdd:TIGR00606 470 SDRILE--------LDQELRKAER-----ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRkldQEMEQLNHHTTTRTQ 536
|
410 420
....*....|....*....|....*.
gi 334351095 701 SSSTTQDRLDYYKLKYNNEVKHNNDL 726
Cdd:TIGR00606 537 MEMLTKDKMDKDEQIRKIKSRHSDEL 562
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-374 |
2.87e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 183 LNQQYLELKAKLIQVEANAAENKQE---PVTEVDHTACQRELSYVQNQLEKTTLQLNTYRDEVAHLEDKtIRIQEDQRAK 259
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ-LGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 260 EEQHQlEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLHEFDhkgSQSLLDLERQLEMKRDSISSLEKEVRALTH 339
Cdd:COG3206 259 LLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR---AQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190
....*....|....*....|....*....|....*
gi 334351095 340 DRVHLETRIKdreiENAKIQSELERLRDNVKNNNS 374
Cdd:COG3206 335 QLAQLEARLA----ELPELEAELRRLEREVEVARE 365
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
201-543 |
4.01e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 201 AAENKQEPVTEVDhtacqrelsyVQNQLEKttlqLNTYRDEVAhlEDKTIRiqedQRAKEEQHQLE-IQMLRSDVNNLNV 279
Cdd:PRK11281 28 RAASNGDLPTEAD----------VQAQLDA----LNKQKLLEA--EDKLVQ----QDLEQTLALLDkIDRQKEETEQLKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 280 SLVNKESELEEDRAKIQRLMNQLHEFDHK--GSQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRikdREIENAK 357
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ---PERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 358 IQSELERLR--DNVKNNNSSNfeigelkhaKASLDDKVRNLTE-ERHNLNQRISALRKEC---DEWKSKYQRNESLDSNH 431
Cdd:PRK11281 165 LYANSQRLQqiRNLLKGGKVG---------GKALRPSQRVLLQaEQALLNAQNDLQRKSLegnTQLQDLLQKQRDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 432 RKAFDSLRQELQTTKTQ--LEETRKTAQQLQTQvienttknsertsqrikDKETQIQK---LESELQFcKQQLkdgSRRL 506
Cdd:PRK11281 236 IQRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQ-----------------DEAARIQAnplVAQELEI-NLQL---SQRL 294
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 334351095 507 QAEEERCRETFEselQNLEMKNGFER-----TKLEREITLLK 543
Cdd:PRK11281 295 LKATEKLNTLTQ---QNLRVKNWLDRltqseRNIKEQISVLK 333
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
349-546 |
5.64e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.74 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 349 KDREIENAKIQSELERLrdnvKNNNSSNFEIGELKHAKasldDKVRnltEERHNLNQRISALRKECDEwkskyqrnesLD 428
Cdd:pfam09787 23 KEKLIASLKEGSGVEGL----DSSTALTLELEELRQER----DLLR---EEIQKLRGQIQQLRTELQE----------LE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 429 SNHRKAFDSLRQELQTTKTQLEETRKTAQQLQTQV---------IENTTKNSERTSQ-RIKDKETQIQKLESELqfckqQ 498
Cdd:pfam09787 82 AQQQEEAESSREQLQELEEQLATERSARREAEAELerlqeelryLEEELRRSKATLQsRIKDREAEIEKLRNQL-----T 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334351095 499 LKDGSRRLQAE-EERCRETFESELQNLEMkngFERTKLEREITLLKEER 546
Cdd:pfam09787 157 SKSQSSSSQSElENRLHQLTETLIQKQTM---LEALSTEKNSLVLQLER 202
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
240-367 |
6.60e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 240 DEVAHLEDKTIRIQEDQRAKEEQHQLEIQMLRSDVNNLNVSLVNKESELEEDRAKIQRLMNQLhefdhkgSQSLLDLERQ 319
Cdd:pfam08614 14 DRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGEL-------AQRLVDLNEE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 334351095 320 LEMKRDSISSLEKEVRALTHDRVHLETRIKDREIENAKIQSELERLRD 367
Cdd:pfam08614 87 LQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-491 |
7.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 281 LVNKESELEEDRAKIQRLMNQLHEFDhkgsQSLLDLERQLEMKRDSISSLEKEVRALTHDRVHLETRIKDReienakiQS 360
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQ----AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER-------RE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334351095 361 EL-ERLRDNVKNNNSSNFeIGELKHAKaSLDD------KVRNLTEERHNLNQRISALRKECDEWKSKYQRNEsldsnhrK 433
Cdd:COG3883 87 ELgERARALYRSGGSVSY-LDVLLGSE-SFSDfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKL-------A 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334351095 434 AFDSLRQELQTTKTQLEETRKTAQQLQTQVIENTTKNSERTSQRIKDKETQIQKLESE 491
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| |
