|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-525 |
3.64e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAglqfennclvgKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsDSRIEMILEESK 452
Cdd:COG1196 392 LRAAAELAA-----------QLEEL----EEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAA 448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 453 TRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-498 |
2.46e-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: 64.31 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 205 TMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKgrelkliIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKE 284
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEK-------LEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 285 saqlLQQLEESRAALRDEQRHLEHQeaengkIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRMATN 364
Cdd:TIGR02168 304 ----KQILRERLANLERQLEELEAQ------LEELESKLDELAEELAELEEKLEEL-KEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 365 ENVDLEELLKGVTNGKAGLQFENNCLVGKLEELsfvsDRNKQDADNARAQLEEEREKHRlatEKLHQENIDYMKTSDSRI 444
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRRERLQQEIEELL---KKLEEAELKELQAELEEL 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17539660 445 EMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQR--ALNSEMANH 498
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-599 |
9.28e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHM-------VDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKE 284
Cdd:TIGR02168 676 RREIEELEEKIEELEEKiaelekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 285 SAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEN---ELASFRQKEKELIDELRM 361
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 362 ATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSfvsdRNKQDADNARAQLEEEREKHRLATEKLhQENIDYMKTSD 441
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE----SELEALLNERASLEEALALLRSELEEL-SEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 442 SRIEMILEESKTRKMMDESTIERLRLDLDneksykkNLEDLLNDLNQRalnsEMANHLQKEgiQSVETYLQMAKKRIEHL 521
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRID-------NLQERLSEEYSL----TLEEAEALE--NKIEDDEEEARRRLKRL 977
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 522 ElelsatnatiefqsQQLDRAGNM-LITEQEIRnqtsvQYKERTSALENQlsqkDAEIENLKRDLQQLVTKHESELKEQ 599
Cdd:TIGR02168 978 E--------------NKIKELGPVnLAAIEEYE-----ELKERYDFLTAQ----KEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-622 |
1.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 272 QELSNILEE--------KEKESAQL--------LQQLEESRAALRDEQRHLEHQeAENGKIVEQLKTvsELNE-KLTMQV 334
Cdd:TIGR02168 155 EERRAIFEEaagiskykERRKETERklertrenLDRLEDILNELERQLKSLERQ-AEKAERYKELKA--ELRElELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 335 KDLQDAsENELASFRQKEKELIDELRMATNE----NVDLEELLKGVTN---GKAGLQFENNCLVGKLEELsfvsDRNKQD 407
Cdd:TIGR02168 232 LRLEEL-REELEELQEELKEAEEELEELTAElqelEEKLEELRLEVSEleeEIEELQKELYALANEISRL----EQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 408 ADNARAQLEEEREKHRLATEKLHQENIDYmktsdsriEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLN 487
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 488 Q--RALNSEMANHLQKEGIQSVEtyLQMAKKRIEHLELELSATNATIEFQSQQLDRAG-NMLITEQEIRNQTSVQYKERT 564
Cdd:TIGR02168 379 EqlETLRSKVAQLELQIASLNNE--IERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660 565 SALENQLSQKDAEIENLKRDLQQlvtkheseLKEQHEQLNVHHQSQQKLHSEAEKLRR 622
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDA--------AERELAQLQARLDSLERLQENLEGFSE 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-629 |
3.80e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESEN-RNLTEKGRELKLIIDSLKsDVTNKRDTAKSSQQREQELSNILEEKEKESAQL--- 288
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKeKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKELESLegs 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 289 -------LQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRM 361
Cdd:PRK03918 254 krkleekIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI-EKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 362 ATNENVDLEELLK---------GVTNGKAGLQFENNCLVGKLEEL-SFVSDRNKQDADNARAQLEEEREKHRLATEKLHQ 431
Cdd:PRK03918 333 LEEKEERLEELKKklkelekrlEELEERHELYEEAKAKKEELERLkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 432 EnIDYMKTSDSRIEMILEESKTRKMM------------DESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHL 499
Cdd:PRK03918 413 R-IGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 500 QKEGIQSVETYLQmakkrIEHLELELSATNA-TIEFQSQQLDRAGNMLIT-EQEIRNQTS-----VQYKERTSALENQLS 572
Cdd:PRK03918 492 ESELIKLKELAEQ-----LKELEEKLKKYNLeELEKKAEEYEKLKEKLIKlKGEIKSLKKeleklEELKKKLAELEKKLD 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660 573 QKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGK 629
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
393-630 |
7.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 393 KLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYM--KTSDSRIEMILEESKTRKMMDESTIERLRLDLD 470
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 471 NEKSYKKNLEDLLNDLNQRALNSEMA-NHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITE 549
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 550 QEIRN--QTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:COG1196 407 EAEEAllERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
...
gi 17539660 628 GKK 630
Cdd:COG1196 487 AEA 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-622 |
9.43e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLL 289
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 290 QQLEESRAALRDEQRHLEhqeaengkivEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDL 369
Cdd:COG4717 195 QDLAEELEELQQRLAELE----------EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 370 EELLKGVTNGKAGLQFennCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILE 449
Cdd:COG4717 265 GGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 450 esktrkmmdestierLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELElsatn 529
Cdd:COG4717 342 ---------------LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK----- 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 530 ATIEFQSQQLDRAGNMLITEQEIRNQTSV-----QYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE-SELKEQHEQL 603
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEEELeeeleELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEEL 481
|
410
....*....|....*....
gi 17539660 604 nvhhqsQQKLHSEAEKLRR 622
Cdd:COG4717 482 ------KAELRELAEEWAA 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-631 |
1.60e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 261 RDTAKSSQQREQELSNiLEEKEKESAQLLQQLEESRAALRDEQRHLEHQeaengkiVEQLKTVSElnekltmQVKDLQDA 340
Cdd:TIGR02168 666 AKTNSSILERRREIEE-LEEKIEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELE-------ELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 341 SENELASFRQKEKELIDELRMATNENVDLEELlkgvtngKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEERE 420
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 421 KHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDES--TIERLRLDLdneKSYKKNLEDLlnDLNQRALNSEmANH 498
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDI---ESLAAEIEEL--EELIEELESE-LEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 499 LQKEgIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLiteqeirnqtsVQYKERTSALENQLSQKDAEI 578
Cdd:TIGR02168 878 LLNE-RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-----------AQLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17539660 579 ENLKRDLQQLVTKHESELKEqheqlnvhhqSQQKLHSEAEKLRREHEALGKKN 631
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIED----------DEEEARRRLKRLENKIKELGPVN 988
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-630 |
1.71e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 219 KKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAA 298
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 299 lrdeqRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEELLKGVTN 378
Cdd:PTZ00121 1394 -----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 379 GKAGLQFENNC-LVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMM 457
Cdd:PTZ00121 1469 AKKADEAKKKAeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 458 DE-STIERLRLDLDNEKSYKKNLEDllNDLNQRALNSEMANHLQKEGIQSV-ETYLQMAKKRIEHLELELSATNATIEFQ 535
Cdd:PTZ00121 1549 DElKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 536 SQQLDRAGNMLIT---EQEIRNQTSVQYKERTSALENQLSQKDAEIEnlKRDLQQLvTKHESELKEQHEQLNVHHQSQQK 612
Cdd:PTZ00121 1627 KAEEEKKKVEQLKkkeAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEA-KKAEEDEKKAAEALKKEAEEAKK 1703
|
410
....*....|....*...
gi 17539660 613 lhseAEKLRREHEALGKK 630
Cdd:PTZ00121 1704 ----AEELKKKEAEEKKK 1717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
268-628 |
2.58e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 268 QQREQELSNILEEKEKEsaqlLQQLE-ESRAA-----LRDEQRHLEHQEAengkiVEQLKTVSELNEKLTMQVKDLQDAS 341
Cdd:COG1196 185 EENLERLEDILGELERQ----LEPLErQAEKAeryreLKEELKELEAELL-----LLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 342 ENELASFRQKEKElIDELRMA-TNENVDLEELLKgvtngkaglqfENNCLVGKLEELSFVSDRNKQDADNARAQLEEERE 420
Cdd:COG1196 256 EELEAELAELEAE-LEELRLElEELELELEEAQA-----------EEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 421 KHRLATEKLHQEnidymKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQ 500
Cdd:COG1196 324 ELAELEEELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 501 KEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmlITEQEIRNQTSVQYKERTSALENQLSQKDAEIEN 580
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE----EEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 17539660 581 LKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALG 628
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
239-605 |
6.32e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 239 LTEKGRELKLIIDSLKSDVTNK---RDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENGK 315
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIdylEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 316 IVEQLKTVSELNEKLTMQVKDLQDASE--NELASFRQKEKELIDELRMATNENV--------DLEELLKGVTNGKAGLQ- 384
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEknNYYKELEERHMKIINDPVYKNRNYIndyfkyknDIENKKQILSNIDAEINk 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 385 FENNclVGKLEEL-SFVSD-----RNKQDADNARAQLEE-----------------EREKHRLATEKLHQENIDYMKTSD 441
Cdd:PRK01156 324 YHAI--IKKLSVLqKDYNDyikkkSRYDDLNNQILELEGyemdynsylksieslkkKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 442 ---SRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRI 518
Cdd:PRK01156 402 idpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 519 E----HLELELSATNATIEFQSQQLDRagnmlITEQEIRnqtsvqykeRTSALENQLSQKDAEIENLKRDLQQLVTKHE- 593
Cdd:PRK01156 482 EekirEIEIEVKDIDEKIVDLKKRKEY-----LESEEIN---------KSINEYNKIESARADLEDIKIKINELKDKHDk 547
|
410
....*....|...
gi 17539660 594 -SELKEQHEQLNV 605
Cdd:PRK01156 548 yEEIKNRYKSLKL 560
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
210-629 |
7.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLL 289
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 290 QQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDE---LRMATNEN 366
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarLLLLLEAE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 367 VDLEELLKGVtnGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEERekhRLATEKLHQENIDYMKTSDS---- 442
Cdd:COG1196 501 ADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI---VVEDDEVAAAAIEYLKAAKAgrat 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 443 --RIEMILEESKTRKMMDESTIERLRLDLDNEKSY----KKNLEDLLNDLNQRALNSEMANHLQKE----------GIQS 506
Cdd:COG1196 576 flPLDKIRARAALAAALARGAIGAAVDLVASDLREadarYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEG 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 507 VETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQ 586
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 17539660 587 QLVTKHESELKEQHEQLNVHHQ---SQQKLHSEAEKLRREHEALGK 629
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIEALGP 781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-627 |
8.70e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELeSENRNLTEKGRELKLIIDSLKSdvtnkrdtakssQQREQELSNILEEKEKESAQLlQQL 292
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEK-RQQLERLRREREKAERYQALLK------------EKREYEGYELLKEKEALERQK-EAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENGK-IVEQLKTVSELNEKLtmqvkdlQDASENELASFRQKEKELIDELRMatnenvdlee 371
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKrLEEIEQLLEELNKKI-------KDLGEEEQLRVKEKIGELEAEIAS---------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 372 llkgvtngkaglqfenncLVGKLEElsfvSDRNKQDADNARAQLEEEREKHRLATEKLHQEnidymktsdsriemilees 451
Cdd:TIGR02169 306 ------------------LERSIAE----KERELEDAEERLAKLEAEIDKLLAEIEELERE------------------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 452 ktrkmmdestIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNAT 531
Cdd:TIGR02169 345 ----------IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 532 IEFQSQQLdragnmliteQEIRNQTSVQyKERTSALENQLSQKDAEIENLKRDLQQLVTKHESElKEQHEQLNvhhQSQQ 611
Cdd:TIGR02169 415 LQRLSEEL----------ADLNAAIAGI-EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-EQELYDLK---EEYD 479
|
410
....*....|....*.
gi 17539660 612 KLHSEAEKLRREHEAL 627
Cdd:TIGR02169 480 RVEKELSKLQRELAEA 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
214-620 |
9.07e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLE 293
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 294 ESRAALrdeQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEnELASFRQKEKELIDELRMATNENVDLEELL 373
Cdd:PRK02224 332 ECRVAA---QAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 374 KGVTNGKAGLQFENNCLVGKLEELSfVSDRNKQDA--------------------------------DNARAQLEEEREK 421
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELE-ATLRTARERveeaealleagkcpecgqpvegsphvetieedRERVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 422 HRLATEKLHQ--ENIDYMKTSDSRIEMILEESKT---RKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMA 496
Cdd:PRK02224 487 LEEEVEEVEErlERAEDLVEAEDRIERLEERREDleeLIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 497 NHLQKEGIQSVETYLQMAKKRIEHLElELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYK---ERTSALENQLSq 573
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFD- 644
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660 574 kDAEIENLKRDLQQLVTKHE------------------------------SELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:PRK02224 645 -EARIEEAREDKERAEEYLEqveekldelreerddlqaeigaveneleelEELRERREALENRVEALEALYDEAEEL 720
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-626 |
1.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLksDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEERLEELRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAENG-KIVEQLKTVSELNEKLTMQVKDLQDA---SENELASFRQKEKELIDELRMAT-NENV 367
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEEleeAQEELEELEEELEQLENELEAAAlEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 368 DLEELLKGVTNGKAGLQFENNCLVGKLEE--------------LSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 434 IDYMKTSDSRIEMILEesktrkmmdestierLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQM 513
Cdd:COG4717 326 AALGLPPDLSPEELLE---------------LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 514 AKKRIEHLELElsatnATIEFQSQQLDRAGNmliteqEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE 593
Cdd:COG4717 391 LEQAEEYQELK-----EELEELEEQLEELLG------ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430
....*....|....*....|....*....|...
gi 17539660 594 SELkEQHEQLNVHHQSQQKLHSEAEKLRREHEA 626
Cdd:COG4717 460 AEL-EQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-627 |
1.66e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 462 IERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDR 541
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 542 AGNMlITEQEIRNQTSVQYKERTSALENQLSQKDAE-IENLKRDLQQLVTKhESELKEQHEQLNVHHQSQQKLHSEAEKL 620
Cdd:COG4942 116 LGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEAL 193
|
....*..
gi 17539660 621 RREHEAL 627
Cdd:COG4942 194 KAERQKL 200
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
214-679 |
2.21e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLVDMEHMVDELESENrnltEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLE 293
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKI----QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 294 ESRAALRDEQRHLEHQeaeNGKIVEQLKTVSELNekltMQVKDLQDASENELasfrqkEKELIDELRMATNENVDLEELL 373
Cdd:TIGR04523 264 KIKKQLSEKQKELEQN---NKKIKELEKQLNQLK----SEISDLNNQKEQDW------NKELKSELKNQEKKLEEIQNQI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 374 KgvtngkaglqfENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDY------MKTSDSRIEMI 447
Cdd:TIGR04523 331 S-----------QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYkqeiknLESQINDLESK 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 448 LEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSA 527
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 528 TNATIEFQSQQLDRAGNMLIT--------EQEIRNQTSVQ--YKERTSALENQLSQKDAEIENLKRDLQqlvtKHESELK 597
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKlneekkelEEKVKDLTKKIssLKEKIEKLESEKKEKESKISDLEDELN----KDDFELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 598 EqhEQLNVHHQSQQKlhsEAEKLRREHEALGKKNCFLGERCKIF---VKDSRSGVMKRSTSSDSLAEFLSKGN-DNETLE 673
Cdd:TIGR04523 556 K--ENLEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELIDQKekeKKDLIKEIEEKEKKISSLEKELEKAKkENEKLS 630
|
....*.
gi 17539660 674 EMMRLI 679
Cdd:TIGR04523 631 SIIKNI 636
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-432 |
3.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQ 291
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKtvsELNEKLTMQVKDLQDASEnELASFRQKEKELIDELRMATNENVDLEE 371
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 372 LLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQE 432
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-623 |
4.37e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 231 ELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQE 310
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 311 AENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKE-KELIDELRMATNENVDLEELLkgvtngkaglqfenNC 389
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL--------------RE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 390 LVGKLEELSFvsdrnkqdadnARAQLEEEREKhrlateklhqenidymktsdsrIEMILEESKTRKMMDESTIERLRLDL 469
Cdd:TIGR02169 817 IEQKLNRLTL-----------EKEYLEKEIQE----------------------LQEQRIDLKEQIKSIEKEIENLNGKK 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 470 DNEKSYKKNLEDLLNDLNQR--ALNSEMANHlqKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLI 547
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRlgDLKKERDEL--EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660 548 TEQEIRNQTSV--QYKERTSALENQLsQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:TIGR02169 942 EDEEIPEEELSleDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
282-623 |
1.29e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 282 EKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSEL-------NEKLTMQVKDLQDASENELASFRQKEkE 354
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVleeheerREELETLEAEIEDLRETIAETERERE-E 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 355 LIDELRMATNENVDLEEllkgvtngkaglqfENNCLVGKLE----ELSFVSDRnKQDADNARAQLEEEREKHRLATEKlH 430
Cdd:PRK02224 277 LAEEVRDLRERLEELEE--------------ERDDLLAEAGlddaDAEAVEAR-REELEDRDEELRDRLEECRVAAQA-H 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 431 QENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETY 510
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 511 LQMAKKRIEHLELELSATNATIEfQSQQLDRAGNMLITEQEIRNQTSV----QYKERTSALENQLSQKDAEIENL----- 581
Cdd:PRK02224 421 RDELREREAELEATLRTARERVE-EAEALLEAGKCPECGQPVEGSPHVetieEDRERVEELEAELEDLEEEVEEVeerle 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 582 ------------------KRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:PRK02224 500 raedlveaedrierleerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-584 |
1.40e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQL--- 288
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELear 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 289 LQQLEESRAALRDEQRHLEHQEAEngkivEQLKTVSELNEKLTMQVKDLqdasENELASFRQKEKELIDELRMATNENVD 368
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 369 LEELLKGVTNGKAGLQFENNCLVGKLEElsfvsdrnkqdadnaraqLEEEREKHRLATEKLHQENIDyMKTSDSRIEMIL 448
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEE------------------LEEELEELEAALRDLESRLGD-LKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 449 EESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNqralnsemANHLQKEGIQSVETYLQMAKKRIEHLELELSAt 528
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE--------DPKGEDEEIPEEELSLEDVQAELQRVEEEIRA- 969
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 529 natiefqsqqLDRAGNMLITEQEIRNQTSVQYKERTSALE---NQLSQKDAEIENLKRD 584
Cdd:TIGR02169 970 ----------LEPVNMLAIQEYEEVLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-542 |
1.43e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 237 RNLTEKGRELKLI-----IDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEA 311
Cdd:COG1196 216 RELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 312 ENGKIVEQLKTVSELNEKLTMQVKDLQ---DASENELASFRQKEKELIDELRMATNENVDLEELLKGVtngkaglqfenn 388
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 389 clvgKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENidymktsdsrIEMILEESKTRKMMDESTIERLRLD 468
Cdd:COG1196 364 ----EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE----------LEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539660 469 LDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRA 542
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
219-627 |
4.96e-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: 50.11 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 219 KKKLVDMEHMVDELESENRNLTEKGR----ELKLIIDSlKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKlqdeNLKELIEK-KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 295 SRAALRDEqrhLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELA----SFRQKEKELIDELRMATNENVDLE 370
Cdd:pfam05483 332 EKEAQMEE---LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 371 ElLKGVTNGKAGLQFENNC-------LVGKLEELSFVSDRNKQDADNARAQL------------EEEREKHRLATEKLhq 431
Cdd:pfam05483 409 E-LKKILAEDEKLLDEKKQfekiaeeLKGKEQELIFLLQAREKEIHDLEIQLtaiktseehylkEVEDLKTELEKEKL-- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 432 ENIDYMKTSDsrieMILEESKtrKMMDESTIERLRLdldneksyKKNLEDLLNDLNQralnsEMANHLQKEGIQSVETYL 511
Cdd:pfam05483 486 KNIELTAHCD----KLLLENK--ELTQEASDMTLEL--------KKHQEDIINCKKQ-----EERMLKQIENLEEKEMNL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 512 qmaKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTK 591
Cdd:pfam05483 547 ---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
410 420 430
....*....|....*....|....*....|....*.
gi 17539660 592 HESELKeqheQLNVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:pfam05483 624 GSAENK----QLNAYEIKVNKLELELASAKQKFEEI 655
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
328-625 |
9.12e-06 |
|
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: 49.35 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 328 EKLTMQVKDLQDA--SENELAS-----FRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFV 400
Cdd:pfam15921 81 EEYSHQVKDLQRRlnESNELHEkqkfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 401 SDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKN-- 478
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 479 --LEDLLndlnqRALNSEMANhlqkegiqSVETYLQMAKKRIEHL----ELELSA-TNATIEFQSQQLDRAGNMLITEQE 551
Cdd:pfam15921 241 fpVEDQL-----EALKSESQN--------KIELLLQQHQDRIEQLisehEVEITGlTEKASSARSQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 552 IRNQTSVqYKERTSALENQLSQKDAEIENLKR-------DLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKL---- 620
Cdd:pfam15921 308 ARNQNSM-YMRQLSDLESTVSQLRSELREAKRmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladl 386
|
....*.
gi 17539660 621 -RREHE 625
Cdd:pfam15921 387 hKREKE 392
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
214-648 |
9.48e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKS------DVTNKRDTAKSSQQREQELSNILEEKEKESAQ 287
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 288 LLQQLEES----RAALRDEQRHLEHQEAE---NGKIVEQLKTVSELNEKLTmqvkdLQDASENELASFRQKEKELIDELR 360
Cdd:TIGR00618 516 ARQDIDNPgpltRRMQRGEQTYAQLETSEedvYHQLTSERKQRASLKEQMQ-----EIQQSFSILTQCDNRSKEDIPNLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 361 matNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTS 440
Cdd:TIGR00618 591 ---NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 441 DSRIEMILEESKTRKMMDESTIERLRLD---LDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKR 517
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 518 IEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIEN-LKRDLQQL---VTKHE 593
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeIPSDEDILnlqCETLV 827
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 594 SELKEQHEQLNVHHQSQ----QKLHSEAEKLRREHEALGKKNCFLGERCKIFVKDSRSG 648
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLgeitHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKI 886
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
213-620 |
1.03e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEH----MVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQRE--QELSNILEEKEKESA 286
Cdd:PRK04863 293 RELYTSRRQLAAEQYrlveMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAdlEELEERLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 287 QLLQQLEESRAALR--------------DEQRHLEHQEAENGKI---VEQLKTVSELNEKLTMQVKDLQDAseneLASFR 349
Cdd:PRK04863 373 EADEQQEENEARAEaaeeevdelksqlaDYQQALDVQQTRAIQYqqaVQALERAKQLCGLPDLTADNAEDW----LEEFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 350 QKEKELIDELRMATNENVDLEEllkgvtngkAGLQFENNC-LVGKLeelsfVSDRNKQDADNARAQLEEEREKHRLATEK 428
Cdd:PRK04863 449 AKEQEATEELLSLEQKLSVAQA---------AHSQFEQAYqLVRKI-----AGEVSRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 429 LHQenidymktsdsrIEMILEEsktrkmmdestierLRLDLDNEksykKNLEDLLNDLNQRAlnsemanHLQKEGIQSVE 508
Cdd:PRK04863 515 LQQ------------LRMRLSE--------------LEQRLRQQ----QRAERLLAEFCKRL-------GKNLDDEDELE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 509 TYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQL 588
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQL 636
|
410 420 430
....*....|....*....|....*....|..
gi 17539660 589 VTkHESELKEQHEQLNvhhQSQQKLHSEAEKL 620
Cdd:PRK04863 637 LE-RERELTVERDELA---ARKQALDEEIERL 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
265-626 |
1.07e-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: 48.97 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 265 KSSQQREQElsnilEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQvkdlqdaSENE 344
Cdd:pfam17380 282 KAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-------RERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 345 LASFRQKEKElidelrmATNENVDLEELLKGVTNGKaglqfennclvgKLEELSF----VSDRNKQDADNARAQ--LEEE 418
Cdd:pfam17380 350 LERIRQEERK-------RELERIRQEEIAMEISRMR------------ELERLQMerqqKNERVRQELEAARKVkiLEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 419 REKhRLATEKLHQENIDYMKTSDSRIEM-ILEESKTRKMmdestiERLRLDldnEKSYKKNLEDLLNDLNQRAlnsemAN 497
Cdd:pfam17380 411 RQR-KIQQQKVEMEQIRAEQEEARQREVrRLEEERAREM------ERVRLE---EQERQQQVERLRQQEEERK-----RK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 498 HLQKEGIQSVETYLQMAKKRIEHLELElSATNATIEFQsqqldRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKdaE 577
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEE-----RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ--E 547
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17539660 578 IENLKRDLQQL--VTKHESELKEQHEQLNVHHQSQqklhsEAEKLRREHEA 626
Cdd:pfam17380 548 MEERRRIQEQMrkATEERSRLEAMEREREMMRQIV-----ESEKARAEYEA 593
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
215-618 |
1.59e-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: 48.89 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 215 LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 295 SRAALRDEqrhlehqeaengKIVEQLKTVSELNEKLTMQVKDLQDASENELA--SFRQKEKELIDELRMATNENVDLEEL 372
Cdd:TIGR00606 784 AKVCLTDV------------TIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqQVNQEKQEKQHELDTVVSKIELNRKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENID--YMKTSDSRIEMILEE 450
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetFLEKDQQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 451 SKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANhlqkegIQSVETYLQMAKKRIEHLELELSATNA 530
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE------LNTVNAQLEECEKHQEKINEDMRLMRQ 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 531 TIEFQSQQlDRAGNMLITEQEIRNQTSVQYKERTSAL----ENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEqlnvh 606
Cdd:TIGR00606 1006 DIDTQKIQ-ERWLQDNLTLRKRENELKEVEEELKQHLkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKG----- 1079
|
410
....*....|..
gi 17539660 607 hQSQQKLHSEAE 618
Cdd:TIGR00606 1080 -YEKEIKHFKKE 1090
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
251-625 |
1.76e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 251 DSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRH----LEHQEAENGKIVEQLKTVSEL 326
Cdd:PLN02939 43 SSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHnrasMQRDEAIAAIDNEQQTNSKDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 327 NEKLTMQVKDLQDASENElasfrQKEKELIDELRMATNEnvDLEELLKGvtngKAGLQFENNCLVGKLEEL---SFVSDR 403
Cdd:PLN02939 123 EQLSDFQLEDLVGMIQNA-----EKNILLLNQARLQALE--DLEKILTE----KEALQGKINILEMRLSETdarIKLAAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 404 NKQDADNARAQLEEEREK--HRLATEKlhqenidymkTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLED 481
Cdd:PLN02939 192 EKIHVEILEEQLEKLRNEllIRGATEG----------LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 482 LLNdlnQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSvqyK 561
Cdd:PLN02939 262 LEK---ERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVD---K 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 562 ERTSALENQLSQKDAE-IENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHE 625
Cdd:PLN02939 336 LEASLKEANVSKFSSYkVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
214-630 |
2.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKliidSLKSDVTNKRDTAKSSQQREQELSNILEEKEKesaqllqqLE 293
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSR--------LE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 294 ESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDAS--ENELASFRQKEK-----ELIDELRMATNEN 366
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakKEELERLKKRLTgltpeKLEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 367 VDLEELLKGVTNGKAGLQFENNCLVGKLEELsfvsDRNKQDADNARAQLEEEREKHRLATEKLHQENIDY-MKTSDSRIE 445
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEEL----KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 446 MILEESKT--RKMMDESTIERLRLDLD-----NEKSYKKNLEDLLNDLNQRALNSEMANHLQKE---------GIQSVET 509
Cdd:PRK03918 477 KLRKELREleKVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikslkkeleKLEELKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 510 YLQMAKKRIEHLELELSATNATIE---FQS--------QQLDRAGNMLIT----EQEIRNQTSVQYKERT--SALENQLS 572
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEelgFESveeleerlKELEPFYNEYLElkdaEKELEREEKELKKLEEelDKAFEELA 636
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 573 QKDAEIENLKRDLQQL---------------VTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:PRK03918 637 ETEKRLEELRKELEELekkyseeeyeelreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
268-630 |
2.57e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 268 QQREQELSNILEEKEKESAQLLQQLEESRAALRD------EQRHLEHQEAENGKIV-EQLKTVSELNEKLTMQVKDLQDA 340
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 341 SENELASfrqkEKELIDELRMATNENVDL----EELLKGVTNGKAGLQF---ENNCLVGKLEELSfvsdRNKQDadnara 413
Cdd:pfam05483 305 LQRSMST----QKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFvvtEFEATTCSLEELL----RTEQQ------ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 414 QLEEEREKHRLATEKLHQEN--IDYMKTSDSRIEMILEESKT-----RKMMDES-TIERLRLDLDNE--------KSYKK 477
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSseLEEMTKFKNNKEVELEELKKilaedEKLLDEKkQFEKIAEELKGKeqelifllQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 478 NLEDLLNDLNQRALNSE--------MANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGN----- 544
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEhylkevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkkqee 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 545 MLITEQEIRNQTSVQYKERTSALENQLSQKDAEI-------ENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEA 617
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkckldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
410
....*....|...
gi 17539660 618 EKLRREHEALGKK 630
Cdd:pfam05483 611 EELHQENKALKKK 623
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
237-620 |
2.74e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 237 RNLTEKGRELKLIIDsLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEaengKI 316
Cdd:COG3096 275 RHANERRELSERALE-LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE----KI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 317 VEQLKTVSELNEKL---TMQVKDLQDASENELASFRQKEKElIDELRmatNENVDLEELLKgVTNGKAgLQFENncLVGK 393
Cdd:COG3096 350 ERYQEDLEELTERLeeqEEVVEEAAEQLAEAEARLEAAEEE-VDSLK---SQLADYQQALD-VQQTRA-IQYQQ--AVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 394 LEELSFVSDRNKQDADNARAQLEEEREKHRLATEKL--HQENIDYMKTSDSRIEMILEesKTRKMMDE-----------S 460
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleLEQKLSVADAARRQFEKAYE--LVCKIAGEversqawqtarE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 461 TIERLRlDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAkkriEHLELELSATNATIEFQSQQLD 540
Cdd:COG3096 500 LLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 541 RAGNMLITEQEIRNQTSVQYKE-------------RTSALENQLSQKDAEIENLKRDLQQLVtKHESELKEQHEQLNvhh 607
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKElaarapawlaaqdALERLREQSGEALADSQEVTAAMQQLL-EREREATVERDELA--- 650
|
410
....*....|...
gi 17539660 608 QSQQKLHSEAEKL 620
Cdd:COG3096 651 ARKQALESQIERL 663
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
406-603 |
3.08e-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: 46.07 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 406 QDADNARAQLEEEREKHRLATEKLhQENIDYMKTSDSRIEMILEESKTRkmmdestIERLRLDLDNEKSYKKNLEDLLNd 485
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAEL-EDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEARIKKYEEQLG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 486 lnqRALNSEMANHLQKEgiqsvetyLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmliteQEIRNQTSVQYKERTS 565
Cdd:COG1579 84 ---NVRNNKEYEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKA 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 17539660 566 ALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQL 603
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
207-588 |
7.15e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 207 KYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESA 286
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 287 QLLQQLEESRAALRDEQRHLEHQEA-ENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMAT-- 363
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAArLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaa 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 364 ---NENVDLE-------ELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG1196 547 alqNIVVEDDevaaaaiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 434 IDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVEtyLQM 513
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA--EEE 704
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 514 AKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQL 588
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-612 |
9.33e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 197 IAEVVDSPTMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQ---REQE 273
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEElkgKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 274 LSNILEEKEKESAQLLQQLEESRAA-------LRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQ---DASEN 343
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSeehylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlelKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 344 ELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEE-------LSFVSDRNKQDADNARAQLE 416
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEnarsieyEVLKKEKQMKILENKCNNLK 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 417 EEREKHRLATEKLHQENIDYMKTSDSriemileESKTRKMMdESTIERLRLDLDNEK--------SYKKNLED------- 481
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSA-------ENKQLNAY-EIKVNKLELELASAKqkfeeiidNYQKEIEDkkiseek 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 482 LLNDLNQRALNSEMANHLQKEgiqsvetylqmAKKRIEHlelELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYK 561
Cdd:pfam05483 673 LLEEVEKAKAIADEAVKLQKE-----------IDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17539660 562 ERTSALENQLSQKDAEIENLKRDLQqlVTKHESELKEQHEQLNVHHQSQQK 612
Cdd:pfam05483 739 SAKAALEIELSNIKAELLSLKKQLE--IEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
275-490 |
1.12e-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: 45.53 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 275 SNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAE----NGKIVEQLKTVSELNEKLTMQVKDLQDAsENELASFRQ 350
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAEL-EKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 351 KEKELIDEL--RMATNENVDLEELLKGVTNGKAGLQFENNclvgkLEELSFVSDRNKQDADNARAQLEEEREKHRLATEK 428
Cdd:COG4942 98 ELEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539660 429 LHQENIDYMKTSDSRIEMILEESKTRKMMD--ESTIERLRLDLDNEKSYKKNLEDLLNDLNQRA 490
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLArlEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
228-621 |
1.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 228 MVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKssQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLE 307
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 308 H-QEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEnelaSFRQKEKELIDELRMATNEnvdleellkgvtngkaglqfe 386
Cdd:pfam15921 303 IiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR----MYEDKIEELEKQLVLANSE--------------------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 387 nnclvgkLEELSFVSDRNKQDADNARAQLEEerekhrlATEKLHQEnidymktsdsRIEMILEESKTRKMMDES-----T 461
Cdd:pfam15921 358 -------LTEARTERDQFSQESGNLDDQLQK-------LLADLHKR----------EKELSLEKEQNKRLWDRDtgnsiT 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 462 IERLRLDLDNEKSYKKNLEDLLndlnqRALNSEMANHLQKegiqsvetylQMAKKRIEHLELE-LSATNATIEFQSQQLD 540
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALL-----KAMKSECQGQMER----------QMAAIQGKNESLEkVSSLTAQLESTKEMLR 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 541 RagnmlITEQEIRNQTSVQYKERT-SALENQLSQKDAEIENLKRDLQQLVTKHESELKE-QHEQLNVHHQSQQKLHSEAE 618
Cdd:pfam15921 479 K-----VVEELTAKKMTLESSERTvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEAL 553
|
...
gi 17539660 619 KLR 621
Cdd:pfam15921 554 KLQ 556
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
445-630 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 445 EMILEESKTRKMMDE-----STIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEG----IQSVETYLQMAK 515
Cdd:COG4913 215 EYMLEEPDTFEAADAlvehfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 516 KRIEHLELELSATNATIEFQSQQLDRAGNMLIT----------------EQEI---------RNQTSVQYKERTSALENQ 570
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdrleqlEREIerlereleeRERRRARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 571 LSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
213-630 |
1.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQ---------------EAENGKIVEQLKTVSELnekltMQVKDL----QDASENELASFR---- 349
Cdd:COG4913 418 RRELRELEAEIASLERRksniparllalrdalAEALGLDEAELPFVGEL-----IEVRPEeerwRGAIERVLGGFAltll 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 350 ------QKEKELIDELRMATNenVDLEELLKGVTNgKAGLQFENNCLVGKLE-----ELSFVSDRNKQDADNARAQLEEE 418
Cdd:COG4913 493 vppehyAAALRWVNRLHLRGR--LVYERVRTGLPD-PERPRLDPDSLAGKLDfkphpFRAWLEAELGRRFDYVCVDSPEE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 419 REKHRLA-TE--------KLHQENIDYMKTSD--------SRIEMILEEsktrkmmdestIERLRLDLDNEKSYKKNLED 481
Cdd:COG4913 570 LRRHPRAiTRagqvkgngTRHEKDDRRRIRSRyvlgfdnrAKLAALEAE-----------LAELEEELAEAEERLEALEA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 482 LLNDLNQRAlnsemANHLQKEGIQSVETYLQMAKKRIEHLELE---LSATNATIEFQSQQLDRAgnmlitEQEIR--NQT 556
Cdd:COG4913 639 ELDALQERR-----EALQRLAEYSWDEIDVASAEREIAELEAElerLDASSDDLAALEEQLEEL------EAELEelEEE 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 557 SVQYKERTSALENQLSQKDAEIENLKRDLQQLVTK----HESELKEQHEQL---NVHHQSQQKLHSEAEKLRREHEALGK 629
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarleLRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEE 787
|
.
gi 17539660 630 K 630
Cdd:COG4913 788 E 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-631 |
1.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 229 VDELESENRNLTEKGRELKLIIDSLKSDVtnkrdtakssqQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEH 308
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 309 QEAEngkiVEQLKTVSELNEKLTMQVKDLqdasENELASFRQKEKELIDELRMATNENVDLEEllkgvtngkaglqfenn 388
Cdd:PRK03918 226 LEKE----VKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERIEELKKEIEELEE----------------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 389 cLVGKLEELsfvsdrnKQDADNARAqLEEEREKHRLATEKLHQENIDYMKTSDSRIEMI--LEESKTRKMMDESTIERLR 466
Cdd:PRK03918 281 -KVKELKEL-------KEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLKELE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 467 LDLDNEKSYKKNLEDLlndlnqRALNSEMANHLQKEGIQSVET------YLQMAKKRIEHLELELSATNATIEFQSQQLD 540
Cdd:PRK03918 352 KRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKlekeleELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 541 RAGNML--------ITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLnvhhqsqqK 612
Cdd:PRK03918 426 KAIEELkkakgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--------K 497
|
410
....*....|....*....
gi 17539660 613 LHSEAEKLRREHEALGKKN 631
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYN 516
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
213-630 |
2.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDT-----AKSSQQREQELSNILEEKEKeSAQ 287
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelkkAAAAKKKADEAKKKAEEKKK-ADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 288 LLQQLEESRAALRDEQRHLEHQEAEN-GKIVEQLKTVSELNEKLTMQVKdlqdasENELASFRQKEKELIDELRMATNEN 366
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEaKKKAEEAKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADEAKKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 367 VDLEELLKGVTNGKAGlQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYM--------K 438
Cdd:PTZ00121 1510 KKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 439 TSDSRIEMIL---EESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAK 515
Cdd:PTZ00121 1589 AEEARIEEVMklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 516 KRIEHLEL--ELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSvQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHE 593
Cdd:PTZ00121 1669 KAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA-EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
410 420 430
....*....|....*....|....*....|....*..
gi 17539660 594 SELKEQHEQLNVHHQSQQKlHSEAEKLRREHEALGKK 630
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEE-EKKAEEIRKEKEAVIEE 1783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
459-627 |
2.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 459 ESTIERLRLDLDNEKSYKKNLEDLLNDLNQRAlnsemaNHLQKEgIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQ 538
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL------EELNEE-YNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 539 LD-------RAGNMLITEQEIRNQTSVQ-YKERTSALENQLSQKDAEIENLKRDLQQLVTKhESELKEQHEQLNVHHQSQ 610
Cdd:COG3883 88 LGeraralyRSGGSVSYLDVLLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAK-KAELEAKLAELEALKAEL 166
|
170
....*....|....*..
gi 17539660 611 QKLHSEAEKLRREHEAL 627
Cdd:COG3883 167 EAAKAELEAQQAEQEAL 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
212-487 |
4.58e-04 |
|
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: 43.86 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKsdvtnkrdtaKSSQQREQELSNILEEKEKESAQlLQQ 291
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----------KLNQQKDEQIKKLQQEKELLEKE-IER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKTvseLNEKLTMQVKDLQDASENELASFRQKEKEL---IDELRMATNENVD 368
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKIKQNLEQKQKELkskEKELKKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 369 LEELLKGVTNGKAGL-----QFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSR 443
Cdd:TIGR04523 508 LEEKVKDLTKKISSLkekieKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17539660 444 IEMILEESKTRK------MMDESTIERLRLDLDNEKSYKKNLEDLLNDLN 487
Cdd:TIGR04523 588 QELIDQKEKEKKdlikeiEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
270-618 |
4.83e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 270 REQELSNILEEKEKESAQLLQ-------QLEESRAALRDEQRHLEHQEAENGKIVEQLKTV----SELNEKLTMQVKDLQ 338
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQaqeaanrQREKEKERYKRDREQWERQRRELESRVAELKEElrqsREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 339 DASEnELAsfrqKEKELIDELRMATNENV-DLEELLKGVTNGKaglqfennclVGKLEELsfvsDRNKQDADNARAQLEE 417
Cdd:pfam07888 108 ASSE-ELS----EEKDALLAQRAAHEARIrELEEDIKTLTQRV----------LERETEL----ERMKERAKKAGAQRKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 418 EREKHRLATEKLHQ--ENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDL--------- 486
Cdd:pfam07888 169 EEAERKQLQAKLQQteEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrslqerlna 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 487 NQR---ALNSEMAN----------HLQKEGIQSVETYLQMAKKRI-------------EHLELELSATNATIEFQSQQLD 540
Cdd:pfam07888 249 SERkveGLGEELSSmaaqrdrtqaELHQARLQAAQLTLQLADASLalregrarwaqerETLQQSAEADKDRIEKLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539660 541 RAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAE 618
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
218-347 |
5.52e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 218 AKKKLvDMEHMVDELESenrnLTEKGRELKLIIDSLKsdvtnkRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRA 297
Cdd:COG0542 400 ARVRM-EIDSKPEELDE----LERRLEQLEIEKEALK------KEQDEASFERLAELRDELAELEEELEALKARWEAEKE 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17539660 298 ALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDA-SENELAS 347
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAE 519
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
288-631 |
5.86e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 288 LLQQLEESRAALRDEQRHLEHQEA-----ENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMA 362
Cdd:pfam02463 138 LVQGGKIEIIAMMKPERRLEIEEEaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 363 TNENVDLEELLKgvtnGKAGLQFENNCLVGKLEELSfvsdRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDS 442
Cdd:pfam02463 218 KLELEEEYLLYL----DYLKLNEERIDLLQELLRDE----QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 443 RIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLE 522
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 523 LELSATNATIEFQSQQLDRAGNMLITEQEIRNQtsvqyKERTSALENQLSQK---DAEIENLKRDLQQLVTKHESELKEQ 599
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKEEELELKSE-----EEKEAQLLLELARQledLLKEEKKEELEILEEEEESIELKQG 444
|
330 340 350
....*....|....*....|....*....|..
gi 17539660 600 HEQLNVHHQSQQKLHSEAEKLRREHEALGKKN 631
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
212-623 |
8.25e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNIL-------EEKEKE 284
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILhelesrlEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 285 SAQLLQQLEESRAALRDEQRHLEHQEAENGK--------------IVEQLKTVSELNEKLTMQVKDLQDaSENELASFRQ 350
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEE-RISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 351 KEKELIDELRMATNEN----VDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHeamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 427 EKLHQENIDYMKTSDSRIEMileesktrkmmdESTIERLRLDLDNEKSYKKNLEDLLNDLNQ--RALNSEMANHL----- 499
Cdd:pfam01576 250 ARLEEETAQKNNALKKIREL------------EAQISELQEDLESERAARNKAEKQRRDLGEelEALKTELEDTLdttaa 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 500 QKEGIQSVETYLQMAKKRIEHlelELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIe 579
Cdd:pfam01576 318 QQELRSKREQEVTELKKALEE---ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL- 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 17539660 580 nlkRDLQQLVTKHESELKEQHEQLnvhhQSQQKLHSEAEKLRRE 623
Cdd:pfam01576 394 ---RTLQQAKQDSEHKRKKLEGQL----QELQARLSESERQRAE 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-452 |
1.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQL 292
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EesRAALRDEQRHLEHQEAENGKIveqlktvselneKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEEL 372
Cdd:COG4942 114 Y--RLGRQPPLALLLSPEDFLDAV------------RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 373 LKGVTNGKAGLQfennclvgkleelsfvsdRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEESK 452
Cdd:COG4942 180 LAELEEERAALE------------------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
344-617 |
1.42e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 344 ELASFRQKEKELIDELRmatNEN-VDLEELLKGVTNGKAGLQFENnclvgkLEELSFVSDRNKQDADNARAQLEEEREKH 422
Cdd:PRK05771 10 LIVTLKSYKDEVLEALH---ELGvVHIEDLKEELSNERLRKLRSL------LTKLSEALDKLRSYLPKLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 423 RLATEKLHQEnidymktSDSRIEMILEESKtrkmmdeSTIERLRlDLDNEKsykKNLEDLLNDLNQ-RALNSEMANHLQK 501
Cdd:PRK05771 81 VKSLEELIKD-------VEEELEKIEKEIK-------ELEEEIS-ELENEI---KELEQEIERLEPwGNFDLDLSLLLGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 502 EGIqSVETYLqMAKKRIEHLELELSATNATIEFQSQQLDRAgnMLITEQEIRNQTSVQYK----------------ERTS 565
Cdd:PRK05771 143 KYV-SVFVGT-VPEDKLEELKLESDVENVEYISTDKGYVYV--VVVVLKELSDEVEEELKklgferleleeegtpsELIR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17539660 566 ALENQLSQKDAEIENLKRDLQQLVTKHESELKEQHEQLnvhhqSQQKLHSEA 617
Cdd:PRK05771 219 EIKEELEEIEKERESLLEELKELAKKYLEELLALYEYL-----EIELERAEA 265
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
550-626 |
1.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 550 QEIRNQTSVQYKERTS---ALENQLSQKDaeiENLKRDLQQLvTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEA 626
Cdd:PRK12704 67 HKLRNEFEKELRERRNelqKLEKRLLQKE---ENLDRKLELL-EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
212-358 |
1.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 212 DRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQR----EQELSNILEEKEKESAQ 287
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17539660 288 L-LQQLEESRAALRDEQRHLEHQEAEngkIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDE 358
Cdd:COG1579 96 KeIESLKRRISDLEDEILELMERIEE---LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
500-603 |
1.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 500 QKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAgnmlitEQEIRNQTsvqykERTSALENQLSQKDAEIE 579
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL------ERRIAALA-----RRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....
gi 17539660 580 NLKRDLQQLvtkhESELKEQHEQL 603
Cdd:COG4942 87 ELEKEIAEL----RAELEAQKEEL 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-630 |
1.88e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 209 MRSDRE--LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQReqelsniLEEKEKESA 286
Cdd:pfam01576 188 MISDLEerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR-------LEEETAQKN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 287 QLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQD--ASENELASFRQKEkelIDELRMATN 364
Cdd:pfam01576 261 NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDttAAQQELRSKREQE---VTELKKALE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 365 ENVDLEEllkgvtngkaglqfennclvgkleelsfvsdrnkqdadnarAQLEEEREKHRLATEKLhQENIDYMKTSDSRI 444
Cdd:pfam01576 338 EETRSHE-----------------------------------------AQLQEMRQKHTQALEEL-TEQLEQAKRNKANL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 445 E---MILEESKTRKMMDESTIERLRLDLDNEKsykKNLEDLLNDLNQRALNSEMA--------NHLQKEgIQSVETYLQM 513
Cdd:pfam01576 376 EkakQALESENAELQAELRTLQQAKQDSEHKR---KKLEGQLQELQARLSESERQraelaeklSKLQSE-LESVSSLLNE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 514 AKKRIEHLELELSATNATIEFQSQQLDRAgnmliTEQEIRNQTSV-QYKERTSALENQLSQKDAEIENLKRDLQQLvTKH 592
Cdd:pfam01576 452 AEGKNIKLSKDVSSLESQLQDTQELLQEE-----TRQKLNLSTRLrQLEDERNSLQEQLEEEEEAKRNVERQLSTL-QAQ 525
|
410 420 430
....*....|....*....|....*....|....*...
gi 17539660 593 ESELKEQHEQLNvhhQSQQKLHSEAEKLRREHEALGKK 630
Cdd:pfam01576 526 LSDMKKKLEEDA---GTLEALEEGKKRLQRELEALTQQ 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-331 |
1.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 222 LVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRD 301
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
90 100 110
....*....|....*....|....*....|
gi 17539660 302 EQRHLEHQEAENGKIVEQLKTVSELNEKLT 331
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
215-623 |
2.03e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 215 LKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEE 294
Cdd:PTZ00440 765 LYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 295 sraalrdeqrhlehqEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENelasfrqkeKELIDELRMATNENVDLEELLK 374
Cdd:PTZ00440 845 ---------------EDENLNLKELEKEFNENNQIVDNIIKDIENMNKN---------INIIKTLNIAINRSNSNKQLVE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 375 GVTNGKAGL---------QFENNCLVGKLEELSFVSDRNKqdadnaraqlEEEREKHRLATEKLHQENIDymktsdsrIE 445
Cdd:PTZ00440 901 HLLNNKIDLknkleqhmkIINTDNIIQKNEKLNLLNNLNK----------EKEKIEKQLSDTKINNLKMQ--------IE 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 446 MILEESKTRKM----MDESTIERLRLDLDNEKSYKKNLEDLlnDLNQRALNSEMANHLQKEGIQSVETYLQMAK------ 515
Cdd:PTZ00440 963 KTLEYYDKSKEningNDGTHLEKLDKEKDEWEHFKSEIDKL--NVNYNILNKKIDDLIKKQHDDIIELIDKLIKekgkei 1040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 516 -----KRIEHLElELSATNATIEFqSQQLDRAGNMLITEQEIrnqtsvQYKERTSALENQLSQKDAEIENLKRDLQQLVT 590
Cdd:PTZ00440 1041 eekvdQYISLLE-KMKTKLSSFHF-NIDIKKYKNPKIKEEIK------LLEEKVEALLKKIDENKNKLIEIKNKSHEHVV 1112
|
410 420 430
....*....|....*....|....*....|...
gi 17539660 591 KHESELKEQHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:PTZ00440 1113 NADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKE 1145
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
266-630 |
2.22e-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: 41.88 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 266 SSQQREQELSNILEE--KEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASEN 343
Cdd:TIGR00618 220 RKQVLEKELKHLREAlqQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 344 E-LASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEElsfvSDRNKQDADNARAQLEEEREKH 422
Cdd:TIGR00618 300 KaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ----EIHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 423 RLaTEKLHQenidymktsdsriemiLEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKE 502
Cdd:TIGR00618 376 TL-TQHIHT----------------LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 503 GI----QSVETYLQMAKKRIEHLELELSATNATiEFQSQQLDRagnmlITEQEIRNQTSV------------QYKERTSA 566
Cdd:TIGR00618 439 YAelcaAAITCTAQCEKLEKIHLQESAQSLKER-EQQLQTKEQ-----IHLQETRKKAVVlarllelqeepcPLCGSCIH 512
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660 567 LENQLSQKDaEIENLKRDLQQL---VTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:TIGR00618 513 PNPARQDID-NPGPLTRRMQRGeqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC 578
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
201-624 |
2.82e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 201 VDSPTMKYMRSDRELKTAKKKLV-DMEHMVDELESENRNLtEKGRELKLIIDSLKS-------DVTNKRDTAKSSQQREQ 272
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESL-EKVSSLTAQLESTKEmlrkvveELTAKKMTLESSERTVS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 273 ELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEAENgkivEQLKTVSELNEKLTMQVkdlqdasenelasfrqKE 352
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG----DHLRNVQTECEALKLQM----------------AE 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 353 KELIDELRMATNENVDLEELLKGVTNG-----KAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEE-EREKHRLAT 426
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGamqveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVKLVN 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 427 EKlhQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQS 506
Cdd:pfam15921 640 AG--SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 507 VETYLQMAKKRIEHLELELSATNATIE-FQS--QQLDRAGNMLITEQEIRNQTSVQYKERTSALENQLSQKDAEIENLK- 582
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAKRGQIDaLQSkiQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRs 797
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 17539660 583 --RDLQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREH 624
Cdd:pfam15921 798 qeRRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQH 841
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
213-524 |
3.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 213 RELKTAKKKLvdmEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQlLQQL 292
Cdd:COG4372 45 EELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-LEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 293 EESRAALRDEQRHLEHQEAE-NGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRMATNENVDLEE 371
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAElQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 372 LLKGVTNGKAGLQFENnclvgKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQENIDYMKTSDSRIEMILEES 451
Cdd:COG4372 201 ELAEAEKLIESLPREL-----AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539660 452 KTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELE 524
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
214-429 |
3.43e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLvdMEHMVDELESEN---RNLTEKGRELKLIIDSLKSDVTNKRDTAKssqqREQELSNILEEKEKESAQLLQ 290
Cdd:PRK03918 504 QLKELEEKL--KKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEELAELLK 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 291 QLEE-SRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLtmqvkDLQDASENELASFRQKEKELIDELRMATNENVDL 369
Cdd:PRK03918 578 ELEElGFESVEELEERLKELEPFYNEYLELKDAEKELEREE-----KELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 370 -----EELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLeEEREKHRLATEKL 429
Cdd:PRK03918 653 ekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKL 716
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
231-374 |
3.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 231 ELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALR-----DEQRH 305
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 306 LEHQEAENGKIVEQL-KTVSELNEKLTMQVKDLQDAsENELASFRQKEKELIDELRMATNE-NVDLEELLK 374
Cdd:COG1579 94 LQKEIESLKRRISDLeDEILELMERIEELEEELAEL-EAELAELEAELEEKKAELDEELAElEAELEELEA 163
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
511-623 |
4.82e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 40.13 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 511 LQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEIRNQTSVQyKERTSALENQLSQ-------KDAEIENLKR 583
Cdd:pfam10186 28 LARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLLKSEVAIS-NERLNEIKDKLDQlrreiaeKKKKIEKLRS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17539660 584 DLQQLVTKHES---ELKE-QHEQLNVHHQSQQKLHSEAEKLRRE 623
Cdd:pfam10186 107 SLKQRRSDLESasyQLEErRASQLAKLQNSIKRIKQKWTALHSK 150
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-525 |
5.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 198 AEVVDSPTMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQqREQELSNI 277
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 278 LEEKEKESAQL-LQQLEESRAALRDEQRHLE--HQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKE 354
Cdd:PTZ00121 1662 KAAEEAKKAEEdKKKAEEAKKAEEDEKKAAEalKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 355 ---LIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLV-----GKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:PTZ00121 1742 dkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeldEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 427 EKLHQENIDYMKTSDSRIEMILEESKtrkmmdesTIERLRLDLDNEKSYKKNLE-------DLLNDLNQRALNSEMANHL 499
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEAD--------AFEKHKFNKNNENGEDGNKEadfnkekDLKEDDEEEIEEADEIEKI 1893
|
330 340
....*....|....*....|....*.
gi 17539660 500 QKEGIQSVETYLQMAKKRIEHLELEL 525
Cdd:PTZ00121 1894 DKDDIEREIPNNNMAGKNNDIIDDKL 1919
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
205-488 |
5.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 205 TMKYMRSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSdvtnkrdtakssqqREQELSNILEEKEKE 284
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE--------------KIEKLESEKKEKESK 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 285 SAQLLQQLEESRAALRDEQrhLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQDASE-------NELASFRQKEKELID 357
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEkekkdliKEIEEKEKKISSLEK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 358 ELRMATNENVDLEELLKGVTNGKAGLQfennclvgklEELSFVsdrnKQDADNARAQLEEEREKHRLATEKLhQENIDYM 437
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKNKLK----------QEVKQI----KETIKEIRNKWPEIIKKIKESKTKI-DDIIELM 682
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17539660 438 KTSDSRIEMILEESKTRKMMD------ESTIERLRLDLDNEKSYKKNLEDLLNDLNQ 488
Cdd:TIGR04523 683 KDWLKELSLHYKKYITRMIRIkdlpklEEKYKEIEKELKKLDEFSKELENIIKNFNK 739
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
214-647 |
5.57e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 214 ELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKssqQREQELSNILEE----------KEK 283
Cdd:TIGR04523 48 ELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN---KLNSDLSKINSEikndkeqknkLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 284 ESAQLLQQLEESRAALRDEQRHLEHQEAE----NGKIVEQLKTVSELNEKLTMQVKDLQDASEN---------------- 343
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKNidkiknkllklellls 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 344 ELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHR 423
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 424 LATEKLHQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANHLQKEG 503
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 504 IQSVETYLQMAKKR-------IEHLELELSATNATIEFQSQQ----------LDRAGNMLITEQEIRNQTSVQYKERTSA 566
Cdd:TIGR04523 365 LEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLnqqkdeqikkLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 567 LENQLSQKDAEIENLKRDLQQLvtkhESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKKNCFLGERCKIFVKDSR 646
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESL----ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
.
gi 17539660 647 S 647
Cdd:TIGR04523 521 S 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
402-630 |
5.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 402 DRNKQDADNARAQLEEEREKHRLATEKL--HQENIDYMKTSDSRIEMILEESKTRKMMDESTIERLRLDLDNEKsykKNL 479
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 480 EDLLNDLNQRALNSEMANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEfqsqQLDRAGNMLITEQEIRNQTSVQ 559
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539660 560 YKERTSALENQLSQKdaeienlkrdlQQLVTKHESELKEQHEQLNVHHQSQQKLHSEAEKLRREHEALGKK 630
Cdd:COG4942 183 LEEERAALEALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
479-627 |
6.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 479 LEDLLNDLNQRALNSE--MANHLQKEGIQSVETYLQMAKKRIEHLELELSATNATIEFQSQQLDRAGNMLITEQEI---- 552
Cdd:COG3206 180 LEEQLPELRKELEEAEaaLEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 553 -RNQTSVQYKERTSALENQLSQK--------------DAEIENLKRDLQQLVTK--------------HESELKEQHEQL 603
Cdd:COG3206 260 lQSPVIQQLRAQLAELEAELAELsarytpnhpdvialRAQIAALRAQLQQEAQRilasleaelealqaREASLQAQLAQL 339
|
170 180
....*....|....*....|....
gi 17539660 604 NVHHQSQQKLHSEAEKLRREHEAL 627
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEVA 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
233-433 |
6.51e-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: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 233 ESENRNLTEKGRELKLIIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESRAALRDEQRHLEHQEA- 311
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 312 --ENGKIVEQL------KTVSELNEKLTMqVKDLQDASENELASFRQKEKELIDELRMATNENVDLEELLKGVTNGKAGL 383
Cdd:COG3883 95 lyRSGGSVSYLdvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17539660 384 QfennclvGKLEELSFVSDRNKQDADNARAQLEEEREKHRLATEKLHQEN 433
Cdd:COG3883 174 E-------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| V_AnPalA_UmRIM20_like |
cd09236 |
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ... |
219-508 |
7.08e-03 |
|
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.
Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 39.65 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 219 KKKLVDmEHMVDELESENRNLTEKGRELKL--IIDSLKSDVTNKRDTAKSSQQREQE-----LSNILEEKEKESAQLLQQ 291
Cdd:cd09236 15 KDRLVN-ESIIDELEELTNRAHSTLRSLNLpgSLQALEKPLGLPPSLLRHAEEIRQEdglerIRASLDDVARLAASDRAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 292 LEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNEKLTMQVKDLQ---DASENELASFRQKEKELIDELRMATNENVD 368
Cdd:cd09236 94 LEEAMDILDDEASEDESLRRKFGTDRWTRPDSHEANPKLYTQAAEYEgylKQAGASDELVRRKLDEWEDLIQILTGDERD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 369 LEELLKGVTNGKAGLQFENNC--LVGKLEELSFVSD---------RNKQDADNARAQLEEE-----REKHRLATEKLHQE 432
Cdd:cd09236 174 LENFVPSSRRPSIPPELERHVraLRVSLEELDRLESrrrrkveraRTKARADDIRPEILREaarleREYPATEVAPAHFE 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539660 433 NI--DYMKTSDSRIEMILEESKTRkmmdESTIERLRldLDNEKSYKKNLEDLLNDLNQRALNS-EMANHLQKEGIQSVE 508
Cdd:cd09236 254 DLfdKRLAKYDKDLDAVSEEAQEQ----EEILQQIE--VANKAFLQSRKGDPATKERERALQSlDLAYFKYKEIVSNLD 326
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
217-426 |
7.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 217 TAKKKLVDMEHMVDELESENRNLTEKgrelkliIDSLKSDVTNKRDTAKSSQQREQELSNILEEKEKESAQLLQQLEESR 296
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 297 AALRDEQRHLEHQEAENGKI---------------VEQLKTVSELNEKLTMQVKDLQDASENELASFRQKEKELIDELRM 361
Cdd:COG3883 86 EELGERARALYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539660 362 ATNENVDLEELLKGVTNGKAGLQFENNCLVGKLEELSFVSDRNKQDADNARAQLEEEREKHRLAT 426
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
210-540 |
8.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 210 RSDRELKTAKKKLVDMEHMVDELESENRNLTEKGRELKLIIDSLKSDVtNKRDTAKS---------SQQREQELSNILEE 280
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKGkcpvcgrelTEEHRKELLEEYTA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 281 KEKESAQLLQQLEESRAALRDEQRHLEHQEAENGKIVEQLKTVSELNE-KLTMQVKDLQDASEN--ELASFRQKEKELID 357
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKaeEYEKLKEKLIKLKG 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 358 ELRMATNENVDLEEL---LKGVTNGKAGLQFENNCLVGKLEELSFVSdrnkqdadnaraqlEEEREKHRLATEKLHQENI 434
Cdd:PRK03918 540 EIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELEELGFES--------------VEELEERLKELEPFYNEYL 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539660 435 DyMKTSDSRIEMILEESKTrkmmDESTIERLRLDLDNEKSYKKNLEDLLNDLNQRALNSEMANhlQKEGIQSVETYLQMA 514
Cdd:PRK03918 606 E-LKDAEKELEREEKELKK----LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGL 678
|
330 340
....*....|....*....|....*.
gi 17539660 515 KKRIEHLELELSATNATIEFQSQQLD 540
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELE 704
|
|
|