|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
66-248 |
3.70e-65 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 218.24 E-value: 3.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 66 DLSRDDLLFLLSILEGELQARDEVIGILKAEKMDLALLEAQYGFVTPKKVLEALQRDAFQAKSTPWQEDIYE----KPMN 141
Cdd:pfam09727 1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKVKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYEamyeKPLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLIDQEIKSQEEKEQEK 221
Cdd:pfam09727 81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160
|
170 180
....*....|....*....|....*..
gi 1915686534 222 EKRVTTLKEELTKLKSFALMVVDEQQR 248
Cdd:pfam09727 161 KKLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
224-773 |
2.02e-19 |
|
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: 94.74 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFH 303
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 304 QDQDTIM---AKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKIskgEYGNAGIMAEVEELRKRVL 380
Cdd:TIGR02168 313 NLERQLEeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL---ESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 381 DMEGK----DEELIKMEEQCRDLNKRLERET---------LQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCN 447
Cdd:TIGR02168 390 QLELQiaslNNEIERLEARLERLEDRRERLQqeieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 448 LEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMF--------VDE--RKTMSEKL------ 511
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisVDEgyEAAIEAALggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 512 ---KKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKrALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNML 588
Cdd:TIGR02168 550 vvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE-IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 589 KNRLQSLE-AIEKDFLKNKLNQD--------------SGKSTTALHQENN-------------KIKELSQEVERLKLKLK 640
Cdd:TIGR02168 629 DDLDNALElAKKLRPGYRIVTLDgdlvrpggvitggsAKTNSSILERRREieeleekieeleeKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 641 DMKAIEDDLMKTEDEYET----LERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLS 716
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915686534 717 REVDALKEkihEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 773
Cdd:TIGR02168 789 AQIEQLKE---ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-731 |
1.26e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKR------KHKEYMEKSDEFICLLEQECERLKKLIDQ------ 209
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkeleELKEEIEELEKELESLEGSKRKLEEKIREleerie 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 210 EIKSQEEKEQEKEKRVTTLK---EELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKlalaEARVQEEEQ 286
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 287 KATRLEKELQtQTTKFHQDQDTIMAKLTNEdsqnRQLQQKLAALsrqidELEETNRSLRKAEEELQDIKEKISKgeygna 366
Cdd:PRK03918 346 KLKELEKRLE-ELEERHELYEEAKAKKEEL----ERLKKRLTGL-----TPEKLEKELEELEKAKEEIEEEISK------ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 367 gIMAEVEELRKRVLDMEGKDEELIKMEEQC----RDLNKRLERETLqsKDFKLEVEKLSKRimaLEKLEDAFNKSKQECY 442
Cdd:PRK03918 410 -ITARIGELKKEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELL--EEYTAELKRIEKE---LKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 443 SLKCNLEKERmttkqlsqELESLKVRIKELEAIESRLEKTeftlkeDLTKLKtltvmfvdERKTMSEKLKKTEDKLQAAS 522
Cdd:PRK03918 484 ELEKVLKKES--------ELIKLKELAEQLKELEEKLKKY------NLEELE--------KKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 523 SQLqveqnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLkaeEEKGndlLSRVNMLKNRLQSLEAIEKDF 602
Cdd:PRK03918 542 KSL-----------KKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELG---FESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 603 LKNK--------LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAI--EDDLMKTEDEYETLERRYANERDKAQF 672
Cdd:PRK03918 605 LELKdaekelerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELAGLRAELEE 684
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 673 LSKELEHVKMELAKYKlAEKTEtsheqwlFKRLQEEEAKSGHLSREVDALKEKIHEYMA 731
Cdd:PRK03918 685 LEKRREEIKKTLEKLK-EELEE-------REKAKKELEKLEKALERVEELREKVKKYKA 735
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
224-775 |
1.85e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEELTKLKSFALmvVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFH 303
Cdd:COG1196 214 RYRELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 304 QDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDME 383
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 384 GKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEK--------LSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTT 455
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeeallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 456 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSE-----KLKKTEDKLQAASSQLQVEQn 530
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvKAALLLAGLRGLAGAVAVLI- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 531 KVTTVTEKLIEETKRALkSKTDVEEKMYSVTKERDDLK------------NKLKAEEEKGNDLLSRVNMLKNRLQSLEAI 598
Cdd:COG1196 531 GVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKaakagratflplDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 599 EKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELE 678
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 679 HVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQG--------DHSVLQKKL 750
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppDLEELEREL 769
|
570 580
....*....|....*....|....*....
gi 1915686534 751 NQQENRNRDLG----REIENLTKELERYR 775
Cdd:COG1196 770 ERLEREIEALGpvnlLAIEEYEELEERYD 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
321-772 |
7.66e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQIDELEET-------NRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELR---KRVLDMEGKDEELI 390
Cdd:PRK03918 217 PELREELEKLEKEVKELEELkeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 391 KMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLE------KERMTTKQLSQELES 464
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 465 LKVRIK--ELEAIESRLEKTEFTLKEDLTKLKTLTVMF------VDERKTMSEKLKKTEDKLQAASSQLQVEQNKvtTVT 536
Cdd:PRK03918 377 LKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIgelkkeIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 537 EKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEE--KGNDLLSRVNMLKNRLQS--LEAIEKDF-----LKNKL 607
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKynLEELEKKAeeyekLKEKL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 608 NQDSGKSTTaLHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDE-----YETLERR------YANERDKAQFLSKE 676
Cdd:PRK03918 535 IKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERlkelepFYNEYLELKDAEKE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 677 LEHVKMELAkyKLAEKTETSheqwlFKRLQEEEAKSGHLSREVDALKEKI--HEYMATEDLICHLQGDHSVLQKKLNQQE 754
Cdd:PRK03918 614 LEREEKELK--KLEEELDKA-----FEELAETEKRLEELRKELEELEKKYseEEYEELREEYLELSRELAGLRAELEELE 686
|
490
....*....|....*...
gi 1915686534 755 NRNRDLGREIENLTKELE 772
Cdd:PRK03918 687 KRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-773 |
1.99e-15 |
|
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: 81.65 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 148 EKHKESYRRILGQLLVAEKSRRQTILELEEEKRKhkeyMEKSDEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKRVTT 227
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 228 LKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLalaEARVQEEEQKATRLEKELQTQTTKFhqdqD 307
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL---EREIEEERKRRDKLTEEYAELKEEL----E 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 308 TIMAKLTNEDSQNR-------QLQQKLAALSRQIDELEETNRSL----RKAEEELQDIKEKISKGEYGNAGIMAEVEELR 376
Cdd:TIGR02169 368 DLRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 377 KRVLDMEGKDEELIKMEEqcrDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTK 456
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS---KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 457 QLSQELesLKVRIKELEAIES----RLE----KTEFTLKEDLTKLKT----------LTVMFVDERktMSEKLKKT---- 514
Cdd:TIGR02169 525 GTVAQL--GSVGERYATAIEVaagnRLNnvvvEDDAVAKEAIELLKRrkagratflpLNKMRDERR--DLSILSEDgvig 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 515 --------EDKLQAASSQ-----LQVE----------QNKVTTVTEKLIEET----------KRALKSKTDVEEKMYSVT 561
Cdd:TIGR02169 601 favdlvefDPKYEPAFKYvfgdtLVVEdieaarrlmgKYRMVTLEGELFEKSgamtggsrapRGGILFSRSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 562 KERDDLKNKLKAEEEKGNDLLSRVNMLKNRL----QSLEAIEKDflKNKLNQDSGKSTTALHQENNKIKELSQEVERLKL 637
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELsdasRKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 638 KLKDMKA----IEDDLMKTEDEYETLERRYANERdkAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSG 713
Cdd:TIGR02169 759 ELKELEArieeLEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 714 HLSREVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 773
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
306-772 |
6.45e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 306 QDTIMAKLTNEDSQNRQLQQKLaalsrQIDELEETNRSLRKAEEELQDIKEKISKgeygnagIMAEVEELRKRVLDMEgk 385
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQIL-----GLDDYENAYKNLGEVIKEIKRRIERLEK-------FIKRTENIEELIKEKE-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 386 dEELIKMEEQCRDLNKRLEretlqskDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESL 465
Cdd:PRK03918 200 -KELEEVLREINEISSELP-------ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 466 KVRIKELEAIESRLEKTEftlkedltklktltvmfvdERKTMSEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKR 545
Cdd:PRK03918 272 KKEIEELEEKVKELKELK-------------------EKAEEYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 546 ALKSKTDVEEKMYSVTKERDDLKNKLkAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKI 625
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 626 KELSQEVERLKLKLKDMKAIEDDLMK------------TEDEYETLERRY-------ANERDKAQFLSKELEHVKMELAK 686
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 687 yKLAEKTETSHEQWLFKRLQEEEAKSGHLSREvdALKEKIHEYMATEDLICHLQGDHSVLQ---KKLNQQENRNRDLGRE 763
Cdd:PRK03918 488 -VLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKK 564
|
....*....
gi 1915686534 764 IENLTKELE 772
Cdd:PRK03918 565 LDELEEELA 573
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-691 |
7.26e-15 |
|
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: 80.10 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 276 LAEARVQEEEQKATRLEKELQTQTTKFHQDQDTI-----MAKLTNEDSQNRQ-LQQKLAALSRQIDELEETNRSLRKaee 349
Cdd:TIGR02168 622 LGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvITGGSAKTNSSILeRRREIEELEEKIEELEEKIAELEK--- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 350 ELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEgkdEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRimaLEK 429
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALR---KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER---LEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 430 LEDAFNKSKQEcyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSE 509
Cdd:TIGR02168 773 AEEELAEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 510 KLKKTEDKLQAASSqlqvEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLL------- 582
Cdd:TIGR02168 846 QIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRreleelr 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 583 SRVNMLKNRLQSLEAiEKDFLKNKLNQDsGKSTTALHQEN-----NKIKELSQEVERLKLKLKDMKAIEddlMKTEDEYE 657
Cdd:TIGR02168 922 EKLAQLELRLEGLEV-RIDNLQERLSEE-YSLTLEEAEALenkieDDEEEARRRLKRLENKIKELGPVN---LAAIEEYE 996
|
410 420 430
....*....|....*....|....*....|....
gi 1915686534 658 TLERRYanerdkaQFLSKELEHVkmELAKYKLAE 691
Cdd:TIGR02168 997 ELKERY-------DFLTAQKEDL--TEAKETLEE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-598 |
7.45e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESyRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLK---KLIDQEIKSQEEKE 218
Cdd:PRK02224 238 EADEVLEEHEER-REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 219 QEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQ 298
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 299 TTKFhqdqDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYG----NAGIMAEVEE 374
Cdd:PRK02224 397 RERF----GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpveGSPHVETIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 375 LRKRVLDMEgkdEELIKMEEQCRDLNKRLER-----------ETLQSK---------DFKLEVEKLSKRIMAL----EKL 430
Cdd:PRK02224 473 DRERVEELE---AELEDLEEEVEEVEERLERaedlveaedriERLEERredleeliaERRETIEEKRERAEELreraAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 431 EDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEfTLKEDLTKLKtltvmfvDERKTMSEK 510
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLR-------EKREALAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 511 LKKTEDKLQAAS---SQL--QVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK---LKAEEEKGNDLL 582
Cdd:PRK02224 622 NDERRERLAEKRerkRELeaEFDEARI----EEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELR 697
|
490
....*....|....*.
gi 1915686534 583 SRVNMLKNRLQSLEAI 598
Cdd:PRK02224 698 ERREALENRVEALEAL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
113-775 |
3.46e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 113 KKVLEALQRDAFQAKStpwQEDIYEKPMNELDKVVEKHKESYRRILGQLLVAeksrRQTILELEEEKRKHKEYMEKSDEF 192
Cdd:TIGR02168 245 QEELKEAEEELEELTA---ELQELEEKLEELRLEVSELEEEIEELQKELYAL----ANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 193 ICLLEQECERL--KKLIDQEI-KSQEEKEQEKEKRVTTLKEELTKLKsfalmvvDEQQRLTAQLTLQRQKIQELTTNAKE 269
Cdd:TIGR02168 318 LEELEAQLEELesKLDELAEElAELEEKLEELKEELESLEAELEELE-------AELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 270 THTKLALAEARVQEEEQKATRLEKELQtqttKFHQDQDTIMAKLtnEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEE 349
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRE----RLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 350 ELQDIKEKISkgeygnagimAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEK 429
Cdd:TIGR02168 465 ELREELEEAE----------QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 430 LEDA----------------FNKSKQECYSLKCNLEKERM--------------TTKQLSQELESLKVRIKELEAIESRL 479
Cdd:TIGR02168 535 YEAAieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 480 EK-----------------------------TEFTLKEDL-------TKLKTLTVMFVDERKTMSEKLKKTEDKLQAASS 523
Cdd:TIGR02168 615 RKalsyllggvlvvddldnalelakklrpgyRIVTLDGDLvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 524 QLQVEQNKVTTVTEKLIEETKRALKSKTDVEekmysvtKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEkdfl 603
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI---- 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 604 kNKLNQDSGKSTTALHQENNKIKELSQEVERLKlklKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKME 683
Cdd:TIGR02168 764 -EELEERLEEAEEELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 684 LakyklaektETSHEQWlfKRLQEEEAKSGHLSREVDALKEKIH--------EYMATEDLICHLQGDHSVLQKKLNQQEN 755
Cdd:TIGR02168 840 L---------EDLEEQI--EELSEDIESLAAEIEELEELIEELEseleallnERASLEEALALLRSELEELSEELRELES 908
|
730 740
....*....|....*....|
gi 1915686534 756 RNRDLGREIENLTKELERYR 775
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLE 928
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-799 |
4.41e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 164 AEKSRRQTILELEEEkRKHKEYMEKSDEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKRVT-TLKEELTKLKSFALMV 242
Cdd:PTZ00121 1100 AEEAKKTETGKAEEA-RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEdARKAEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 243 VDEQQRLTAQLTLQRQKIQEL--TTNAKETHTKLALAEARVQEEEQKATRLEKelqTQTTKFHQDQDTIMAKLTNEDSQN 320
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDArkAEAARKAEEERKAEEARKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQIDELEETNRslRKAEEeLQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEE---QCR 397
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEA--RKADE-LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkKAD 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 398 DLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEK---ERMTTKQLSQELESLKVRIKELEA 474
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEEDKKKADELKK 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 475 IESRLEKTEFTLK--EDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTD 552
Cdd:PTZ00121 1413 AAAAKKKADEAKKkaEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 553 VEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH--QENNKIKELSQ 630
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 631 EVERLKLKLK---DMKAIE----DDLMKTEDEYETLE----RRYANERDKAQFLSKElEHVKMELAKYKLAEKTETSHEQ 699
Cdd:PTZ00121 1572 AEEDKNMALRkaeEAKKAEeariEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE 1650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 700 WLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDlichlqgdhsvLQKKLNQQENRNRDLGREIENLTKELERYRHFSK 779
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
650 660
....*....|....*....|
gi 1915686534 780 SLRPSLNGRRISDPQVFSKE 799
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEA 1739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
172-525 |
8.60e-14 |
|
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: 76.26 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 172 ILELEEEKRKHKEYMEKsdeficlLEQECERLKKLIDQEIKSQE--EKEQEKEKRVTTLKEELTKLKSFALM-----VVD 244
Cdd:TIGR02169 165 VAEFDRKKEKALEELEE-------VEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEGYELLkekeaLER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 245 EQQRLTAQLTLQRQKIQELTtnakethtklalaeARVQEEEQKATRLEKELQTQTTKfhqdqdtIMAKLTNEdsqNRQLQ 324
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLT--------------EEISELEKRLEEIEQLLEELNKK-------IKDLGEEE---QLRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 325 QKLAALSRQI----DELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEgkdEELIKMEEQCRDLN 400
Cdd:TIGR02169 294 EKIGELEAEIasleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 401 KRLEREtlqSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELeaiESRLE 480
Cdd:TIGR02169 371 AELEEV---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL---EEEKE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1915686534 481 KTEFTLKEDLTKLKTLTVMFVDERKTM---SEKLKKTEDKLQAASSQL 525
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-687 |
1.20e-13 |
|
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: 75.87 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 283 EEEQKATRLEKELQtqttKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDEL----EETNRSLRKAEEELQDIKEKI 358
Cdd:TIGR02169 671 SEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeiEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 359 SKGEYGNAGIMAEVEELRKRVLDMEgkdEELIKMEEQCRDLNKRLERETLQSKDFKL-EVEKLSKRIMA-LEKLEDAFNK 436
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEArLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 437 SKQEcyslKCNLEKERMTTKQLSQELESLKVRI-KELEAIESRLEKTEFTLKEDLTKLKTLtvmfvDERKtmsEKLKKTE 515
Cdd:TIGR02169 824 LTLE----KEYLEKEIQELQEQRIDLKEQIKSIeKEIENLNGKKEELEEELEELEAALRDL-----ESRL---GDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 516 DKLQAASSQLQVEQNKvttvteklieetkralksktdveekmysvtkerddlknkLKAEEEKGNDLLSRvnmLKNRLQSL 595
Cdd:TIGR02169 892 DELEAQLRELERKIEE---------------------------------------LEAQIEKKRKRLSE---LKAKLEAL 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 596 EAIEKDFLKNKlnqDSGKSTTALHQENNKIKELSQEVERlklklkDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSK 675
Cdd:TIGR02169 930 EEELSEIEDPK---GEDEEIPEEELSLEDVQAELQRVEE------EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
410
....*....|..
gi 1915686534 676 ELEHVKMELAKY 687
Cdd:TIGR02169 1001 ERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-688 |
1.45e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 113 KKVLEAlqRDAFQAKSTPWQEDIYEKPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEf 192
Cdd:PTZ00121 1237 KDAEEA--KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE- 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 193 icllEQECERLKKLIDQEIKSQEEKEQekekrvttlKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTtnaKETHT 272
Cdd:PTZ00121 1314 ----AKKADEAKKKAEEAKKKADAAKK---------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK---KEEAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQ-------QKLAALSRQIDELEETNRSLR 345
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkadeaKKKAEEAKKADEAKKKAEEAK 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 346 KAEEELQDIKEKISKGEYGNAGIMA-EVEELRKRVLDMEGKDEELIKMEEQCR--DLNKRLERETLQSKDFKLEVEKLSK 422
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAkKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADEAKKAEEAKKAD 1537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 423 RIMALEKLEDAFNKSKQEcySLKCNLEKERMTTKQLSQELESLKVR-IKELEAIESRLEKTEFTLKEDLTKLKTLTVMFV 501
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAE--ELKKAEEKKKAEEAKKAEEDKNMALRkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 502 DERKTMSEKLKKTEDklqaassqlqvEQNKVTTVTEKLIEETKRALKSKTDVEE-KMYSVTKERDDLKNKLKAEEEKGND 580
Cdd:PTZ00121 1616 EEAKIKAEELKKAEE-----------EKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 581 LLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH-QENNKIKelsqeVERLKLKLKDMKAIEDDLMKTEDEYETL 659
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaEEENKIK-----AEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
570 580
....*....|....*....|....*....
gi 1915686534 660 ERRYANERDKAQFLSKELEHVKMELAKYK 688
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-520 |
2.09e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 164 AEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKL---IDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFAL 240
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 241 MVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFhqdqDTIMAKLTNEDSQN 320
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQID----ELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRV-----------LDMEGK 385
Cdd:TIGR02168 820 ANLRERLESLERRIAaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasleealallrSELEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 386 DEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMAL-EKLEDAFNKSKQECYSLKCNLEKERMttkQLSQELES 464
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKR 976
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 465 LKVRIKEL--------EAIESRLEKTEF--TLKEDLTKLKTlTVMFVDER--KTMSEKLKKTEDKLQA 520
Cdd:TIGR02168 977 LENKIKELgpvnlaaiEEYEELKERYDFltAQKEDLTEAKE-TLEEAIEEidREARERFKDTFDQVNE 1043
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
142-728 |
3.90e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYM-----EKSDEFICLLEQECERLKKLIDQEIKSQEE 216
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAkkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 217 KEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAqltlQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQ 296
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 297 TQTTKFHQDQDTIMA--KLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYG--NAGIMAEV 372
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkKAEEKKKA 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 373 EELRKRVLDMEGKDEELIKMEEqcrdlnKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAfnKSKQECYSLKCNLEKER 452
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEE------AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKA 1505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 453 MTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKV 532
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 533 TtvteKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSG 612
Cdd:PTZ00121 1586 A----KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 613 KSTtalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDE---YETLERRYANERDKAQFLSKELE--HVKMELAKY 687
Cdd:PTZ00121 1662 KAA----EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEenKIKAEEAKK 1737
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1915686534 688 KLAEKTETSHEqwlFKRLQEEEAKSGHLSREVDALKEKIHE 728
Cdd:PTZ00121 1738 EAEEDKKKAEE---AKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-810 |
1.04e-12 |
|
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: 72.84 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 120 QRDAFQAKSTPWQEDIYEKPMNELDKVVEKHKesyRRILGQLLVAEKSRRQ-----TILELEEEKRKHKE--YMEKSDEF 192
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEQLISEHE---VEITGLTEKASSARSQansiqSQLEIIQEQARNQNsmYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 193 ---ICLLEQECERLKKLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTA-------QLTLQRQKIQE 262
Cdd:pfam15921 323 estVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrekELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 263 LTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNED-------SQNRQLQQKLAALSRQID 335
Cdd:pfam15921 403 LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNeslekvsSLTAQLESTKEMLRKVVE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 336 ELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVlDMEGKDEELIKME-EQCRDLNKRLERETLQSKDFK 414
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-DLKLQELQHLKNEgDHLRNVQTECEALKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 415 LEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLK----VRIKELEAIESRLEKTEFTL---- 486
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKdkkdAKIRELEARVSDLELEKVKLvnag 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 487 KEDLTKLKTLTvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLiEETKRALKSktdveeKMYSVTKERDD 566
Cdd:pfam15921 642 SERLRAVKDIK----QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKM------QLKSAQSELEQ 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 567 LKNKLKAEEEKGNDLLS--------------RVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIK 626
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKvamgmqkqitakrgQIDALQSKIQFLEEAmtnankEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 627 EL----SQEvERLKLKLKDMKAIEDDLMKTEDEYETLERRYANE--RDKAQFL--SKELE---HVKMELAKYKLAEKTET 695
Cdd:pfam15921 791 ELevlrSQE-RRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTldVKELQgpgYTSNSSMKPRLLQPASF 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 696 SHEQWLFKRLQEEEAKSGHLSREVDALKEKiheymATEDLICHLQGDHSVLQKKLNQQENRNRDLGRE---------IEN 766
Cdd:pfam15921 870 TRTHSNVPSSQSTASFLSHHSRKTNALKED-----PTRDLKQLLQELRSVINEEPTVQLSKAEDKGRApslgalddrVRD 944
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1915686534 767 LTKELERYRHFSKSLRPSLNGRRISDPQVFSKE-VQTEAVDNEPP 810
Cdd:pfam15921 945 CIIESSLRSDICHSSSNSLQTEGSKSSETCSREpVLLHAGELEDP 989
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-577 |
1.30e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 233 TKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQ---DQDTI 309
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleeDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 310 MAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSL--RKAEEELQDIKEKISKgeygnagIMAEVEELRKRVLDMEGKDE 387
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSK-------LEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 388 ELIKMEEQCRDlnkrlERETLQSkdfklEVEKLSKRIMALEKLEDAFNKSKQEcysLKCNLEKERMTTKQLSQELESLKV 467
Cdd:TIGR02169 823 RLTLEKEYLEK-----EIQELQE-----QRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 468 RIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTED----------------KLQAASSQLQVEQNK 531
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelsleDVQAELQRVEEEIRA 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1915686534 532 VTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEK 577
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-667 |
3.89e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 158 LGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLiDQEIKSQEEKEQEKEKRVTTLKEELTKLKS 237
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL-EAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 238 FALMVVDEQQRLTAQLTLQR-------QKIQELTTNAKETHTKLALAEARVQEEEQKATRLE---KELQTQTTKFHQDQD 307
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQAHNEEAESLRedaDDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 308 TIMAKLTNEDSQNRQLQQKLAALSRQIDELEE----TNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRV---- 379
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRErfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeae 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 380 -LDMEGK---------DEELIKMEEQCRDLNKRLERETLqskDFKLEVEKLSKRIMALEKLedafnkskqecyslkcnle 449
Cdd:PRK02224 447 aLLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELE---DLEEEVEEVEERLERAEDL------------------- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 450 kermttKQLSQELESLKVRikeLEAIESRLEKTEFTLKEDLTKLKTLtvmfvDERKT-MSEKLKKTEDKLQAASSQLQVE 528
Cdd:PRK02224 505 ------VEAEDRIERLEER---REDLEELIAERRETIEEKRERAEEL-----RERAAeLEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 529 QNKVTTVTEKLiEETKRALKSKTDVEEKMYSVTKERDD---LKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKN 605
Cdd:PRK02224 571 REEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEierLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 606 KLNQDSGKSTTALHQENNKIKELS-----------------QEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANER 667
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELReerddlqaeigavenelEELEELRERREALENRVEALEALYDEAEELESMYGDLR 728
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-678 |
8.83e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 141 NELDKVVEKHKESYRRILGQLLVAEKSRR----------QTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLIDQE 210
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIArleerrreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 211 IKSQEEKEQEKEKRVTTLKEELTKLKSFAlmvvDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATR 290
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELA----EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 291 LEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMA 370
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 371 EVEELRKR----VLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKR------IMALEKLEDAFNKSKQE 440
Cdd:COG1196 513 ALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratFLPLDKIRARAALAAAL 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 441 cysLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQA 520
Cdd:COG1196 593 ---ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 521 ASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKmysvTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEK 600
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEE----ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 601 DFLKNKLNQDsgksttalHQENNKIKELSQEVERLKLKLKDMKAIEddlMKTEDEYETLERRYanerdkaQFLSKELE 678
Cdd:COG1196 746 ELLEEEALEE--------LPEPPDLEELERELERLEREIEALGPVN---LLAIEEYEELEERY-------DFLSEQRE 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-708 |
9.04e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 334 IDEL---EETNRSLRKAEEELQDIKEKISKgeygnagIMAEVEELRKRVLDMEGKDEELIKMeeqcRDLNKRLEretlqs 410
Cdd:TIGR02169 159 IDEIagvAEFDRKKEKALEELEEVEENIER-------LDLIIDEKRQQLERLRREREKAERY----QALLKEKR------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 411 kdfKLEVEKLSKRIMALEKledafnkskqecyslkcnlEKERmTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDL 490
Cdd:TIGR02169 222 ---EYEGYELLKEKEALER-------------------QKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 491 TKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK 570
Cdd:TIGR02169 279 KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 571 LKAEEEKGNDLLSRVNMLKNRLQSL------EAIEKDFLKNKLN----------QDSGKSTTALHQENNKIKELSQEV-- 632
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETrdelkdYREKLEKLKREINelkreldrlqEELQRLSEELADLNAAIAGIEAKIne 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 633 --ERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEE 708
Cdd:TIGR02169 439 leEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEV 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-672 |
1.42e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 113 KKVLEALQRDAFQAKStpwQEDIYEKPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEf 192
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKK---KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE- 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 193 icllEQECERLKKLIDQEIKsqeekeqekekrvttlKEELTKLKSFALMVVDEQQRLTAqltlQRQKIQELTTNAKEthT 272
Cdd:PTZ00121 1390 ----KKKADEAKKKAEEDKK----------------KADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEE--A 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEE--- 349
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakk 1523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 350 --ELQDIKEKISKGEYGNAGIMAEVEELRKRvldmegkdEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLS--KRIM 425
Cdd:PTZ00121 1524 adEAKKAEEAKKADEAKKAEEKKKADELKKA--------EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 426 ALEKLEDAFNKSKQEcySLKcNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLK-EDLTKLKTLTVMF-VDE 503
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAE--EAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaEEENKIKAAEEAKkAEE 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 504 RKTMSEKLKKTEDKLQAASSQLQV---EQNKVTTVTEKLIEETKRALKSKTDVEE---KMYSVTKERDDLKNK---LKAE 574
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKKKAEELKKAEEEnkiKAEEAKKEAEEDKKKaeeAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 575 EEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEV----ERLKLKLKDMKAIEDDLM 650
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIieggKEGNLVINDSKEMEDSAI 1832
|
570 580
....*....|....*....|..
gi 1915686534 651 KTEDEYETLERRYANERDKAQF 672
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKF 1854
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-678 |
1.45e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQIDELEETNRSLRKAE------EELQDIKEKISKGEYGNAGimAEVEELRKRvldMEGKDEELIKMEE 394
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLV--LRLEELREE---LEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 395 QCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKledafnkskqECYSLKCNLEKERMTTKQLSQELESLKVRIKELEA 474
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQK----------ELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 475 IESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEetkralksktdVE 554
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ-----------LE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 555 EKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVER 634
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1915686534 635 LKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELE 678
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-688 |
2.78e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 283 EEEQKATRLEKELQTQTTKFHQDQDTImakltnedsqnRQLQQKLAALSRQIDELEETNRSLRKAEE------ELQDIKE 356
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-----------EELEEELEELEAELEELREELEKLEKLLQllplyqELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 357 KISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQS-KDFKLEVEKLSKRImalEKLEDAFN 435
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRL---AELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 436 KSKQECYSLKCNLE--KERMTTKQLSQELESLKVRIK------ELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTM 507
Cdd:COG4717 217 EAQEELEELEEELEqlENELEAAALEERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 508 SEKLKKTEDKLQAASSQLQVEQNKVTTVTEKL-----------------IEETKRALKSKTDVEEKMY--SVTKERDDLK 568
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALglppdlspeellelldrIEELQELLREAEELEEELQleELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 569 NKLKAEEE-----------KGNDLLSRVNMLKNRLQSL----EAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVE 633
Cdd:COG4717 377 AEAGVEDEeelraaleqaeEYQELKEELEELEEQLEELlgelEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 634 RLKLKLKDMKAiEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYK 688
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
278-694 |
6.23e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 278 EARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEK 357
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 358 ISKGEYGNAGIMAEVEELRKRVLDMEGKD---------------------EELIKMEEQCRDlnkRLERETLQSKDFKLE 416
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERddllaeaglddadaeavearrEELEDRDEELRD---RLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 417 VEKLSKRIMALE----KLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIK----ELEAIESRLEKTEFTLKE 488
Cdd:PRK02224 344 AESLREDADDLEeraeELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 489 DLTKLKTLTVmfvdERKTMSEKLKKTEDKLQAAS--------------SQLQVEQNKVTTVTEKL--IEETKRALKSKTD 552
Cdd:PRK02224 424 LREREAELEA----TLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELedLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 553 VEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLnQDSGKSTTALHQENNK----IKEL 628
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-RAAELEAEA-EEKREAAAEAEEEAEEareeVAEL 577
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915686534 629 SQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyaNERDKAQflsKELEhvkmELAKYKLAEKTE 694
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIADAEDEIERL--REKREAL---AELN----DERRERLAEKRE 634
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-709 |
1.45e-10 |
|
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: 65.84 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 156 RILGQLLVAEKSRRQTILELEEEKRKHKEYMEKS-DEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKRVTTLKEELTK 234
Cdd:TIGR00606 358 RHQEHIRARDSLIQSLATRLELDGFERGPFSERQiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 235 LKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKlalaEARVQEEEQKATRLEKELQTQTTKfhQDQDTIMAKLT 314
Cdd:TIGR00606 438 LGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL----DQELRKAERELSKAEKNSLTETLK--KEVKSLQNEKA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 315 NEDSQNRQLQQKLAALSRQIDELEETNRSLRK---AEEELQDIKEKISKGEYGNAGIMAEVEELRKRvldMEGKDEELIK 391
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkmdKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW---LHSKSKEINQ 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 392 MEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALE-KLEDAFNKSKQECY--SLKCNLEKERMTTKQLSQELESLKVR 468
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQDEESDleRLKEEIEKSSKQRAMLAGATAVYSQF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 469 IKELEAIES-------RLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIE 541
Cdd:TIGR00606 669 ITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 542 ETKRALKSKTDVEEKMYSVTKERDDLKNkLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQE 621
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 622 NNKIKE-------LSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMEL----AKYKLA 690
Cdd:TIGR00606 828 NQEKQEkqheldtVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDA 907
|
570
....*....|....*....
gi 1915686534 691 EKTETSHEQWLFKRLQEEE 709
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKE 926
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
224-777 |
1.50e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.02 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEeeqKATRLEKELQTQTTKFH 303
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE---KRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 304 QDQdtimAKLTNEDSQNRQLQQ----KLAALSRQID----ELEETNRSLRKAEEELQDIKEKIskgeygNAGIMAEVEEL 375
Cdd:pfam12128 319 KDR----SELEALEDQHGAFLDadieTAAADQEQLPswqsELENLEERLKALTGKHQDVTAKY------NRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 376 rkrVLDMEGKDEELIKMEEQcRDLNKRLERETLQSKDFKLEveklskrimalEKLEDAFNKSKQECYSLKCNLEKERMTT 455
Cdd:pfam12128 389 ---NRDIAGIKDKLAKIREA-RDRQLAVAEDDLQALESELR-----------EQLEAGKLEFNEEEYRLKSRLGELKLRL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 456 KQL---SQELESLKVRIKELEAIESRLEKTeFTLKEDLTklktltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKV 532
Cdd:pfam12128 454 NQAtatPELLLQLENFDERIERAREEQEAA-NAEVERLQ----------SELRQARKRRDQASEALRQASRRLEERQSAL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 533 TTVTEKLIEETKRAL----KSKTDVEEKMYSVTKE----RDDLKNKLKAEEEKGNDLLSRVNMlknRLQSLEAIEKDFLK 604
Cdd:pfam12128 523 DELELQLFPQAGTLLhflrKEAPDWEQSIGKVISPellhRTDLDPEVWDGSVGGELNLYGVKL---DLKRIDVPEWAASE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 605 NKLNQDSGKSTTALHQENNKIKELSQ-------EVERLKLKLKDMKAI----EDDLMKTEDEYETLERR----YANERDK 669
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEqlvqangELEKASREETFARTAlknaRLDLRRLFDEKQSEKDKknkaLAERKDS 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 670 AQFLSKELEHVKMELA---KYKLAEKTETSHE---QWLFKRLQEEEAKSGHLSReVDALKEKIHEYMATEDLICHLQGDH 743
Cdd:pfam12128 680 ANERLNSLEAQLKQLDkkhQAWLEEQKEQKREartEKQAYWQVVEGALDAQLAL-LKAAIAARRSGAKAELKALETWYKR 758
|
570 580 590
....*....|....*....|....*....|....
gi 1915686534 744 SVlqKKLNQQENRNRDLGREIENLTKELERYRHF 777
Cdd:pfam12128 759 DL--ASLGVDPDVIAKLKREIRTLERKIERIAVR 790
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
169-772 |
2.43e-10 |
|
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: 64.99 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 169 RQTILELEEEKRKHKEYMEKSDEFICLLEqECERLKKLIDQEIKSQEEKEQEKEKRVTTLKeeltklksfalMVVDEQQR 248
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEE-LKLQELKLKEQAKKALEYYQLKEKLELEEEY-----------LLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 249 LTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKfhqDQDTIMAKLTNEDSQNRQLQQKLA 328
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 329 ALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMA----EVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLE 404
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREaeeeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 405 RETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEF 484
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 485 TLKEDLTKLKTLTVMFV--------DERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEK 556
Cdd:pfam02463 471 EDLLKETQLVKLQEQLElllsrqklEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 557 MYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEA------------IEKDFLKNKLNQDSGKSTTALHQENNK 624
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLksiavleidpilNLAQLDKATLEADEDDKRAKVVEGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 625 IKELSQEVERLKLKL----KDMKAIEDDLMKTEDEYETLE--RRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHE 698
Cdd:pfam02463 631 DTELTKLKESAKAKEsglrKGVSLEEGLAEKSEVKASLSEltKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 699 QWLFKRLQEEEAKSGHLSREVD-------ALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 771
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDkineelkLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
.
gi 1915686534 772 E 772
Cdd:pfam02463 791 E 791
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
325-736 |
3.57e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 325 QKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEygnagimAEVEELRKRVLDMEgKDEELIKMEEQCRDLNKRLE 404
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLE-KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 405 RETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNL-EKERMTTKQLSQELESLKVRIKELEAIESRLEKTE 483
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 484 FTLKEDLTKLKTLTvmfvdERKTMSEKLKKTEDKLQAASSQLQVE------------------------------QNKVT 533
Cdd:COG4717 223 EELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLALLglggsllsliltiagvlflvlgllallfllLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 534 TVTEKLIEETkRALKSKTDVEEKMYSVTKERDDLKNKLKAEE--------EKGNDLLSRVNMLKNRLQ-SLEAIEKDFLK 604
Cdd:COG4717 298 ASLGKEAEEL-QALPALEELEEEELEELLAALGLPPDLSPEEllelldriEELQELLREAEELEEELQlEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 605 NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEyETLERRYANERDKAQFLSKELEHVKMEL 684
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1915686534 685 AKYKLA-EKTETSHEqwLFKRLQEEEaksgHLSREVDALKEKIHEYMATEDLI 736
Cdd:COG4717 456 AELEAElEQLEEDGE--LAELLQELE----ELKAELRELAEEWAALKLALELL 502
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-781 |
3.59e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 208 DQEIKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLtlqrQKIQELTTNAKETHTKLALA---------- 277
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQL----QAETELCAEAEEMRARLAARkqeleeilhe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 278 -EARVQEEEQKATrlekELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKE 356
Cdd:pfam01576 80 lESRLEEEEERSQ----QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 357 KISKGEYGNAGIMAEVEELRKRVLDMEGKDEELI-------KMEEQCR----DLNKRLERETL----QSKDFKLEVEKLS 421
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMIsdleerlKKEEKGRqeleKAKRKLEGESTdlqeQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 422 KRIMALEK-LEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLkvrikELE-AIESRLEKTEFTLKEDLTKLKTLTVM 499
Cdd:pfam01576 236 AQLAKKEEeLQAALARLEEETAQKNNALKKIRELEAQISELQEDL-----ESErAARNKAEKQRRDLGEELEALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 500 FVD----------ERKTMSEKLKKT-EDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLK 568
Cdd:pfam01576 311 TLDttaaqqelrsKREQEVTELKKAlEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 569 NKLKAEEEKGNDLLSRVNMLKNRLQSLEA--IEKDFLKNKLNQDSGKS-------TTALHQENNKIKELSQEVERLKLKL 639
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEGQLQELQArlSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 640 KDMK-----------AIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA--KYKLAEKTETSHeqwlfkrlQ 706
Cdd:pfam01576 471 QDTQellqeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmKKKLEEDAGTLE--------A 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 707 EEEAKSgHLSREVDALKEKIHEYMATEDlichlqgdhsvlqkKLNQQENRnrdLGREIENLTKELERYRHFSKSL 781
Cdd:pfam01576 543 LEEGKK-RLQRELEALTQQLEEKAAAYD--------------KLEKTKNR---LQQELDDLLVDLDHQRQLVSNL 599
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-609 |
2.10e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 136 YEKPMNELDKVVEKHKESYRRILGQLLVAEksrrQTILELEEEKRKHKEYMEKSDEficlLEQECERLKKLID---QEIK 212
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLE----LLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEkkqQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 213 SQEEKEQEKEKRVTTLKEELTKLKsfalmvvDEQQRLTAQLTLQRQKIQELTTNAKETHTKLAlaearvQEEEQKATRLE 292
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIK-------KQLSEKQKELEQNNKKIKELEKQLNQLKSEIS------DLNNQKEQDWN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 293 KELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKgeyGNAGIMAEV 372
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK---ENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 373 EELRKRVLDMEGK-----------DEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQ-- 439
Cdd:TIGR04523 387 KNLESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsl 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 440 ---------ECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEK 510
Cdd:TIGR04523 467 etqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 511 LKKTEDKLQaaSSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKN 590
Cdd:TIGR04523 547 LNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
490 500
....*....|....*....|.
gi 1915686534 591 RLQSLEAIEK--DFLKNKLNQ 609
Cdd:TIGR04523 625 ENEKLSSIIKniKSKKNKLKQ 645
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-774 |
2.31e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 70 DDLLFLLSILEGELQARDEVIGILKAEKMDLALLEAqygfVTPKKVLEALQRDAFQAKStpwQEDIYEKPMNELDKVVEK 149
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ----LRVKEKIGELEAEIASLER---SIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 150 HKESYRRILGQLlvaEKSRRQtILELEEEKRKHKEYMEKSDEFICLLEQECERLkkliDQEIKSQEEKEQEKEKRVTTLK 229
Cdd:TIGR02169 327 LEAEIDKLLAEI---EELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 230 EELTKLKSFALMVVDEQQRLTAQLtlqrqkiqelttnaKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQdqdtI 309
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEEL--------------ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ----L 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 310 MAKLTNEDSQNRQLQQKLAALSRQideleetnrsLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEEL 389
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKE----------LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 390 IKMEEQ--------------------------CRDLNKR--LERETL----QSKDFKLEVEKLSKR---------IMALE 428
Cdd:TIGR02169 531 GSVGERyataievaagnrlnnvvveddavakeAIELLKRrkAGRATFlplnKMRDERRDLSILSEDgvigfavdlVEFDP 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 429 KLEDAFNKSKQECY------SLKCNLEKERMTT--------------------------KQLSQELESLKVRIKELEAIE 476
Cdd:TIGR02169 611 KYEPAFKYVFGDTLvvedieAARRLMGKYRMVTlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKREL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 477 SRlekteftLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALkskTDVEEK 556
Cdd:TIGR02169 691 SS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED-LSSLEQEI---ENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 557 MYSVTKERDDLKNKLKAEEEKGNDLLSRVNM--LKNRLQSLEAIEKDFLK-----NKLNQDSGKSTTALHQENNKIKELS 629
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRiearlREIEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 630 QEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANE----RDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRL 705
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 706 QEEEAKSGHLSREVDALKEKIHE--YMATEDLichlqgDHSVLQKKLNQQENRNRDLG----REIENLTKELERY 774
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEdeEIPEEEL------SLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRL 988
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
414-678 |
5.65e-09 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 60.33 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 414 KLEVEKLSKRIMALEKLEDAFNKSKQecYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKteftLKEDLTKL 493
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRS--YLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKE----LEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 494 KtltvmfvDERKTMSEKLKKTEdKLQAASSQLQVEQN-KVTTVTEKLIEETKralksktdveekmYSVTKERDDLKNKLK 572
Cdd:PRK05771 113 E-------NEIKELEQEIERLE-PWGNFDLDLSLLLGfKYVSVFVGTVPEDK-------------LEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 573 AEEEKGNDLLSRVNmLKNRLQSLEAI--EKDFLKNKLNqDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLM 650
Cdd:PRK05771 172 ISTDKGYVYVVVVV-LKELSDEVEEElkKLGFERLELE-EEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEEL 249
|
250 260
....*....|....*....|....*...
gi 1915686534 651 KTEDEYetlerrYANERDKAQFLSKELE 678
Cdd:PRK05771 250 LALYEY------LEIELERAEALSKFLK 271
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
246-771 |
8.38e-09 |
|
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: 60.12 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 246 QQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQ 325
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 326 KLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVldmegkdEELIKMEEQcrdlnkRLER 405
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL-------EELLRTEQQ------RLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 406 ETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFT 485
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 486 LKEDLTKLKTLTVMFVDERKTM-----SEKLKKTEdkLQAASSQLQVEQNKVTTVTEKLIEETK--------------RA 546
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLkteleKEKLKNIE--LTAHCDKLLLENKELTQEASDMTLELKkhqediinckkqeeRM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 547 LKSKTDVEEK-------MYSVTKE----RDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDsgKST 615
Cdd:pfam05483 533 LKQIENLEEKemnlrdeLESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN--KNI 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 616 TALHQENNKIKELSQEverlklKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQflsKELEHVKmeLAKYKLAEKTET 695
Cdd:pfam05483 611 EELHQENKALKKKGSA------ENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ---KEIEDKK--ISEEKLLEEVEK 679
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 696 SH--EQWLFKRLQEEEAKSGHLSREVDALKEK-IHEYmatEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 771
Cdd:pfam05483 680 AKaiADEAVKLQKEIDKRCQHKIAEMVALMEKhKHQY---DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
227-577 |
8.66e-09 |
|
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: 59.99 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 227 TLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLE---KELQTQTTKFH 303
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQeaqDKINEELKLLK 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 304 QDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDEL-EETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDM 382
Cdd:pfam02463 743 QKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 383 EGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQEL 462
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 463 ESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEE 542
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
|
330 340 350
....*....|....*....|....*....|....*
gi 1915686534 543 TKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEK 577
Cdd:pfam02463 983 FEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
164-775 |
1.29e-08 |
|
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: 59.60 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 164 AEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLIDQEIKsQEEKEQEKEKRVTTLKEELTKLKSFALMVV 243
Cdd:pfam02463 210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ-EIEKEEEKLAQVLKENKEEEKEKKLQEEEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 244 DEQQRLTAQLTLQRQKIQELTT----NAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQ 319
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVddeeKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 320 NRQLQQKLAALSRQIDELEETNRsLRKAEEELQDIKEKISKGEygnagimAEVEELRKRVLDMEGKDEELIKMEEQCRDL 399
Cdd:pfam02463 369 EQLEEELLAKKKLESERLSSAAK-LKEEELELKSEEEKEAQLL-------LELARQLEDLLKEEKKEELEILEEEEESIE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 400 NKRLERETLQSKDFKLEVEKLSKRIMaLEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRL 479
Cdd:pfam02463 441 LKQGKLTEEKEELEKQELKLLKDELE-LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 480 EKTEFTLKEDLTKLKTLTVMFVD---ERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEk 556
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVAVENYKvaiSTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE- 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 557 mysvTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTA--LHQENNKIKELSQEVER 634
Cdd:pfam02463 599 ----IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEegLAEKSEVKASLSELTKE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 635 LKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAE---KTETSHEQWLFKRLQEEEAK 711
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQdkiNEELKLLKQKIDEEEEEEEK 754
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915686534 712 SGHLSREVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYR 775
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE 818
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-473 |
1.46e-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: 59.31 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 174 ELEEEKRKHKEYMEKSDEFICLLEQECERLKklidQEIKSQEEKEQEKEKRVTTLKEELTKLK-----SFALMVVDEQQR 248
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVK----SELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 249 LTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLE---KELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQ 325
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 326 KLAALSRQIDELEEtnrSLRKAEEELQDIKekiskgeygnagimAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLE- 404
Cdd:TIGR02169 883 RLGDLKKERDELEA---QLRELERKIEELE--------------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEe 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 405 --RETLQSKDFKLEVEKLSKRIMALE----KLEDAFNKSKQECYSLKCNLEKermttkqLSQELESLKVRIKELE 473
Cdd:TIGR02169 946 ipEEELSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-440 |
1.48e-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: 59.30 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEficlLEQECERLKKLIDQEIKsqeekeqek 221
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALRE--------- 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 222 ekRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTK 301
Cdd:TIGR02168 804 --ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 302 FHQ----------DQDTIMAKLTNEDSQNRQLQQKLAALSrqiDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIM-- 369
Cdd:TIGR02168 882 RASleealallrsELEELSEELRELESKRSELRRELEELR---EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAea 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 370 ------AEVEELRKRVLDMEGKDEEL--IKME--EQCRDLNKRLERETLQSKDFKLEVEKLSKRI-----MALEKLEDAF 434
Cdd:TIGR02168 959 lenkieDDEEEARRRLKRLENKIKELgpVNLAaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIeeidrEARERFKDTF 1038
|
....*.
gi 1915686534 435 NKSKQE 440
Cdd:TIGR02168 1039 DQVNEN 1044
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
245-797 |
1.69e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.98 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 245 EQQRLTAQLT-LQRQKIQ----------ELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKL 313
Cdd:pfam05557 3 ELIESKARLSqLQNEKKQmelehkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 314 TNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKME 393
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 394 EQCRDLNKR---LERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMttkqLSQELESLKVRIK 470
Cdd:pfam05557 163 SSLAEAEQRikeLEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLL----LKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 471 ELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMseklkKTEDKLQAASSQLQveQNKVTTVTEK--LIEETKRALK 548
Cdd:pfam05557 239 REEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNL-----RSPEDLSRRIEQLQ--QREIVLKEENssLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 549 SKTDVEEKMYSVTKERDDLKNKLKAEEEkgndllsrvnmLKNRLQ---SLEAIEKDFLKNKL-NQDSGKSTT-ALHQENN 623
Cdd:pfam05557 312 ARRELEQELAQYLKKIEDLNKKLKRHKA-----------LVRRLQrrvLLLTKERDGYRAILeSYDKELTMSnYSPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 624 KIKELSQEVERLKLKLKDMKAieddlmktedEYETLERRYANERDKAQFLSKELEhvkmelakyklaektetsheqwlFK 703
Cdd:pfam05557 381 RIEEAEDMTQKMQAHNEEMEA----------QLSVAEEELGGYKQQAQTLERELQ-----------------------AL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 704 RLQEEEAKSGHLSREVDALKEKIHEYMAT-----------EDLICH--LQGD-----HSVLQKKLNQQENRNRDLGREIE 765
Cdd:pfam05557 428 RQQESLADPSYSKEEVDSLRRKLETLELErqrlreqknelEMELERrcLQGDydpkkTKVLHLSMNPAAEAYQQRKNQLE 507
|
570 580 590
....*....|....*....|....*....|..
gi 1915686534 766 NLTKELERYRHFSKSLRPSLNGRRISDPQVFS 797
Cdd:pfam05557 508 KLQAEIERLKRLLKKLEDDLEQVLRLPETTST 539
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-657 |
2.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 330 LSRQIDELE------ETNRSLrKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRL 403
Cdd:COG1196 198 LERQLEPLErqaekaERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 404 ERETLQSKDFKLEVEKLSKRIMALEKledafnkskqecyslkcNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTE 483
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQ-----------------DIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 484 FTLKEDLTKLKTltvmfvdERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMysvTKE 563
Cdd:COG1196 340 EELEEELEEAEE-------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 564 RDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLK-NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDM 642
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEeAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|....*
gi 1915686534 643 KAIEDDLMKTEDEYE 657
Cdd:COG1196 490 AARLLLLLEAEADYE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-653 |
2.45e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 113 KKVLEALQRDAFQAKSTPWQEDIYEKPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEf 192
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE- 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 193 icllEQECERLKKLIDQEIKSQEEKEQEKEKRVT---TLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQelTTNAKE 269
Cdd:PTZ00121 1456 ----AKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--ADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 270 THTKLALAEARVQEEEQKATRLEK--------ELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETN 341
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKaeelkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 342 RSLRKAEEE---------LQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQcrdlnkrlerETLQSKD 412
Cdd:PTZ00121 1610 EEAKKAEEAkikaeelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE----------DKKKAEE 1679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 413 FKLEVEKLSKRIMALEKLEDAFNKSKQecysLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTK 492
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 493 LKTLTVMFVDERKTMSEKLKKTEdklqaassqlQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLK 572
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKE----------AVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 573 -AEEEKGNDLLSRVNMLKNRLQSLEaiEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVErlklKLKDMKAIEDDLMK 651
Cdd:PTZ00121 1826 eMEDSAIKEVADSKNMQLEEADAFE--KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIE----EADEIEKIDKDDIE 1899
|
..
gi 1915686534 652 TE 653
Cdd:PTZ00121 1900 RE 1901
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
205-683 |
2.99e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 205 KLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEE 284
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 285 E--------------------QKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQI----DELEET 340
Cdd:TIGR04523 186 QknidkiknkllklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLnqlkDEQNKI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 341 NRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKD--EELIKMEEQCRDLNKRLERETLQSKDFKLEVE 418
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 419 KLSKRIM------------------ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLE 480
Cdd:TIGR04523 346 QLKKELTnsesensekqreleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 481 KTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLiEETKRALKSKTDveeKMYSV 560
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL-EQKQKELKSKEK---ELKKL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 561 TKERDDLKNKLKAEEEKGNDLLSRVNMLKNRL----QSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLK 636
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1915686534 637 lklKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKME 683
Cdd:TIGR04523 582 ---KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-577 |
3.18e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 143 LDKVVEKHKESYRRILGQLLVAEKSR-RQTILELEEEKRKHKEYMEKSDEfICLLEQECERLKKlidqeiksqeekeqek 221
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEA---------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 222 ekRVTTLKEELTKLKSF--ALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQT 299
Cdd:COG4717 110 --ELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 300 TKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEEtNRSLRKAEEELQDIKEKISKGEYG--------------- 364
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLlliaaallallglgg 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 365 ---------------NAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFK--LEVEKLSKRIMAL 427
Cdd:COG4717 267 sllsliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 428 EKLEDAFNKSKQecyslkcnlEKERMTTKQLSQELESL--KVRIKELEAIESRLEKTEfTLKEDLTKLKTLTVMFVDERK 505
Cdd:COG4717 347 EELQELLREAEE---------LEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 506 TMSEKLKKT-----EDKLQAASSQLQVEQNKVTTVTEKL--IEETKRALKSKTDVEEKMYsvtkERDDLKNKLKAEEEK 577
Cdd:COG4717 417 ELEELLEALdeeelEEELEELEEELEELEEELEELREELaeLEAELEQLEEDGELAELLQ----ELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-433 |
8.30e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 228 LKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKF----- 302
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 303 ----HQDQDTIMAKLTNEDSQ------------NRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKekiskgeygna 366
Cdd:COG4942 112 alyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALL----------- 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915686534 367 gimAEVEELRKRVLDMEGKDEELIKmeeqcrDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDA 433
Cdd:COG4942 181 ---AELEEERAALEALKAERQKLLA------RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
251-819 |
1.15e-07 |
|
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: 56.52 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 251 AQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAAL 330
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 331 SRQIDELEETNRSLRKAEEELQDIKEKISKgeygnagiMAEVEELRKRvLDMEGKDEELIKMEEQCRDLNKRLER--ETL 408
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQ--------EAVLEETQER-INRARKAAPLAAHIKAVTQIEQQAQRihTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 409 QSKDFKLEVE-----KLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKvRIKELEAIESRLEKTE 483
Cdd:TIGR00618 317 QSKMRSRAKLlmkraAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 484 FTLKEDLTKLKTL--TVMFVDERKtmseklKKTEDKLQAASSQLQVEQnKVTTVTEKLIEETKRALKSKTDVEEKMYSVT 561
Cdd:TIGR00618 396 QSLCKELDILQREqaTIDTRTSAF------RDLQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 562 KERD----DLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEaiekdflknklnqdsgKSTTALHQENNKIKELSQEVERLKL 637
Cdd:TIGR00618 469 KEREqqlqTKEQIHLQETRKKAVVLARLLELQEEPCPLC----------------GSCIHPNPARQDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 638 KLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSR 717
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 718 EVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQqenrnrdLGREIENLTKELERYRHFSKSLRPSLNG-RRISDPQVF 796
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-------LHALQLTLTQERVREHALSIRVLPKELLaSRQLALQKM 685
|
570 580
....*....|....*....|...
gi 1915686534 797 SKEVQTEAVDNEPPDYKSLIPLE 819
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAQCQTLLRE 708
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
318-837 |
1.34e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 56.24 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 318 SQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGnagimaEVEELRKRVLDMEgKDEELIKMEEQCR 397
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFG------RSLKAKKRFSLLK-KETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 398 DLNKRLERETLQSKdfklEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTT-----------KQLSQELESLK 466
Cdd:COG5022 879 LAERQLQELKIDVK----SISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARlkkllnnidleEGPSIEYVKLP 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 467 VRIKELEAiESRLEKTEFTLkEDLTKLKTLTVmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVttvteKLIEETKRA 546
Cdd:COG5022 955 ELNKLHEV-ESKLKETSEEY-EDLLKKSTILV---REGNKANSELKNFKKELAELSKQYGALQEST-----KQLKELPVE 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 547 LKSKTDVEEKMYSVTKErddLKNKLKAEEEKGNDLLSrVNMLKNRLQSLEaIEKDFLKNKLNQDSGKSTTalhqeNNKIK 626
Cdd:COG5022 1025 VAELQSASKIISSESTE---LSILKPLQKLKGLLLLE-NNQLQARYKALK-LRRENSLLDDKQLYQLEST-----ENLLK 1094
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 627 ElsqeverlkLKLKDMKAIEDDLMKTEDEYETL---ERRYANERDKAQFLSKELEHVKMELAKYKLAEKT---------- 693
Cdd:COG5022 1095 T---------INVKDLEVTNRNLVKPANVLQFIvaqMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLEldglfweanl 1165
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 694 -ETSHEQWlFKRLQEEEAKSGH---------------LSREVDALKEKIHEYMATEDLICHL--QGDHSVLQKKLNQQEN 755
Cdd:COG5022 1166 eALPSPPP-FAALSEKRLYQSAlydeksklsssevndLKNELIALFSKIFSGWPRGDKLKKLisEGWVPTEYSTSLKGFN 1244
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 756 RNRDLGREIENLTKelERYRHFSKSLRPSLNGRRISdPQVFSKEVQTEAVDNEPPDYKSLIPLERAVINGQLYEESENQD 835
Cdd:COG5022 1245 NLNKKFDTPASMSN--EKLLSLLNSIDNLLSSYKLE-EEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSE 1321
|
..
gi 1915686534 836 ED 837
Cdd:COG5022 1322 EL 1323
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-781 |
1.50e-07 |
|
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: 55.95 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 164 AEKSRRQTILELEEEKRKHKEYMEKS---DEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKR----VTTLKEELTKLK 236
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKhtqaLEELTEQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 237 SFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQE--------EEQKATRLEK--------------- 293
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQElqarlsesERQRAELAEKlsklqselesvssll 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 294 -ELQTQTTKFHQDQDTIMAKLtnEDSQ---NRQLQQKLAaLSRQIDELEETNRSLRKAEEELQDIKEKISKgeygnagim 369
Cdd:pfam01576 450 nEAEGKNIKLSKDVSSLESQL--QDTQellQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEAKRNVER--------- 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 370 aEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLEREtLQSKDFKLEveklsKRIMALEKLEDAFNKSKQECYSLKCNLE 449
Cdd:pfam01576 518 -QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE-LEALTQQLE-----EKAAAYDKLEKTKNRLQQELDDLLVDLD 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 450 KERMTTKQLSQELESLKVRIKELEAIESRL----EKTEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQL 525
Cdd:pfam01576 591 HQRQLVSNLEKKQKKFDQMLAEEKAISARYaeerDRAEAEAREKETRALSLARA-LEEALEAKEELERTNKQLRAEMEDL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 526 QVEQNKVTTVTEKLiEETKRALksktdvEEKMYSVTKERDDLKNKLKAEEEKgnDLLSRVNMlknrlQSLEAIEKDFLKN 605
Cdd:pfam01576 670 VSSKDDVGKNVHEL-ERSKRAL------EQQVEEMKTQLEELEDELQATEDA--KLRLEVNM-----QALKAQFERDLQA 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 606 KLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-----ERDKAQF--LSKELE 678
Cdd:pfam01576 736 RDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEavkqlKKLQAQMkdLQRELE 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 679 HVKME----LAKYKLAEKTETSHEQWLFkRLQEEEAKSGHLSREVDALKEKIHEYMAT---------------EDLICHL 739
Cdd:pfam01576 816 EARASrdeiLAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASgasgksalqdekrrlEARIAQL 894
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1915686534 740 QGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSL 781
Cdd:pfam01576 895 EEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKS 936
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
131-678 |
1.59e-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: 55.80 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 131 WQEDIYEKPMNELDKVVEKHKESYRRILgQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLID-- 208
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQIS-ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSek 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 209 -QEIKSQEEKEQEKEKRVTTLKEELTKLKSfalmvvDEQQRLTAQLTLQRQKIQELTTNAKethTKLALAEARVQEEEQK 287
Cdd:TIGR04523 273 qKELEQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 288 ATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAG 367
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 368 IMAEVEELRKRVLDMEGKDEELIK----MEEQCRDLNKRLERETLQSKDFKLEVEKLSKRimaLEKLEDAFNKSKQECYS 443
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNqdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKELKSKEKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 444 LKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKT-----LTVMFVDERKTMSEKLKKTEDKL 518
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkeNLEKEIDEKNKEIEELKQTQKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 519 QAASSQLQveqnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKnKLKAEEEKGNDLLSRVNMLKNRL-QSLEA 597
Cdd:TIGR04523 581 KKKQEEKQ----------ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE-KAKKENEKLSSIIKNIKSKKNKLkQEVKQ 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 598 IEKDFL--KNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKdmKAIED-----DLMKTEDEYETLERRYAnerdKA 670
Cdd:TIGR04523 650 IKETIKeiRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYK--KYITRmirikDLPKLEEKYKEIEKELK----KL 723
|
....*...
gi 1915686534 671 QFLSKELE 678
Cdd:TIGR04523 724 DEFSKELE 731
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
273-777 |
1.77e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.23 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTT--KFHQDQDTIMAKltnedsqnrqlqqKLAALSRQIDELEETNRSLR--KAE 348
Cdd:PRK04778 38 KQELENLPVNDELEKVKKLNLTGQSEEKfeEWRQKWDEIVTN-------------SLPDIEEQLFEAEELNDKFRfrKAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 349 EELQDIKEKISKGEygnagimAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLeRETLQSKDFKL--EVEKLSKRima 426
Cdd:PRK04778 105 HEINEIESLLDLIE-------EDIEQILEELQELLESEEKNREEVEQLKDLYREL-RKSLLANRFSFgpALDELEKQ--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 427 LEKLEDAFNKSKQEcySLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTeftLKEDLTKLKT----------- 495
Cdd:PRK04778 174 LENLEEEFSQFVEL--TESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTE---LPDQLQELKAgyrelveegyh 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 496 LTVMFVDER-KTMSEKLKKTEDKLqaasSQLQVEqnkvttVTEKLIEETKRALKSKTDVEEKMY----SVTKERDDLKNK 570
Cdd:PRK04778 249 LDHLDIEKEiQDLKEQIDENLALL----EELDLD------EAEEKNEEIQERIDQLYDILEREVkarkYVEKNSDTLPDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 571 LKAEEEKGNDL-----------------LSRVNMLKNRLQSleaIEKDFLKNKLNQDSGKSTtalhqennkikeLSQEVE 633
Cdd:PRK04778 319 LEHAKEQNKELkeeidrvkqsytlneseLESVRQLEKQLES---LEKQYDEITERIAEQEIA------------YSELQE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 634 RLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKL--------AEKTETSHE-QWLFKR 704
Cdd:PRK04778 384 ELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNLpglpedylEMFFEVSDEiEALAEE 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 705 LQEEEAKSGHLSREVDALKEKIHE-YMATEDLIchlqgDHSVLQKKLNQQENRNRDLGREIEN-LTKELERYRHF 777
Cdd:PRK04778 464 LEEKPINMEAVNRLLEEATEDVETlEEETEELV-----ENATLTEQLIQYANRYRSDNEEVAEaLNEAERLFREY 533
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
282-771 |
4.36e-07 |
|
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: 54.41 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 282 QEEEQKATRLE----KELQTQTTKFHQDQDTIMAKLTNEDSQnrqLQQKLAALSRQIDELEETNRSL--RKAEEE--LQD 353
Cdd:pfam01576 3 QEEEMQAKEEElqkvKERQQKAESELKELEKKHQQLCEEKNA---LQEQLQAETELCAEAEEMRARLaaRKQELEeiLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 354 IKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEElikmEEQCRDlNKRLERETLQSKdfkleVEKLSKRIMALEKLEDA 433
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE----EEAARQ-KLQLEKVTTEAK-----IKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 434 FNKSK----QECYSLKCNLEKERMTTKQLSQ-------ELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVD 502
Cdd:pfam01576 150 LSKERklleERISEFTSNLAEEEEKAKSLSKlknkheaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 503 ERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVE-EKMY--SVTKERDDLKNKLKAEEEKGN 579
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEsERAArnKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 580 DLLSRVNMlKNRLQSLEAIEKDFLKNKLnQDSGKSTTALHQE-----NNKIKELSQEVE---RLKLKL-KDMKAIEDDLM 650
Cdd:pfam01576 310 DTLDTTAA-QQELRSKREQEVTELKKAL-EEETRSHEAQLQEmrqkhTQALEELTEQLEqakRNKANLeKAKQALESENA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 651 KTEDEYETL-----ERRYANERDKAQFLSKELEHVKMELAKYKLAEKTE--TSHEQWLFKRLQEEEAKSGHLSREVDALK 723
Cdd:pfam01576 388 ELQAELRTLqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSklQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 724 EKIHEY-----------MATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 771
Cdd:pfam01576 468 SQLQDTqellqeetrqkLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-786 |
4.60e-07 |
|
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: 54.29 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 447 NLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFtLKEDLTKL-KTLTVMFVDERKtmsEKLKKTEDKLQAASSQL 525
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELeLALLVLRLEELR---EELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 526 QVEQNKVTTVTEKLieETKRALKSKtdVEEKMYSVTKERDDLKNKLkaeeekgNDLLSRVNMLKNRLQSLEaiekdflkN 605
Cdd:TIGR02168 256 EELTAELQELEEKL--EELRLEVSE--LEEEIEELQKELYALANEI-------SRLEQQKQILRERLANLE--------R 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 606 KLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANerdkaqfLSKELEHVKMELA 685
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-------LEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 686 KYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEdlichLQGDHSVLQKKLNQQENRNRDLGREIE 765
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEELEEELEELQEELERLEEALE 464
|
330 340
....*....|....*....|.
gi 1915686534 766 NLTKELERYRHFSKSLRPSLN 786
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELA 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-546 |
4.62e-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: 53.61 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 274 LALAEARVQEEEQKAtrLEKELQtqttKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEetnRSLRKAEEELQD 353
Cdd:COG4942 10 LLALAAAAQADAAAE--AEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 354 IKEKISKGEygnagimAEVEELRKRvldmegKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDA 433
Cdd:COG4942 81 LEAELAELE-------KEIAELRAE------LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 434 fnkskqecyslkcnlEKERMttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKK 513
Cdd:COG4942 148 ---------------RREQA--EELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEK 206
|
250 260 270
....*....|....*....|....*....|...
gi 1915686534 514 TEDKLQAASSQLQVEQNKVTTVTEKLIEETKRA 546
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
348-773 |
6.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 348 EEELQDIKEKISKGEYGNAGI-MAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMA 426
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 427 LEKLEDafnkskqecyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKteftLKEDLTKLKT-LTVMFVDERK 505
Cdd:COG4717 128 LPLYQE---------------LEALEAELAELPERLEELEERLEELRELEEELEE----LEAELAELQEeLEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 506 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLiEETKRALKSktdveekmYSVTKERDDLKNKLKAEEE--------- 576
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELEEELEQ--------LENELEAAALEERLKEARLllliaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 577 ----KGNDLLSRVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIE 646
Cdd:COG4717 260 allgLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 647 DDLMKTEDEYETLERRYANERDKAQFlsKELEHVKMELAKYKLAEkTETSHEQWL--FKRLQEEEAKSGHLSREVDALKE 724
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1915686534 725 KIHEYMATEDLIcHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 773
Cdd:COG4717 417 ELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-405 |
8.70e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 257 RQKIQELTTnakethtKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDtiMAKLTNEDSQNRQLQQKLAALSRQIDE 336
Cdd:COG4913 609 RAKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 337 LEETNRSLRKAEEELQDIKEKISKGEygnagimaevEELRKRVLDMEGKDEELIKMEEQCRDLNKRLER 405
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELE----------EELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
205-774 |
1.09e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 205 KLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEE 284
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 285 EQKATRLEK---ELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAAlsrqIDELEETNRSLRKAEEELQDIKEKISKG 361
Cdd:TIGR04523 158 NNKYNDLKKqkeELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN----LKKKIQKNKSLESQISELKKQNNQLKDN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 362 eygnagIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQEC 441
Cdd:TIGR04523 234 ------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 442 YS------LKCNLEKERMTTKQLSQELE---SLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLK 512
Cdd:TIGR04523 308 WNkelkseLKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 513 KTEDKLQAASSQLQveqnKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRL 592
Cdd:TIGR04523 388 NLESQINDLESKIQ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 593 QSLEAIEKDFLK--NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKa 670
Cdd:TIGR04523 464 ESLETQLKVLSRsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD- 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 671 qfLSKELEHVKMELAKYKLAEktetsheqwlfkrlqeeeaksghlsrEVDALKEKIHEymatedlichLQGDHSVLQKKL 750
Cdd:TIGR04523 543 --LEDELNKDDFELKKENLEK--------------------------EIDEKNKEIEE----------LKQTQKSLKKKQ 584
|
570 580
....*....|....*....|....
gi 1915686534 751 NQQENRNRDLGREIENLTKELERY 774
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEK 608
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-711 |
1.58e-06 |
|
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: 52.74 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 125 QAKSTPWQEdIYEKPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICL--LEQECER 202
Cdd:TIGR00606 565 LLGYFPNKK-QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqdEESDLER 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 203 LKKLIDQEIKSQeekeqekekrvTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQ 282
Cdd:TIGR00606 644 LKEEIEKSSKQR-----------AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 283 EEEQKATRLEKElqtqttkfhqdQDTIMAKLTNEDSQnrqlqqklaaLSRQIDELEETNRSLRKAEEELQDIKEKISKGE 362
Cdd:TIGR00606 713 STESELKKKEKR-----------RDEMLGLAPGRQSI----------IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 363 YGNAGIMAEvEELRKRVLDMEGKDEELikmEEQCRDLNKRLERET--LQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQE 440
Cdd:TIGR00606 772 TLLGTIMPE-EESAKVCLTDVTIMERF---QMELKDVERKIAQQAakLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 441 CYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKKTEDKLQA 520
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE----IKDAKEQDSPLETFLEKDQQ 923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 521 ASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKE-RDDLKNKLKAEEEKGNDLLSRVNMLKNRL-QSLEAI 598
Cdd:TIGR00606 924 EKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKInEDMRLM 1003
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 599 EKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIE--DDLMKTEDEYETLERRYANERDKAQFLSKE 676
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQmkQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
570 580 590
....*....|....*....|....*....|....*
gi 1915686534 677 LEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAK 711
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
471-767 |
2.35e-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: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 471 ELEAIESRLEKTEFTLKEDLTKLKTLTvmfvDERKTmSEKLKKTEDKLQAASSQLQVEQNKVTtvtEKLIEETKRALKSK 550
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLR----REREK-AERYQALLKEKREYEGYELLKEKEAL---ERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 551 TDVEEKmysVTKERDDLKNKLKAEEEKGNDLLSRVNmlknRLQSLEAIEkdfLKNKLnqdsGKSTTALHQENNKIKELSQ 630
Cdd:TIGR02169 250 EEELEK---LTEEISELEKRLEEIEQLLEELNKKIK----DLGEEEQLR---VKEKI----GELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 631 EVERLKLKLKDmkaIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyklaektetsheqwLFKRLQEEEA 710
Cdd:TIGR02169 316 ELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------------LRAELEEVDK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915686534 711 KSGHLSREVDALKEKIHEYmatEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENL 767
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
312-531 |
2.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 312 KLTNEDSQNRQLQQKLAALSRQID----ELEETNRSLRKAEEELQDIKEKISKGEygnagimAEVEELRKRVldmegkDE 387
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDalqaELEELNEEYNELQAELEALQAEIDKLQ-------AEIAEAEAEI------EE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 388 ELIKMEEQCRDLNKRLERET-----LQSKDFklevEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERmttKQLSQEL 462
Cdd:COG3883 84 RREELGERARALYRSGGSVSyldvlLGSESF----SDFLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 463 ESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNK 531
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
148-755 |
3.22e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 148 EKHKESYR-RILGQLLVAEKSRRQTIL--ELEEEKRKHKEY-MEKSDEficLLEQECERLKKLIDQEIksqeeKEQEKEK 223
Cdd:COG5022 821 KLQKTIKReKKLRETEEVEFSLKAEVLiqKFGRSLKAKKRFsLLKKET---IYLQSAQRVELAERQLQ-----ELKIDVK 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEELTKLKSFALMVV-DEQQRLTAQLTLQRQKIQELTTNAKETHTKLALA-EARVQEEEQKatrlekeLQTQTTK 301
Cdd:COG5022 893 SISSLKLVNLELESEIIELKkSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSiEYVKLPELNK-------LHEVESK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 302 FHQDQDTIMAKLTNEDSQNRQLQ----------QKLAALSRQIDELEETNRSLRKAEEELQDIK--EKISKGEYGNAGIM 369
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREGNkanselknfkKELAELSKQYGALQESTKQLKELPVEVAELQsaSKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 370 AEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQ-------SKDFKLEVEKLSKRIMALEKLEDAFNKSKQecy 442
Cdd:COG5022 1046 KPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQlestenlLKTINVKDLEVTNRNLVKPANVLQFIVAQM--- 1122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 443 sLKCNLEKERMttkqlsqelESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAAS 522
Cdd:COG5022 1123 -IKLNLLQEIS---------KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS 1192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 523 SQLQVEqnkVTTVTEKLIEETKR-------------ALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLK 589
Cdd:COG5022 1193 KLSSSE---VNDLKNELIALFSKifsgwprgdklkkLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSID 1269
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 590 NRLQS-------LEAIEKDFLKN-----------KLNQDSGKSTTALHQ--ENNKIKELSQEVERLKLKLKDMKAIEDDL 649
Cdd:COG5022 1270 NLLSSykleeevLPATINSLLQYinvglfnalrtKASSLRWKSATEVNYnsEELDDWCREFEISDVDEELEELIQAVKVL 1349
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 650 MKTEDEYETLERRYanerdKAQFLSKELEHVKMeLAKYKLAEKtETSHEQWLFKRLQEEEAKS--GHLSREVDALKEKIH 727
Cdd:COG5022 1350 QLLKDDLNKLDELL-----DACYSLNPAEIQNL-KSRYDPADK-ENNLPKEILKKIEALLIKQelQLSLEGKDETEVHLS 1422
|
650 660
....*....|....*....|....*...
gi 1915686534 728 EYMATEDLICHLQGDHSVLQKKLNQQEN 755
Cdd:COG5022 1423 EIFSEEKSLISLDRNSIYKEEVLSSLSA 1450
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
310-662 |
3.28e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.39 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 310 MAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISK------GEYGNAgimaeVEELRKRVLDME 383
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKtllanrFSYGPA-----IDELEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 384 GKDEEL---------IKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRI-MALEKLEDAFNKSKQECYSLK-CNLEKER 452
Cdd:pfam06160 160 EEFSQFeeltesgdyLEAREVLEKLEEETDALEELMEDIPPLYEELKTELpDQLEELKEGYREMEEEGYALEhLNVDKEI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 453 mttKQLSQELESLKVRIKELEaiesrLEKTEFTLKEDLTKLKTLTVMF---VDERKTMSEKLKKTEDKLQAASSQLQVEQ 529
Cdd:pfam06160 240 ---QQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYDLLekeVDAKKYVEKNLPEIEDYLEHAEEQNKELK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 530 NKVTTVTEKLI---EETKRALKSKTDVE--EKMYSVTKERDD--------LKNKLKAEEEKGNDLLSRVNMLKNRLQSLE 596
Cdd:pfam06160 312 EELERVQQSYTlneNELERVRGLEKQLEelEKRYDEIVERLEekevayseLQEELEEILEQLEEIEEEQEEFKESLQSLR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 597 AIEKDFLKNKLNQDSGKSTTALHQEN------------------NKIKELSQEVERLKLklkDMKAIEDDLMKTEDEYET 658
Cdd:pfam06160 392 KDELEAREKLDEFKLELREIKRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVPL---NMDEVNRLLDEAQDDVDT 468
|
....
gi 1915686534 659 LERR 662
Cdd:pfam06160 469 LYEK 472
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-685 |
3.35e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 356 EKISKGEYGNAGIMAEVEELR-----KRVLDMEGKDEELI----KMEEQCRDLNKRLE-RETLQSKDFKLEVE----KLS 421
Cdd:COG3206 71 SGLSSLSASDSPLETQIEILKsrpvlERVVDKLNLDEDPLgeeaSREAAIERLRKNLTvEPVKGSNVIEISYTspdpELA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 422 KRImaLEKLEDAFNKskqecYSLKCNLEKERMTTKQLSQELESLKvriKELEAIESRLEktEFTLKEDLTKLKtltvmfv 501
Cdd:COG3206 151 AAV--ANALAEAYLE-----QNLELRREEARKALEFLEEQLPELR---KELEEAEAALE--EFRQKNGLVDLS------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 502 DERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLieETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDL 581
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 582 LSRVNMLKNRLQSLEAiekdflknKLNQDSGKSTTALHQEnnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLER 661
Cdd:COG3206 290 HPDVIALRAQIAALRA--------QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER 358
|
330 340
....*....|....*....|....
gi 1915686534 662 RYANERDKAQFLSKELEHVKMELA 685
Cdd:COG3206 359 EVEVARELYESLLQRLEEARLAEA 382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
160-723 |
3.71e-06 |
|
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: 51.59 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 160 QLLVAEKSRRQTILELEEEKRKHKEyMEKSDEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSFA 239
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKE-IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 240 LMVVDEQ-------QRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQT--------------- 297
Cdd:TIGR00606 311 QRTVREKerelvdcQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATrleldgfergpfser 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 298 QTTKFHQDQDTIMAKLTNEDSQN-RQLQQKLAALSRQIDELEETNRS-----------LRKAEEELQDIKEKISKGEYGN 365
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQADEIRDEKKGlgrtielkkeiLEKKQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 366 AGIMAEVEELRKRVLDM---------EGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAF-- 434
Cdd:TIGR00606 471 DRILELDQELRKAERELskaeknsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDeq 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 435 ---NKSKQECY------------SLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKL--KTLT 497
Cdd:TIGR00606 551 irkIKSRHSDEltsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYedKLFD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 498 VMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETK-------RALKSK-------TDVEEKMYSVTKE 563
Cdd:TIGR00606 631 VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEaelqefiSDLQSKLRLAPDK 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 564 RDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNqdsgKSTTALHQENNKIKELSQEVERLKLKLKDMK 643
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK-EIPELRNKLQ----KVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 644 AIEDDLMKTEDEYETL---ERRYANERDKAQF--LSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSRE 718
Cdd:TIGR00606 786 VCLTDVTIMERFQMELkdvERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
....*
gi 1915686534 719 VDALK 723
Cdd:TIGR00606 866 TNELK 870
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
197-770 |
4.48e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.37 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 197 EQECERLKKL----IDQEIKSqeekeqekekrvttLKEELTKLKSFALMVVDEQqrltaqLTLQRQKIQELTTNAKETHT 272
Cdd:PTZ00440 672 KNEYEKLEFMksdnIDNIIKN--------------LKKELQNLLSLKENIIKKQ------LNNIEQDISNSLNQYTIKYN 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTTKF-----HQDQDTIMAKLTNED--SQNRQLQQKLAALSRQIDELEEtnrSLR 345
Cdd:PTZ00440 732 DLKSSIEEYKEEEEKLEVYKHQIINRKNEFilhlyENDKDLPDGKNTYEEflQYKDTILNKENKISNDINILKE---NKK 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 346 KAEEELQDIKEKISKGEYGNAGIMAEVEELRKRvLDMEGKDEELIKMEEQCRDLNKRLErETLQskdfklEVEKLSKRIM 425
Cdd:PTZ00440 809 NNQDLLNSYNILIQKLEAHTEKNDEELKQLLQK-FPTEDENLNLKELEKEFNENNQIVD-NIIK------DIENMNKNIN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 426 ALEKLEDAFNKS---KQECYSLKCNLEKERMTTKQLSQELES------------LKVRIKELEAIESRLEKTEFT----- 485
Cdd:PTZ00440 881 IIKTLNIAINRSnsnKQLVEHLLNNKIDLKNKLEQHMKIINTdniiqkneklnlLNNLNKEKEKIEKQLSDTKINnlkmq 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 486 LKEDLTKLKTLTVMFVDERKTMSEKLKKTED-------KLQAASSQLQVEQNKVTTVT----EKLIEETKRALKSK-TDV 553
Cdd:PTZ00440 961 IEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehfksEIDKLNVNYNILNKKIDDLIkkqhDDIIELIDKLIKEKgKEI 1040
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 554 EEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNklnqdsgksttalhqennkIKELSQEVE 633
Cdd:PTZ00440 1041 EEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKK-------------------IDENKNKLI 1101
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 634 RLKLKLKDMKAIEDDLM-KTEDEYET----LERRYANERDkaqfLSKELEHVKMELAKYKLAEKTETSHEQWLF----KR 704
Cdd:PTZ00440 1102 EIKNKSHEHVVNADKEKnKQTEHYNKkkksLEKIYKQMEK----TLKELENMNLEDITLNEVNEIEIEYERILIdhivEQ 1177
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915686534 705 LQEEEAKSGHLSREVDALKEKIHEYMAteDLICHLQGDHSVLqkKLNQQENRNRDLGREIENLTKE 770
Cdd:PTZ00440 1178 INNEAKKSKTIMEEIESYKKDIDQVKK--NMSKERNDHLTTF--EYNAYYDKATASYENIEELTTE 1239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
242-884 |
7.23e-06 |
|
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: 50.43 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 242 VVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLE----------KELQTQTTKFHQDQDTIMA 311
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYEneldplknrlKEIEHNLSKIMKLDNEIKA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 312 KLTNE---DSQNRQLQQKLA----ALSRQIDELEETN-RSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRV---- 379
Cdd:TIGR00606 274 LKSRKkqmEKDNSELELKMEkvfqGTDEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlq 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 380 LDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFkLEVEKLSKRIMALEKLEDAFNKSKQECYSLKcnlEKERMTTKQLS 459
Cdd:TIGR00606 354 LQADRHQEHIRARDSLIQSLATRLELDGFERGPF-SERQIKNFHTLVIERQEDEAKTAAQLCADLQ---SKERLKQEQAD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 460 QELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKL 539
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQN 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 540 ----IEETKRALKSK-------TDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV-------NMLKNRLQSLEA---I 598
Cdd:TIGR00606 509 ekadLDRKLRKLDQEmeqlnhhTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKeinQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 599 EKDFLKnKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDM---KAIEDDLMKTEDEYETLERRYANERDKAQFLSK 675
Cdd:TIGR00606 589 TRDRLA-KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 676 ELEHVKME------LAKYKLAEKTETsheQWLFKRLQEEEAKSGHLSREVDALKEKIHEymATEDLICHLQGDHSVLQ-- 747
Cdd:TIGR00606 668 FITQLTDEnqsccpVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEK--RRDEMLGLAPGRQSIIDlk 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 748 -KKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQVFSKEVQTEAVDNEPPDYKSLIPLERAVINGQ 826
Cdd:TIGR00606 743 eKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 827 LYEESENQDEDPNDEGSVLSFKCSQSTPCPVNRKLWIPWMKSKEGHLQNGKMQTKPNA 884
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-773 |
8.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 144 DKVVEkHKESYRRILGQLLVAEKSRR---------QTILELEEEKRKHKEYMEKSD-----EFICLLEQECERLkkliDQ 209
Cdd:COG4913 228 DALVE-HFDDLERAHEALEDAREQIEllepirelaERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEEL----RA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 210 EIKSQEEKEQEKEKRVTTLKEELTKLKSfALMVVDEQQ--RLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQK 287
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEA-QIRGNGGDRleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 288 ATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELeETNRSLrkaeeelqdikekiskgeygnag 367
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-ERRKSN----------------------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 368 IMAEVEELRKRVLDMEGKDE-------ELIKMEEQCRDLNKRLEReTLQSKDFKLEVEklskrimalEKLEDAFNKsKQE 440
Cdd:COG4913 438 IPARLLALRDALAEALGLDEaelpfvgELIEVRPEEERWRGAIER-VLGGFALTLLVP---------PEHYAAALR-WVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 441 CYSLKCNLEKERMTTKQLSQELESL-------KVRIKELEA---IESRLEKTEFTLK-EDLTKLK------TLTVMfVDE 503
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLdpdslagKLDFKPHPFrawLEAELGRRFDYVCvDSPEELRrhpraiTRAGQ-VKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 504 RKTMSEK--------------------------LKKTEDKLQAASSQLQVEQNKVTTVTEKLieETKRALKSKTDVEEKM 557
Cdd:COG4913 586 NGTRHEKddrrrirsryvlgfdnraklaaleaeLAELEEELAEAEERLEALEAELDALQERR--EALQRLAEYSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 558 YSVTKERDDLKNKLkAEEEKGNDLLSRvnmLKNRLQSLEAIEKDflknkLNQDSGKSTTALHQENNKIKELSQEVERLKL 637
Cdd:COG4913 664 ASAEREIAELEAEL-ERLDASSDDLAA---LEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 638 KLKDMKAIEDdlmktEDEYETLERRYAN------ERDKAQFLSKELEHVKMELAkyKLAEKTETSHEQwlFKRLQEEEAk 711
Cdd:COG4913 735 RLEAAEDLAR-----LELRALLEERFAAalgdavERELRENLEERIDALRARLN--RAEEELERAMRA--FNREWPAET- 804
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915686534 712 sGHLSREVDALKE--KIHEYMATEDLICHlqgdhsvlQKKLNQQENRNrdLGREIENLTKELER 773
Cdd:COG4913 805 -ADLDADLESLPEylALLDRLEEDGLPEY--------EERFKELLNEN--SIEFVADLLSKLRR 857
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
284-434 |
8.42e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 284 EEQKATRLEKELQT-QTTKFHQDQDtimakLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGE 362
Cdd:COG2433 383 EELIEKELPEEEPEaEREKEHEERE-----LTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 363 YGNAGIMAEVEELRKRVLDMEGkdeELIKMEEQCRDLNKRLER-ETLQSKDFK------LEVEKLSKRimALEKLEDAF 434
Cdd:COG2433 458 RREIRKDREISRLDREIERLER---ELEEERERIEELKRKLERlKELWKLEHSgelvpvKVVEKFTKE--AIRRLEEEY 531
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
140-343 |
1.39e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 140 MNELDKVVEKHKESYRRILGQLLVAEK---SRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLIDQEIKSQEE 216
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 217 KEQEKEKRVTTLKEELTKL-KSFALM--VVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEK 293
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAvRRLQYLkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1915686534 294 ELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRS 343
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
273-512 |
1.54e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQ-QKLAALSRQID-ELEETNRSLRKAEEE 350
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAKTIKaEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 351 LQDIKEKISKGEYGNAGIMAEVEELRKrVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKL 430
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKSKIEQFQK-VIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 431 EDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAiESRLEKTEF-TLKEDLTKL---KTLTVMFVDERKT 506
Cdd:PHA02562 329 MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-EFVDNAEELaKLQDELDKIvktKSELVKEKYHRGI 407
|
....*.
gi 1915686534 507 MSEKLK 512
Cdd:PHA02562 408 VTDLLK 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
247-409 |
1.99e-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: 47.23 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 247 QRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNrqLQQK 326
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA--LQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 327 LAALSRQIDELEEtnrSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRV-LDMEGKDEELIKMEEQCRDLNKRLER 405
Cdd:COG1579 98 IESLKRRISDLED---EILELMERIEELEEELAELEAELAELEAELEEKKAELdEELAELEAELEELEAEREELAAKIPP 174
|
....
gi 1915686534 406 ETLQ 409
Cdd:COG1579 175 ELLA 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
592-775 |
2.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 592 LQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQ 671
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 672 FLSKELEHVKMELAKYKLAEKTETSHEQWlfKRLQEEEAKSGHLSREVDALKEKIHEY------------MATEDLICHL 739
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEELEELEAELAELqeeleelleqlsLATEEELQDL 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 1915686534 740 QGDHSVLQKKLNQQENRNRDLGREIENLTKELERYR 775
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
377-782 |
2.52e-05 |
|
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: 48.81 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 377 KRVLDMEGKDEELIKMEEQCRdlnKRLERETLQSKDFKLEVEklskrimALEKLEDAFNKSKQECYSLKCNLEKERMTTK 456
Cdd:pfam02463 135 YNFLVQGGKIEIIAMMKPERR---LEIEEEAAGSRLKRKKKE-------ALKKLIEETENLAELIIDLEELKLQELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 457 QLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVT 536
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 537 EKLIEETKRALKSKtdvEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTT 616
Cdd:pfam02463 285 EEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 617 ALHQENNKIKElsqevERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETS 696
Cdd:pfam02463 362 EKLQEKLEQLE-----EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 697 HEQWLFKR--------LQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLT 768
Cdd:pfam02463 437 ESIELKQGklteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
410
....*....|....
gi 1915686534 769 KELERYRHFSKSLR 782
Cdd:pfam02463 517 KDGVGGRIISAHGR 530
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
142-792 |
3.35e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 142 ELDKVVEKHKESYRRILGQLLVAEK-------------SRRQTILELEEEKRKHKEYMEKSDEFICLLEQEcERLKKLID 208
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSlernydklkdvidMLRAEISNIDYLEEKLKSSNLELENIKKQIADD-EKSHSITL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 209 QEIKSQEEKEQEKEKRVTTLKEELTKLKSFAlmvvDEQQRLTAQLtlqrqkiqelttnaKETHTKLALAEARVQEEEQKA 288
Cdd:PRK01156 218 KEIERLSIEYNNAMDDYNNLKSALNELSSLE----DMKNRYESEI--------------KTAESDLSMELEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 289 TRLEKelqTQTTKFHQDQDTIMAKLTNEdSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISkgeygnagi 368
Cdd:PRK01156 280 ERHMK---IINDPVYKNRNYINDYFKYK-NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS--------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 369 maEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKledafnkskqecySLKCNL 448
Cdd:PRK01156 347 --RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD-------------AIKKEL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 449 EKERMTTKQLSQELESLKVRIKELEAIESRLEKTE-------------FTLKEDltKLKTLTVMFVDERKTMSEKLKKTE 515
Cdd:PRK01156 412 NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgTTLGEE--KSNHIINHYNEKKSRLEEKIREIE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 516 DKLQAASSQlQVEQNKVTTVTEKliEETKRALKSKTDVEEKMYSVTKERDDLkNKLKAEEEKGNDLLSRVNMLKnrLQSL 595
Cdd:PRK01156 490 IEVKDIDEK-IVDLKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLK--LEDL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 596 EAIEKDFLkNKLNQDSGKSTTALHQE----NNKIKELSQEVERLKLKLKDMKA-IEDDLMKTEDEYETLERRYANERDKA 670
Cdd:PRK01156 564 DSKRTSWL-NALAVISLIDIETNRSRsneiKKQLNDLESRLQEIEIGFPDDKSyIDKSIREIENEANNLNNKYNEIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 671 ---QFLSKELEHVKMELAKYKLAEKTETSheqwLFKRLQEEEAKSGHLSREVDALKEKIHEYMATedlichlqgdHSVLQ 747
Cdd:PRK01156 643 iliEKLRGKIDNYKKQIAEIDSIIPDLKE----ITSRINDIEDNLKKSRKALDDAKANRARLEST----------IEILR 708
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1915686534 748 KKLNQQENRNRDLGREIENLTK------ELERYRH-FSKSLRPSLNGRRISD 792
Cdd:PRK01156 709 TRINELSDRINDINETLESMKKikkaigDLKRLREaFDKSGVPAMIRKSASQ 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
456-712 |
3.47e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 456 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLktltvmfvderktmSEKLKKTEDKLQAASSQLQVEQNKVTTV 535
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------ERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 536 TEKlIEETKRALKsktdveekmysvtKERDDLKNKLKAEEEKGNdlLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKST 615
Cdd:COG4942 89 EKE-IAELRAELE-------------AQKEELAELLRALYRLGR--QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 616 TALHQENNKIKELSQEVERLKLKLKDMKAieddlmKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTET 695
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLA------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*..
gi 1915686534 696 SheqwLFKRLQEEEAKS 712
Cdd:COG4942 227 A----LIARLEAEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
224-355 |
6.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNA--KETHTKLALAEARVQEEEQKAT-------RLEKE 294
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTpnhpdviALRAQ 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915686534 295 LQTQTTKFHQDQDTIMAKLtneDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIK 355
Cdd:COG3206 300 IAALRAQLQQEAQRILASL---EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
329-785 |
7.15e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 329 ALSRQIDELEETNRSLrKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETL 408
Cdd:TIGR00606 170 ALKQKFDEIFSATRYI-KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 409 QSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQEleslkvrikELEAIESRLEKTEFTLKE 488
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE---------QLNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 489 DLTKLKTLTVMFVDERKTMSEklKKTEDKLQAASSQLQVEQNKVTTVTEKLiEETKRALKSKTDVEEKMYSVTKErddLK 568
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQ--EKTELLVEQGRLQLQADRHQEHIRARDS-LIQSLATRLELDGFERGPFSERQ---IK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 569 NKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTT------ALHQENNKIKELSQEVERLKLKLKDM 642
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTielkkeILEKKQEELKFVIKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 643 KAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTE------TSHEQWLF---KRLQEEEAKSG 713
Cdd:TIGR00606 474 LELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtTTRTQMEMltkDKMDKDEQIRK 553
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915686534 714 HLSREVDALKEKIHEYMATEDLICHLQGdhsvLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 785
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHS----KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
224-607 |
7.78e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.82 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEEL-TKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKF 302
Cdd:pfam15964 304 RLTKERDDLmSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 303 HQDQDTIMAKLTNEDSQNRQ----LQQKLAALSRQIDELEETNRSLRKAEEELQ---------------DIKEKISKGEY 363
Cdd:pfam15964 384 AQEKEALRKEMKKEREELGAtmlaLSQNVAQLEAQVEKVTREKNSLVSQLEEAQkqlasqemdvtkvcgEMRYQLNQTKM 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 364 GNAGIMAEVEELRKRVL-DMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKrimALEKLEDAFNKSKQECY 442
Cdd:pfam15964 464 KKDEAEKEHREYRTKTGrQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTE---LLGESEHQLHLTRLEKE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 443 SLKCNLEKE-RMTTKQLSQELESLKVRIKELEAiesRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAA 521
Cdd:pfam15964 541 SIQQSFSNEaKAQALQAQQREQELTQKMQQMEA---QHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSE 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 522 SSQLQVEQNKVTTVTEKLIEETKRaLKSKTDVEEKMYSVTKER-DDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLeAIEK 600
Cdd:pfam15964 618 VEQLSQEKEYLQDRLEKLQKRNEE-LEEQCVQHGRMHERMKQRlRQLDKHCQATAQQLVQLLSKQNQLFKERQNL-TEEV 695
|
....*..
gi 1915686534 601 DFLKNKL 607
Cdd:pfam15964 696 QSLRSQV 702
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
237-403 |
1.01e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 46.77 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 237 SFALMVVDeqQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMA---KL 313
Cdd:COG5283 2 QVILGAVD--KPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQagiDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 314 TNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISK-GEYGNAGI-------------------MAEVe 373
Cdd:COG5283 80 RQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRlAGAGAAAAaigaalaasvkpaidfedaMADV- 158
|
170 180 190
....*....|....*....|....*....|
gi 1915686534 374 elrKRVLDMEGKDEELIKMEEQCRDLNKRL 403
Cdd:COG5283 159 ---AATVDLDKSSEQFKALGKQARELSAQT 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
344-493 |
1.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 344 LRKAEEELQDIKEKISKgeygnagimaEVEELRKRVLdMEGKDEELIKMEEQCRDLNKRleRETLQSKDFKLE--VEKLS 421
Cdd:PRK12704 33 IKEAEEEAKRILEEAKK----------EAEAIKKEAL-LEAKEEIHKLRNEFEKELRER--RNELQKLEKRLLqkEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 422 KRIMALEKLEDAFNKSKQECYSLKCNLEK-----ERMTTKQLsQELEslkvRIKEL---EAIESRLEKTEFTLKEDLTKL 493
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKkeeelEELIEEQL-QELE----RISGLtaeEAKEILLEKVEEEARHEAAVL 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
198-401 |
1.29e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 198 QECERLKKLIDQEIKS----QEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTK 273
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 274 LALAEARVQEEEQKATRLEK--ELQTQTTKFHQDQDtIMAKLTNedsQNRQLQQKLAALSRQIDELEETNRSLRKAEEEL 351
Cdd:PHA02562 264 AAKIKSKIEQFQKVIKMYEKggVCPTCTQQISEGPD-RITKIKD---KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1915686534 352 QDIKEKISKGEYG-------NAGIMAEVEELRKRVLDmegKDEELIKMEEQCRDLNK 401
Cdd:PHA02562 340 LELKNKISTNKQSlitlvdkAKKVKAAIEELQAEFVD---NAEELAKLQDELDKIVK 393
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
224-409 |
1.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 224 RVTTLKEEL----TKLKSFA----LMVVDEQ-QRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLE-- 292
Cdd:COG3206 183 QLPELRKELeeaeAALEEFRqkngLVDLSEEaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 293 ---KELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDelEETNRSLRKAEEELQDIKEKIskgeygnAGIM 369
Cdd:COG3206 263 pviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ--QEAQRILASLEAELEALQARE-------ASLQ 333
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915686534 370 AEVEELRKRVLDMEGKDEELIKMEEQcRDLNKRLERETLQ 409
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLERE-VEVARELYESLLQ 372
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
246-352 |
1.38e-04 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 46.25 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 246 QQRL--TAQLTLQRQkiqelttNAKETHTklalAEARVQEEEqkatrlekeLQTQTTKFHQDQDTIMAKLTNEDSQNRQL 323
Cdd:PRK06975 345 NRKVdrLDQELVQRQ-------QANDAQT----AELRVKTEQ---------AQASVHQLDSQFAQLDGKLADAQSAQQAL 404
|
90 100 110
....*....|....*....|....*....|.
gi 1915686534 324 QQKLAALSRQID--ELEETNRSLRKAEEELQ 352
Cdd:PRK06975 405 EQQYQDLSRNRDdwMIAEVEQMLSSASQQLQ 435
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
256-427 |
1.45e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 256 QRQKIQELTTNAKETHTKLALAEARvQEEEQKATRLEKE-------LQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLA 328
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEAK-EEIHKLRNEFEKElrerrneLQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 329 ALSRQIDELEETNRSLRKAEEELQDIKEKISkgeygnaGIMAevEELRKRVLDmegkdeeliKMEEQCRD----LNKRLE 404
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERIS-------GLTA--EEAKEILLE---------KVEEEARHeaavLIKEIE 179
|
170 180
....*....|....*....|...
gi 1915686534 405 RETlqskdfKLEVEKLSKRIMAL 427
Cdd:PRK12704 180 EEA------KEEADKKAKEILAQ 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
219-798 |
1.63e-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: 45.78 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 219 QEKEKRVTTLKEEL----TKLKSFALMVVD-----------------EQQRLTAQLTLQRQKIQELTTNAKETHTKLALA 277
Cdd:TIGR04523 36 KQLEKKLKTIKNELknkeKELKNLDKNLNKdeekinnsnnkikileqQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 278 EARVQEEEQKATRLEKELQ----------TQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEE----TNRS 343
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKenkknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 344 LRKAEEELQDIKEKISKgeygNAGIMAEVEELRKRVL-----------DMEGKDEELIKMEEQCRDLNKRLERETLQSKD 412
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQK----NKSLESQISELKKQNNqlkdniekkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 413 FKLEVEKLSKRImalEKLEDAFNKSKQECYSLkcNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTK 492
Cdd:TIGR04523 272 KQKELEQNNKKI---KELEKQLNQLKSEISDL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 493 LKTLTVMFVDERKTMSEKLKKTEDKLQ-----------------AASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEE 555
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEklkkenqsykqeiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 556 KMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLK--NKLNQDSGKSTTALHQENNKIKELSQEVE 633
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 634 RLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKaqfLSKELEHVKMELAKYKLAEK--------TETSHEQWLFKRL 705
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFELKKENLEKEideknkeiEELKQTQKSLKKK 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 706 QEE-EAKSGHLSREVDALKEKIHEYMATEdlichlqgdhSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPS 784
Cdd:TIGR04523 584 QEEkQELIDQKEKEKKDLIKEIEEKEKKI----------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
650
....*....|....
gi 1915686534 785 LNGRRISDPQVFSK 798
Cdd:TIGR04523 654 IKEIRNKWPEIIKK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
137-660 |
1.70e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 137 EKPMNELDKVVEKHKESYRRILGQLLVAEKSRRqtilELEEEKRK--------HKEYME--------------KSDEFIC 194
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKlegestdlQEQIAElqaqiaelraqlakKEEELQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 195 LL---EQECER----LKKL---------IDQEIKSQEEKEQEKEKRVTTLKEELTKLKSfalMVVDEQQRLTAQLTLQRQ 258
Cdd:pfam01576 248 ALarlEEETAQknnaLKKIreleaqiseLQEDLESERAARNKAEKQRRDLGEELEALKT---ELEDTLDTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 259 KIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELE 338
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 339 etnRSLRKAEEELQDIKEKISKGEYGNA-------GIMAEVEELRKRVLDMEGKD----EELIKMEEQCRDLNKRLERET 407
Cdd:pfam01576 405 ---HKRKKLEGQLQELQARLSESERQRAelaeklsKLQSELESVSSLLNEAEGKNiklsKDVSSLESQLQDTQELLQEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 408 LQ-----SKDFKLEVEKLSKRIMALEKLEDAFNKSKQ------ECYSLKCNLEKERMTT-------KQLSQELESLKVRI 469
Cdd:pfam01576 482 RQklnlsTRLRQLEDERNSLQEQLEEEEEAKRNVERQlstlqaQLSDMKKKLEEDAGTLealeegkKRLQRELEALTQQL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 470 KELEAIESRLEKTEFTLKEDLTKLktltVMFVDERKTMSEKLKKTEDKLqaasSQLQVEQNkvtTVTEKLIEETKRALKS 549
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDL----LVDLDHQRQLVSNLEKKQKKF----DQMLAEEK---AISARYAEERDRAEAE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 550 KTDVEEKMYSVTKERDDLKNKlKAEEEKGNdllsrvnmlknrlQSLEAIEKDFLKNKlnQDSGKSttaLHQENNKIKELS 629
Cdd:pfam01576 631 AREKETRALSLARALEEALEA-KEELERTN-------------KQLRAEMEDLVSSK--DDVGKN---VHELERSKRALE 691
|
570 580 590
....*....|....*....|....*....|.
gi 1915686534 630 QEVERLKLKLKDMkaiEDDLMKTEDEYETLE 660
Cdd:pfam01576 692 QQVEEMKTQLEEL---EDELQATEDAKLRLE 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-409 |
1.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 63 QAEDLSRDDLLFLLSILEGELQARDEVIGILKAEKMDLALLEAQY----GFVTPKKVLEALQRDAFQAKSTPWQEDIYEK 138
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 139 PMNE------LDKVVEKHKESYRRIlgQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFI--------CLLEQECERLK 204
Cdd:COG1196 539 ALEAalaaalQNIVVEDDEVAAAAI--EYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaavdlvaSDLREADARYY 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 205 KLIDQE---------IKSQEEKEQEKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLA 275
Cdd:COG1196 617 VLGDTLlgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 276 LAEARVQEEEQKATRLEKELQTQTtkfHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIK 355
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEE---LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1915686534 356 EKISKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQ 409
Cdd:COG1196 774 REIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-440 |
2.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 232 LTKLKSFALMVVDEQQRLTAQLTLQRQKIQEL-------TTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTTKFHQ 304
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELlaalglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 305 DQDTIMAKLTNEDS---------QNRQLQQKLAALSRQIDELEETNRSLRKA------EEELQDIKEKISKGEygnagim 369
Cdd:COG4717 373 AALLAEAGVEDEEElraaleqaeEYQELKEELEELEEQLEELLGELEELLEAldeeelEEELEELEEELEELE------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915686534 370 AEVEELRKRVLDMEgkdEELIKMEEQCRDLNKRLERETLQSKdFKLEVEKLSKRIMALEKLEDAFNKSKQE 440
Cdd:COG4717 446 EELEELREELAELE---AELEQLEEDGELAELLQELEELKAE-LRELAEEWAALKLALELLEEAREEYREE 512
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
322-801 |
2.50e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 322 QLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGIMAEVEELRKRVldmEGKDEELIKMeEQCRDlnk 401
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQL---EQLQEENFRL-ETARD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 402 rleretlqskDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMT---TKQLSQELESLKVRIKELEaiesr 478
Cdd:pfam05622 84 ----------DYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESsdkVKKLEATVETYKKKLEDLG----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 479 lektefTLKEDLTKLKTLTVMFVDERKTMSEKLKKTedklQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTD---VEE 555
Cdd:pfam05622 149 ------DLRRQVKLLEERNAEYMQRTLQLEEELKKA----NALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 556 KMYSVTKERDDLKNK----------LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLnqdsgKSTTALHQENNKI 625
Cdd:pfam05622 219 KLEALQKEKERLIIErdtlretneeLRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEI-----REKLIRLQHENKM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 626 KELSQEvERLKLKLKDMKAIEDDLMKTEDEYETlERRYANERdkaqflSKELEHVKMELAKYKLAEKTETSHEQWLFKRL 705
Cdd:pfam05622 294 LRLGQE-GSYRERLTELQQLLEDANRRKNELET-QNRLANQR------ILELQQQVEELQKALQEQGSKAEDSSLLKQKL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 706 QEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHsvLQKKLNQQENRNRDLGreiENLTKELERYRHFSKSLRPSL 785
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDE--LQEALRKKDEDMKAME---ERYKKYVEKAKSVIKTLDPKQ 440
|
490
....*....|....*.
gi 1915686534 786 NGRRISDPQVFSKEVQ 801
Cdd:pfam05622 441 NPASPPEIQALKNQLL 456
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
310-700 |
2.65e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 310 MAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEE-LQDIKEKISKGEYGN--AGIMAEVEEL---RKRVLD-- 381
Cdd:TIGR01612 485 IDENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIiGFDIDQNIKAKLYKEieAGLKESYELAknwKKLIHEik 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 382 --MEGKDEELIKMEEQCRDL-NKRLE--RETLQSKDFKLEVEklskrimalEKLEDAFNKSK--QECYSLKCNLEKERMT 454
Cdd:TIGR01612 565 keLEEENEDSIHLEKEIKDLfDKYLEidDEIIYINKLKLELK---------EKIKNISDKNEyiKKAIDLKKIIENNNAY 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 455 TKQLS-----QELESLKVRIKELEAIESRLEKTeftLKEDLTKLKTLTVMFVDErktmsEKLKKTEDK--LQAASSQLQV 527
Cdd:TIGR01612 636 IDELAkispyQVPEHLKNKDKIYSTIKSELSKI---YEDDIDALYNELSSIVKE-----NAIDNTEDKakLDDLKSKIDK 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 528 EQNKVTTVTEKLIE------ETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNrlqslEAIEKD 601
Cdd:TIGR01612 708 EYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK-----EKDELN 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 602 FLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLerryanerdKAQFLSKELEHVK 681
Cdd:TIGR01612 783 KYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFM---------KDDFLNKVDKFIN 853
|
410
....*....|....*....
gi 1915686534 682 MElakYKLAEKTETSHEQW 700
Cdd:TIGR01612 854 FE---NNCKEKIDSEHEQF 869
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
198-728 |
2.87e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 198 QECERLKKLIDQEIksqeekeqekekrvTTLKEELTklksfalmvvdEQQRLTAQLTLQRQKIQElttnakethtKLALA 277
Cdd:pfam01576 204 QELEKAKRKLEGES--------------TDLQEQIA-----------ELQAQIAELRAQLAKKEE----------ELQAA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 278 EARVQEEEQKATRLEK---ELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQI-DELEETNrslrkAEEELQD 353
Cdd:pfam01576 249 LARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELeDTLDTTA-----AQQELRS 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 354 IKEkiskgeygnagimAEVEELRKRVldmegkDEELIKMEEQCRDLNKRlERETLQSKDFKLEVEKLSKriMALEKLEDA 433
Cdd:pfam01576 324 KRE-------------QEVTELKKAL------EEETRSHEAQLQEMRQK-HTQALEELTEQLEQAKRNK--ANLEKAKQA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 434 FNKSKQEcyslkcnLEKERMTTKQLSQELE----SLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvdERKTMSE 509
Cdd:pfam01576 382 LESENAE-------LQAELRTLQQAKQDSEhkrkKLEGQLQELQARLSESERQRAELAEKLSKLQS-------ELESVSS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 510 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTdveeKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLK 589
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLST----RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 590 NRLQSleaiekdfLKNKLNQDSGksttALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKT----EDEYETLERRYAN 665
Cdd:pfam01576 524 AQLSD--------MKKKLEEDAG----TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTknrlQQELDDLLVDLDH 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915686534 666 ERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHE 728
Cdd:pfam01576 592 QRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEE 654
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
328-496 |
3.22e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 328 AALSRQI-----DELEETNRSLRKAEEELQDIKEKISKGEygnagimAEVEELRKRVLDMEG----KDEELIKMEEQCRD 398
Cdd:COG2433 380 EALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAeleeKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 399 LNKRLERETLQSKdfklEVEKLSKRIMALEKledafnkskqecyslkcnlekermttkqlsqELESLKVRIKELEAIESR 478
Cdd:COG2433 453 ARSEERREIRKDR----EISRLDREIERLER-------------------------------ELEEERERIEELKRKLER 497
|
170
....*....|....*....
gi 1915686534 479 LEKTEFTL-KEDLTKLKTL 496
Cdd:COG2433 498 LKELWKLEhSGELVPVKVV 516
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
132-636 |
4.73e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 132 QEDIYE---KPMNELDKVvEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSdeficlLEQECERLkklid 208
Cdd:TIGR01612 1185 KKNIYDeikKLLNEIAEI-EKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKA------MEAYIEDL----- 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 209 QEIKSQEEKEQEKEKRVTTLKEELtklKSFALMVVDEQQRLTAQltlqrQKIQELTTNAKETHTKLALAEARvqeeEQKA 288
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGIEMDIKAEM---ETFNISHDDDKDHHIIS-----KKHDENISDIREKSLKIIEDFSE----ESDI 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 289 TRLEKELQT---QTTKFHQDQDTIMAKLTN-----EDSQNRQLQQKLAALSRQIDELEET-NRSLRKAEEELQDIKEKIS 359
Cdd:TIGR01612 1321 NDIKKELQKnllDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNiKDELDKSEKLIKKIKDDIN 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 360 KGEYGNA-----------GIMAEVEELRKRVLDMEGKDEELIKMEEQCRDlNKRLERETLQSKDFKLE-VEKLSK----- 422
Cdd:TIGR01612 1401 LEECKSKiestlddkdidECIKKIKELKNHILSEESNIDTYFKNADENNE-NVLLLFKNIEMADNKSQhILKIKKdnatn 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 423 ----RIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEaIESRLEKTEFTLKEDLTKLKTLTV 498
Cdd:TIGR01612 1480 dhdfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKFAKTKKDSEIIIKEIKDAHK 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 499 MFVDERKTMSEKLKKTEDKlqaassQLQVE--------QNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK 570
Cdd:TIGR01612 1559 KFILEAEKSEQKIKEIKKE------KFRIEddaakndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKK 1632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915686534 571 LK-----AEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKlnqdsgkstTALHQENNKIKELSQEVERLK 636
Cdd:TIGR01612 1633 ISsfsidSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKK---------KELDELDSEIEKIEIDVDQHK 1694
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-360 |
4.88e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 132 QEDIYEKPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEFICLLEQECERLKKLIDQei 211
Cdd:PHA02562 196 QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQ-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 212 ksqeekeqekekrvttlkeeLTKLKSFaLMVVDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKatrl 291
Cdd:PHA02562 274 --------------------FQKVIKM-YEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI---- 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915686534 292 EKELQTQTTKFHQDQDTIMAK---LTNEDSQNRQLQqklAALSRQIDELEETNRSLRKAEEELQDIKEKISK 360
Cdd:PHA02562 329 MDEFNEQSKKLLELKNKISTNkqsLITLVDKAKKVK---AAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
350-550 |
6.26e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 350 ELQDIKEKISKgeygnagIMAEVEELRKRVLDMEgkdEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEK 429
Cdd:COG1579 11 DLQELDSELDR-------LEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 430 LEDAFNKSKQecYslkcnlekermttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSE 509
Cdd:COG1579 81 QLGNVRNNKE--Y-------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1915686534 510 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSK 550
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
535-722 |
8.50e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 535 VTEKLIEEtkralksKTDVEEKMYSVTKERDDlkNKLKAEEEKGNDLLSRVNMLKNRLQSLEaiekdflknklnqdsgks 614
Cdd:COG2433 381 ALEELIEK-------ELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELE------------------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 615 ttalhqenNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANerdkaqfLSKELEHVKMELAkyKLAEKTE 694
Cdd:COG2433 434 --------AELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-------LERELEEERERIE--ELKRKLE 496
|
170 180
....*....|....*....|....*....
gi 1915686534 695 tsheqwLFKRLQEEEAKSGHLS-REVDAL 722
Cdd:COG2433 497 ------RLKELWKLEHSGELVPvKVVEKF 519
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
291-430 |
8.78e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 291 LEKELQTQTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKA-EEELQDIKEKISKGEYGNAGIM 369
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKV 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915686534 370 AEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKL-EVEKLSKRIMALEKL 430
Cdd:smart00787 225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFkEIEKLKEQLKLLQSL 286
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
138-660 |
9.13e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 138 KPMNELDKVVEKHKESYRRILGQLLVAEKSRRQTILELEEEKRKHKEYMEKSDEfiCLLEQECERLKKLIDQEIKSQEEK 217
Cdd:TIGR01612 917 KKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDN--TLIDKINELDKAFKDASLNDYEAK 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 218 EQEKEKRVTTLKEELTKLKSFAL-MVVDEQQRLTAQLTlqrQKIQELTTNAKETHTKLALAEARVQEEEQKA-------- 288
Cdd:TIGR01612 995 NNELIKYFNDLKANLGKNKENMLyHQFDEKEKATNDIE---QKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniell 1071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 289 -TRLEKELQTQTTKFHQDQDTImaKLTNEDSQNRQLQQKLAALSRQI-DELEETNRSLRKAEEELQDIKEKisKGEYGNA 366
Cdd:TIGR01612 1072 nKEILEEAEINITNFNEIKEKL--KHYNFDDFGKEENIKYADEINKIkDDIKNLDQKIDHHIKALEEIKKK--SENYIDE 1147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 367 gIMAEVEELRKrVLDMEGKDEELIKMEEQCRDLNKRLEREtlqsKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKC 446
Cdd:TIGR01612 1148 -IKAQINDLED-VADKAISNDDPEEIEKKIENIVTKIDKK----KNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGK 1221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 447 NLEKerMTTKQLSQELESLKVRIKELEAIESRLEKteftLKEDLTKLKTLTVMFVDERKTMsEKLKKTEDKLQAASSQLQ 526
Cdd:TIGR01612 1222 NLGK--LFLEKIDEEKKKSEHMIKAMEAYIEDLDE----IKEKSPEIENEMGIEMDIKAEM-ETFNISHDDDKDHHIISK 1294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 527 VEQNKVTTVTEKlieetkrALKSKTDVEEKmysvtKERDDLKNKLK---AEEEKGNdllSRVNMLKNRLQSLEAIEK-DF 602
Cdd:TIGR01612 1295 KHDENISDIREK-------SLKIIEDFSEE-----SDINDIKKELQknlLDAQKHN---SDINLYLNEIANIYNILKlNK 1359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 603 LKNKLNqdsgksttalhqennKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLE 660
Cdd:TIGR01612 1360 IKKIID---------------EVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLE 1402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
244-532 |
9.76e-04 |
|
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: 43.40 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 244 DEQQRLTAQLTLQRQKIQELttnaKETHTKLA--LAEARVQEEEQKATRLEkELQTQTTKFHQDQDTIMAKltneDSQNR 321
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQL----KEQLQLLNklLPQANLLADETLADRLE-ELREELDAAQEAQAFIQQH----GKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 322 QLQQKLAALSRQIDELEETNRSLRKAEEELQDIKekiskgeygnAGIMAeVEELRKRVLDMEGKDEEliKMEEQCRDLNK 401
Cdd:COG3096 921 QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLK----------QQIFA-LSEVVQRRPHFSYEDAV--GLLGENSDLNE 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 402 RLERETLQSKdfklevEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEK 481
Cdd:COG3096 988 KLRARLEQAE------EARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR 1061
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 482 TEftLKEDLTKL--------KTLTVmFVDERKTMSEKLKKTEDKLQAASSqlQVEQNKV 532
Cdd:COG3096 1062 DE--LHEELSQNrsrrsqleKQLTR-CEAEMDSLQKRLRKAERDYKQERE--QVVQAKA 1115
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
246-556 |
1.02e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.22 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 246 QQRLTAQ-LTLQRQK--IQELTTNAKETHTKL-----ALAEARVQEEEQKATRLEKELQTQTTKFHQDQDTIMAKLTNED 317
Cdd:pfam18971 562 ENKLTAKgLSLQEANklIKDFLSSNKELAGKAlnfnkAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKS 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 318 SQNRQLQQKLAALSrQIDEL-----EETNR---------SLRKAEEELQDIKEKISKgeygnagimaEVEELRKRVLDME 383
Cdd:pfam18971 642 GNKNKMEAKAQANS-QKDEIfalinKEANRdaraiaytqNLKGIKRELSDKLEKISK----------DLKDFSKSFDEFK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 384 -GKDEELIKMEEQCRDLNKRLeretlqsKDFKLEVEKLSK---RIMALEKLEDAFNKSKQECYSLKCNLE---KERMTTK 456
Cdd:pfam18971 711 nGKNKDFSKAEETLKALKGSV-------KDLGINPEWISKvenLNAALNEFKNGKNKDFSKVTQAKSDLEnsvKDVIINQ 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 457 QLSQELESLKVRIKELEAIE--SRLEKTeftlkedLTKLKTLTvmfvdeRKTMSEKLKKTEDKLQAASSQL-QVEQNKV- 532
Cdd:pfam18971 784 KVTDKVDNLNQAVSVAKAMGdfSRVEQV-------LADLKNFS------KEQLAQQAQKNEDFNTGKNSELyQSVKNSVn 850
|
330 340
....*....|....*....|....*..
gi 1915686534 533 -TTVTEKL--IEETKRAlKSKTDVEEK 556
Cdd:pfam18971 851 kTLVGNGLsgIEATALA-KNFSDIKKE 876
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
372-816 |
1.21e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 372 VEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKE 451
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 452 RMTTKQLSQELESLKVRIKELEAIESRLEKTE--------------FTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDk 517
Cdd:PRK01156 255 ESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyknrnyindyFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 518 LQAASSQLQVEQNKvttvteklIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN-MLKNRLQSLE 596
Cdd:PRK01156 334 LQKDYNDYIKKKSR--------YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISeILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 597 AIEKDF--LKNKLNQDSGKsTTALHQENNKIKELSQEVERLKLKL--------------------------KDMKAIEDD 648
Cdd:PRK01156 406 AIKKELneINVKLQDISSK-VSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeksnhiinhynEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 649 LMKTEDEYETLERRYANERDKAQFLSKE------LEHVKMELAKYKLaEKTETSHEQWLFKRLQEEEAKSGHLSREVDAL 722
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEeinksiNEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 723 KEKIHEY---MATEDLIC--HLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYrhfSKSLRPSLNGRRISDPQVFS 797
Cdd:PRK01156 564 DSKRTSWlnaLAVISLIDieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS---IREIENEANNLNNKYNEIQE 640
|
490
....*....|....*....
gi 1915686534 798 KEVQTEAVDNEPPDYKSLI 816
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQI 659
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
507-726 |
1.22e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 507 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERddlKNKLKAEEEKGNDLLSRVN 586
Cdd:PRK05771 51 LLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEE---ISELENEIKELEQEIERLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 587 MLKN------RLQSLE-------AIEKDFLKNKLNQDSGKSTTALHQENNKI-------KELSQEVERLkLKLKDMKAIE 646
Cdd:PRK05771 128 PWGNfdldlsLLLGFKyvsvfvgTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEE-LKKLGFERLE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 647 -DDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEqwlfkrLQEEE-----AKSGHL----- 715
Cdd:PRK05771 207 lEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIE------LERAEalskfLKTDKTfaieg 280
|
250
....*....|....
gi 1915686534 716 ---SREVDALKEKI 726
Cdd:PRK05771 281 wvpEDRVKKLKELI 294
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
244-602 |
1.28e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 244 DEQQRLTAQLTLQRQKIQELTTNAKEThtkLALAEARVQEEEQKATRLEKELQTQTTKFHQDQD------------TIMA 311
Cdd:PRK10246 297 ERIQEQSAALAHTRQQIEEVNTRLQST---MALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwrAQFS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 312 KLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKaeeelQDIKEKISKgeygnagiMAEVEELRKRvldmegkdeeLIK 391
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTA-----DEVAAALAQ--------HAEQRPLRQR----------LVA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 392 MEEQCRDLNKRLERetlqskdfkleveklskrimalekLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKV---- 467
Cdd:PRK10246 431 LHGQIVPQQKRLAQ------------------------LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceq 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 468 --RIKELEAIESRLEK------------------TEFTLKEDLTKLKTLTvmfvDERKTMSEKLKKTEDKLQAASSQLQV 527
Cdd:PRK10246 487 eaRIKDLEAQRAQLQAgqpcplcgstshpaveayQALEPGVNQSRLDALE----KEVKKLGEEGAALRGQLDALTKQLQR 562
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915686534 528 EQNKVTTvtekLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEE--EKGNDLLSRVNMLKNRLQSLEAIEKDF 602
Cdd:PRK10246 563 DESEAQS----LRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEehERQLRLLSQRHELQGQIAAHNQQIIQY 635
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-576 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQIDELEETNRSLRKAEEE---LQDIKEKisKGEYGNAGIMAEVEELRKRVLDMEGKDEELIKMEEQCR 397
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQielLEPIREL--AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 398 DLNKRLERETLQSKDFKLEVEKLSKRimaLEKLEDAFNKSKQEcyslkcNLEkermttkQLSQELESLKVRIKELEAIES 477
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGD------RLE-------QLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 478 RLEKT----EFTL---KEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQnkvttvtEKLIEETKRALKSK 550
Cdd:COG4913 363 RLEALlaalGLPLpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL-------RELEAEIASLERRK 435
|
250 260
....*....|....*....|....*.
gi 1915686534 551 TDVEEKMYSVtkeRDDLKNKLKAEEE 576
Cdd:COG4913 436 SNIPARLLAL---RDALAEALGLDEA 458
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
486-724 |
1.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 486 LKEDLTKLKTLTVMfvderktmsEKLKKteDKLQAASSQLQVEQNKVTTVTEKL------IEETKRalKSKTDVEEKMYS 559
Cdd:PHA02562 155 LVEDLLDISVLSEM---------DKLNK--DKIRELNQQIQTLDMKIDHIQQQIktynknIEEQRK--KNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 560 VTKERDDLKNkLKAEEEKGNDLLSRVNM------------------LKNRLQSLEAIEKDFLKNklnQDSGKSTTALHQE 621
Cdd:PHA02562 222 YDELVEEAKT-IKAEIEELTDELLNLVMdiedpsaalnklntaaakIKSKIEQFQKVIKMYEKG---GVCPTCTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 622 NNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEY--------------ETLERRYANERDKAQFLSKELEHVKMELAKY 687
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqskkllelknkiSTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
250 260 270
....*....|....*....|....*....|....*..
gi 1915686534 688 KLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKE 724
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
200-610 |
2.30e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 200 CERLKKLIdQEIKSQEEKEQEKEKRVTTLKEELTKLKSFAlmvvDEQQRLTAQLTLQRQKIQELTTNAK------ETHTK 273
Cdd:pfam05622 89 CEELEKEV-LELQHRNEELTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKKLEDLGDLRRqvklleERNAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 274 LALAEARVQEEEQKATRLEKELQT---QTTKFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEE 350
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 351 L---QDIKEKISKGEYGNAGIMAEVEELRKRVLDMEGKdEELIKMEEQcrdlNKRL-ERETLQSKDfkleveklskRIMA 426
Cdd:pfam05622 244 LrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIR-EKLIRLQHE----NKMLrLGQEGSYRE----------RLTE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 427 LEKLEDAFNKSKQEcysLKCNLEKERMTTKQLSQELESLKvriKELEAIESRLEKTEfTLKEDLTKLKtltvmfvderkt 506
Cdd:pfam05622 309 LQQLLEDANRRKNE---LETQNRLANQRILELQQQVEELQ---KALQEQGSKAEDSS-LLKQKLEEHL------------ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 507 msEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTD----VEE--KMYsVTKERDDLKN-KLKAEEEKGN 579
Cdd:pfam05622 370 --EKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEdmkaMEEryKKY-VEKAKSVIKTlDPKQNPASPP 446
|
410 420 430
....*....|....*....|....*....|.
gi 1915686534 580 DLLSRVNMLKNRLQSLEAIEKDFLKNKLNQD 610
Cdd:pfam05622 447 EIQALKNQLLEKDKKIEHLERDFEKSKLQRE 477
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
257-479 |
2.34e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 257 RQKIQELTTNAKETHTKLALAEARVQEEEQkATRLEKELQTQTTKfHQDQDTIMAKLTNEDSQnRQLQQKLAALSRQIDE 336
Cdd:PRK04863 448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQ-AYQLVRKIAGEVSR-SEAWDVARELLRRLREQ-RHLAEQLQQLRMRLSE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 337 LEETNRSLRKAEEELQDIKEKISKGeYGNAgimAEVEELRkrvldmEGKDEELIKMEEQCRDLNKRLERETLQSKDFKLE 416
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKN-LDDE---DELEQLQ------EELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915686534 417 VEKLSKRIM-------ALEKLEDAFN---KSKQECYSLKCN-LEKERmttkQLSQELESLKVRIKELEAIESRL 479
Cdd:PRK04863 595 IQRLAARAPawlaaqdALARLREQSGeefEDSQDVTEYMQQlLERER----ELTVERDELAARKQALDEEIERL 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
148-365 |
2.35e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 148 EKHKESYRRILGQLLVAEKSRRQTILELEEEKRK---HKEYMEKSDEFICLLEQECERLKKLIDQEIKSQEEKEQEKEKR 224
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 225 VTTLKEELTKLKSFALMV----VDEQQRLTAQLTLQRQKIQELTTNAKETHTKLALAEARVQEEEQKATRLEKELQTQTT 300
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVlkarTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915686534 301 KFHQDQDTIMAKLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGN 365
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
507-671 |
2.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 507 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALKS-KTDVEEKMYSVTKERDDLKNKLKAEEEKGN------ 579
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKlQAEIAEAEAEIEERREELGERARALYRSGGsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 580 ---------DLLSRVNMLK----NRLQSLEAIEKDflKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIE 646
Cdd:COG3883 107 vllgsesfsDFLDRLSALSkiadADADLLEELKAD--KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|....*
gi 1915686534 647 DDLMKTEDEYETLERRYANERDKAQ 671
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
292-433 |
2.80e-03 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 41.08 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 292 EKELQTQ-TTKFHQDQDTIMAKLTNE-DSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISKGEYGNAGI- 368
Cdd:pfam14362 105 EKEIDRElLEIQQEEADAAKAQLAAAyRARLAELEAQIAALDAEIDAAEARLDALQAEARCELDGTPGTGTGVPGDGPVa 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 369 ---MAEVEELRKRVLDMEGK-DEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALEKLEDA 433
Cdd:pfam14362 185 ktkQAQLDAAQAELAALQAQnDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEALNRLTTE 253
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
247-352 |
3.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 247 QRLTAQLTLQRQKIQELTTNAKETH-------TKLALAEARVQEEEQKA-TRLEKELQTQTTKFHQDQDTImAKLTNEDS 318
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTPNHpdvialrAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQL-AQLEARLA 344
|
90 100 110
....*....|....*....|....*....|....
gi 1915686534 319 QNRQLQQKLAALSRQIDELEETNRSLRKAEEELQ 352
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
509-726 |
3.04e-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: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 509 EKLKKTEDKLQAASSQLQVEQNKvttvTEKLIEETKRALKsktDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNML 588
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLA---ALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 589 KNRLQSLEAIEKDFLKN-KLNQDSGKSTTALHQENnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANER 667
Cdd:COG4942 96 RAELEAQKEELAELLRAlYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915686534 668 DKAQFLSKELEHVKMELAKYKlAEKTETSHEqwLFKRLQEEEAKSGHLSREVDALKEKI 726
Cdd:COG4942 174 AELEALLAELEEERAALEALK-AERQKLLAR--LEKELAELAAELAELQQEAEELEALI 229
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
247-451 |
3.65e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 247 QRLTAQLTLQRQKIQELTTNAKETHTKLalaearvqeeeqkaTRLEKELQTQTTKFHQDQDTIMAKLTNEDSqnRQLQQK 326
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTALETLEKALKDLLTDEGG--AIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 327 LAALSRQIDELEETNrsLRKAEEELQDIKEKISKGEygnagimAEVEELRKRVLDMEgkdeeliKMEEQCRDLNkrlere 406
Cdd:cd22656 181 IKDLQKELEKLNEEY--AAKLKAKIDELKALIADDE-------AKLAAALRLIADLT-------AADTDLDNLL------ 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1915686534 407 tlqskdfklevEKLSKRIMALEKLEDAFNKSKQECYSLKCNLEKE 451
Cdd:cd22656 239 -----------ALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDD 272
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
273-725 |
3.85e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 273 KLALAEARVQEEEQKATRLEKELQTQTTKFHQDQdtimaKLTNEDSQNRQLQQKLAALSRQIDELEetnRSLRKAEEELQ 352
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN-----QLQPDPAKTKALQTVIEMKDTKISSLE---RNIRDLEDEVQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 353 DIKEKISKGEYGNAGIMAEVEELRKRVLDMEGK----DEELIKMEEQCRDLNKRLERETLQSKDFKLEVEKLSKRIMALE 428
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKidqlKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 429 KLEdafNKSKQECYSLKCNL-EKERM---TTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDER 504
Cdd:pfam10174 338 QRA---AILQTEVDALRLRLeEKESFlnkKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKD 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 505 KTMSEkLKKTEDKLQAASSQlqvEQNKVTTVTEKLIEETK--RALKSKTDVE-----EKMYSVTKERDDLKNKLKA---- 573
Cdd:pfam10174 415 KQLAG-LKERVKSLQTDSSN---TDTALTTLEEALSEKERiiERLKEQREREdrerlEELESLKKENKDLKEKVSAlqpe 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 574 ---EEEKGNDLLSRVNML-------KNRLQSLE-AIEKDF-----LKNKLN--QDSGKSTTALHQENNKIKELSQEV--- 632
Cdd:pfam10174 491 lteKESSLIDLKEHASSLassglkkDSKLKSLEiAVEQKKeecskLENQLKkaHNAEEAVRTNPEINDRIRLLEQEVary 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 633 -----------ERLKLKLKDMKAIEDDLMKTEDEYETLERR--------YANERDKAQFLSKELEHVKMELAKYKLAEKT 693
Cdd:pfam10174 571 keesgkaqaevERLLGILREVENEKNDKDKKIAELESLTLRqmkeqnkkVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
490 500 510
....*....|....*....|....*....|....*...
gi 1915686534 694 ETSHEQW------LFKRLQEEEAKSGHLSREVDALKEK 725
Cdd:pfam10174 651 NSQQLQLeelmgaLEKTRQELDATKARLSSTQQSLAEK 688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
624-775 |
3.96e-03 |
|
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: 41.59 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 624 KIKELSQEVERL---KLKLKDMKAIEDDLMKTEdEYETLERRYANERDKAQfLSKELEHVKMELAKY--KLAEKTETSHE 698
Cdd:TIGR02169 192 IIDEKRQQLERLrreREKAERYQALLKEKREYE-GYELLKEKEALERQKEA-IERQLASLEEELEKLteEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 699 qwLFKRLQEEEAKSGHL-SREVDALKEKIHEYMA----TEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 773
Cdd:TIGR02169 270 --IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
..
gi 1915686534 774 YR 775
Cdd:TIGR02169 348 ER 349
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
227-433 |
4.02e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 227 TLKEELTKLKSFALMVVDEQQRLTAQLT------LQRQKIQELTT------NAKETHTKLALAEARVQEEEQKATRLEKE 294
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEeleaaaLQPGEEEELEEerrrlsNAEKLREALQEALEALSGGEGGALDLLGQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 295 LQTQttkfhqdqdtiMAKLTNEDSQnrqLQQKLAALSRQIDELEETNRSLRKA-------EEELQDIKEKIS-----KGE 362
Cdd:COG0497 249 ALRA-----------LERLAEYDPS---LAELAERLESALIELEEAASELRRYldslefdPERLEEVEERLAllrrlARK 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915686534 363 YGN--AGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETlqskdfklevEKLSK-RIMALEKLEDA 433
Cdd:COG0497 315 YGVtvEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----------EKLSAaRKKAAKKLEKA 378
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
387-505 |
4.11e-03 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 39.89 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 387 EELIKMEEQCRDLNKRLERETLqskdfklEVEKLSKRimALEKLEDafNKSKQECYSLK-----CNLEKERmttKQLSQE 461
Cdd:pfam09727 80 AELEKLVEKQRETQRRMLEQLA-------AAEKRHRR--VIRELEE--EKRKHARDTAQgddftYLLEKER---ERLKQE 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1915686534 462 LESLKVRIKELEAiesRLEKTEFTLKEDLTKLKTLTVMFVDERK 505
Cdd:pfam09727 146 LEQEKAQQKRLEK---ELKKLLEKLEEELSKQKQIALLLVKERK 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
95-301 |
4.32e-03 |
|
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: 41.26 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 95 AEKMDLALLEAQYGFVTPKKVLEALQRDAFQAKSTPWQEdIYEKPMNELDKVVEKHKESYRRIlGQLLVAEKSRRQTILE 174
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 175 LEEEKRKHKEYMEKSDEficLLEQECERLKKLIDQEIKSQEEKEQEKEKRVTTLKEELTKLKSfalmvvdEQQRLTAQLT 254
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRK---ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-------EEERRKQQEM 548
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1915686534 255 LQRQKIQELTTNAKETHTKLALAEA------RVQEEEQKATRLEKELQTQTTK 301
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEReremmrQIVESEKARAEYEATTPITTIK 601
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
534-775 |
5.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 534 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiekdfLKNKLNQDSGK 613
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-----KRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 614 STTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANER----------DKAQFLSKELEHVKME 683
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekelvEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 684 LAKYKLAEKTETSHEQW------LFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRN 757
Cdd:COG1340 156 LEKNEKLKELRAELKELrkeaeeIHKKIKELAEEAQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADELHEEI 232
|
250
....*....|....*...
gi 1915686534 758 RDLGREIENLTKELERYR 775
Cdd:COG1340 233 IELQKELRELRKELKKLR 250
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
312-576 |
5.37e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 312 KLTNEDSQNRQLQQKLAALSRQIDELEETNRSLRKAEEELQDIKEKISkgeygnagimaeveELRKRVLDMEGKDEELIK 391
Cdd:pfam05911 567 DDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWIS--------------NHCFSLLDVSSMEDEIKK 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 392 MEeqCRDLNKRLERETLQSKDFKLEVEKLSK---------RIMALEKLEDAFNK-SKQECYSLKcnLEKERMTT--KQLS 459
Cdd:pfam05911 633 HD--CIDKVTLSENKVAQVDNGCSEIDNLSSdpeipsdgpLVSGSNDLKTEENKrLKEEFEQLK--SEKENLEVelASCT 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 460 QELESLKVRIKELEaiesrleKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKL 539
Cdd:pfam05911 709 ENLESTKSQLQESE-------QLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVEL 781
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1915686534 540 IEETK---RALKSKTDVEEKMYSVTKER------DDLKNKLKAEEE 576
Cdd:pfam05911 782 EEEKNcheELEAKCLELQEQLERNEKKEssncdaDQEDKKLQQEKE 827
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
372-669 |
5.40e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 372 VEELRKRVL----DMEGKDEELIKMEEqcrDLNKRLERETLQSKDFKLEVEK------LSKRI--MALEKLEdafnkskq 439
Cdd:PTZ00108 1037 VKELKKLGYvrfkDIIKKKSEKITAEE---EEGAEEDDEADDEDDEEELGAAvsydylLSMPIwsLTKEKVE-------- 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 440 ecyslkcNLEKERMTTKQLSQELESLKVR---IKELEAIESRLEKTEFTLKEDLTKLKTLTVM-FVDERKTMSEKLKKTE 515
Cdd:PTZ00108 1106 -------KLNAELEKKEKELEKLKNTTPKdmwLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKtKGKASKLRKPKLKKKE 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 516 DKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSL 595
Cdd:PTZ00108 1179 KKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDND 1258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915686534 596 EAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKD--MKAIEDDLMKTEDEYE--TLERRYANERDK 669
Cdd:PTZ00108 1259 EFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSptKKKVKKRLEGSLAALKkkKKSEKKTARKKK 1336
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
316-671 |
5.54e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 316 EDSQNRQLQQKLAALSRQIdeLEETNRSLRKAEEEL-QDIKEKISkgeygnagimAEVEELRKRVLDMEGKDEELIKMEE 394
Cdd:NF033838 82 KHTQNVALNKKLSDIKTEY--LYELNVLKEKSEAELtSKTKKELD----------AAFEQFKKDTLEPGKKVAEATKKVE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 395 QCRDLNKRLERE------TLQSKDFKLEVEKLSKRImalekledafNKSKQECYSLKCNLEKERMTTKQLSQELESLKVR 468
Cdd:NF033838 150 EAEKKAKDQKEEdrrnypTNTYKTLELEIAESDVEV----------KKAELELVKEEAKEPRDEEKIKQAKAKVESKKAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 469 IKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALK 548
Cdd:NF033838 220 ATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 549 SKTdvEEKMYSVTKERDDLKNKLKAEEEKgndllSRVNMLKNRLQSL--EAIEKDFLKNKLNQDSGKSTTALHQENNKIK 626
Cdd:NF033838 300 LKP--EKKVAEAEKKVEEAKKKAKDQKEE-----DRRNYPTNTYKTLelEIAESDVKVKEAELELVKEEAKEPRNEEKIK 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1915686534 627 ELSQEVERLKLKLKDMKAIEDDLMKTEDEyetlERRYANERDKAQ 671
Cdd:NF033838 373 QAKAKVESKKAEATRLEKIKTDRKKAEEE----AKRKAAEEDKVK 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
321-479 |
8.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 321 RQLQQKLAALSRQID----ELEETNRSLRKAEEELQDIKEKISKGEY--GNAG-------IMAEVEELRKRVLDMEgkDE 387
Cdd:COG1579 34 AELEDELAALEARLEaaktELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRnnkeyeaLQKEIESLKRRISDLE--DE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 388 ELIKMEeqcrdlnkrlERETLQSkdfklEVEKLSKRimaLEKLEDAFNKSKQEcyslkcnLEKErmtTKQLSQELESLKV 467
Cdd:COG1579 112 ILELME----------RIEELEE-----ELAELEAE---LAELEAELEEKKAE-------LDEE---LAELEAELEELEA 163
|
170
....*....|...
gi 1915686534 468 RIKELEA-IESRL 479
Cdd:COG1579 164 EREELAAkIPPEL 176
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
76-412 |
8.67e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 76 LSILEGELQARDEVIGILKAEKMDLALLEAQYGFVTPKKVLEALQRDAFQAKSTPWQEDIYEKPMNELDKVVEK----HK 151
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEklgeNA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 152 ESYRRILGQL------------LVAEKSRRQTILELEEEKRKHKEYMEKSDEFiclleqecERLKKLIDQEIKsqeEKEQ 219
Cdd:COG5185 275 ESSKRLNENAnnlikqfentkeKIAEYTKSIDIKKATESLEEQLAAAEAEQEL--------EESKRETETGIQ---NLTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 220 EKEKRVTTLKEELTKLKSFALMVVDEQQRLTAQLTLQ---------RQKIQELTTNAKETHTKLALA-EARVQEEEQKAT 289
Cdd:COG5185 344 EIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDsfkdtiestKESLDEIPQNQRGYAQEILATlEDTLKAADRQIE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 290 RLEKELQTQTTKFHQDQDTIMAkLTNEDSQNRQLQQKLaALSRQIDELEETNRSLR----KAEEELQDIKEKISKGEYGN 365
Cdd:COG5185 424 ELQRQIEQATSSNEEVSKLLNE-LISELNKVMREADEE-SQSRLEEAYDEINRSVRskkeDLNEELTQIESRVSTLKATL 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1915686534 366 AGIMAEVEELRKRVLDMEGKDEELIKMEEQCRDLNKRLERETLQSKD 412
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
247-377 |
9.36e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 247 QRLTAQLTLQRQKIQELTTNAKETHTKLALAEA---RVQ-----------EEEQKATRLEKELQTQTTKFHQDQdtimak 312
Cdd:PRK09039 63 AELADLLSLERQGNQDLQDSVANLRASLSAAEAersRLQallaelagagaAAEGRAGELAQELDSEKQVSARAL------ 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915686534 313 ltnedSQNRQLQQKLAALSRQIDELEEtnrSLRKAEEELQDIKEKISK-GEYGNAGIMAEVEELRK 377
Cdd:PRK09039 137 -----AQVELLNQQIAALRRQLAALEA---ALDASEKRDRESQAKIADlGRRLNVALAQRVQELNR 194
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
260-360 |
9.94e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915686534 260 IQELTTNAKETHTKLALAEARVQEeeqkATRLEKELQTQTTKFHQDQDTIMAKltnedsQNRQLQQKLAALSRQIDELEE 339
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKE----AEKLKEELEEKKEKLQEEEDKLLEE------AEKEAQQAIKEAKKEADEIIK 591
|
90 100
....*....|....*....|....*..
gi 1915686534 340 TNRSLRK------AEEELQDIKEKISK 360
Cdd:PRK00409 592 ELRQLQKggyasvKAHELIEARKRLNK 618
|
|
| |
