|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
35-876 |
1.75e-13 |
|
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: 74.77 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 35 EAENYQNTLQLEQEVRNQDRFIstLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQVDDLTSHNEHLCKELIKIDQLAEQ 114
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFY--LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 115 LEKEKNFVVDSANKELeeakidlicqqnniIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTleadkdHYKSEAQHLR 194
Cdd:pfam15921 164 MLEDSNTQIEQLRKMM--------------LSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 195 KMMRsrsksprrpsptargancdvellktttrdreELKCMLEKYERHLAEIQGNVKVLKSE-RDKIFLLYEQAQEEITRL 273
Cdd:pfam15921 224 KILR-------------------------------ELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 274 RREmmksckspksttaHAILRRVETERDVAftdlrrMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDEr 353
Cdd:pfam15921 273 ISE-------------HEVEITGLTEKASS------ARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 354 meqmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCL 433
Cdd:pfam15921 333 ---------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 434 DEK-------IDNFTRQNIAQREEISILGGTLNDLAKEKE---------------------CLQACLDKKSENIASLGES 485
Cdd:pfam15921 404 WDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiqgkneslekvsSLTAQLESTKEMLRKVVEE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 486 LAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAH---DNDNLQEQFAKAKQE 562
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 563 NQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKnilksEESENRQMMEQLRKANEDAEnwENKARQSEADNNTLKLELIT 642
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKK--DAKIRELEARVSDLELEKVK 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 643 AEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHK--SVVK---------MEEELQKVQFEKVSALADLSSTRELCI 711
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyEVLKrnfrnkseeMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 712 KLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqnleallvANRDKEYqsqiaLQEKESEIQLLK 791
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-------------ANKEKHF-----LKEEKNKLSQEL 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 792 EHLCLAENKMA----IQSRDVAQFRNVVTQLEADLDITKRQLG-----TERFERERA---------VQELRRQNYSSNay 853
Cdd:pfam15921 779 STVATEKNKMAgeleVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVrlklqhtldVKELQGPGYTSN-- 856
|
890 900
....*....|....*....|....
gi 1034616907 854 hmsSTMKPN-TKCHSPERAHHRSP 876
Cdd:pfam15921 857 ---SSMKPRlLQPASFTRTHSNVP 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-662 |
1.76e-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: 74.71 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 330 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 409
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 410 SD-------TQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASL 482
Cdd:TIGR02168 757 TEleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 483 GESLAMKEKTISGMKNIIAEMEQASRQCTEALivceqdvSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQE 562
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 563 NQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL-RKANEDAENWENKARQSEADNNTLKLELI 641
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340
....*....|....*....|.
gi 1034616907 642 TAEAEGNRLKEKVDSLNREVE 662
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
450-763 |
2.34e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 450 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLd 529
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 530 etndelaQIARERDilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMM 609
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 610 EQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHlnaersyksqistlhksvvkmEEEL 689
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---------------------LKKL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616907 690 QKVQFEKVSalADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLE 763
Cdd:TIGR02168 431 EEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-597 |
1.15e-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: 68.93 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 297 ETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 373
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 374 MKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI 453
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 454 LGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQASRQCTEAlivcEQDVSRMRRQLDETND 533
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEELSEELREL----ESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616907 534 ELAQIARERDILAHDNDNLQEQFA-KAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 597
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
525-792 |
6.66e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 525 RRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQkvqdtnlEVNKLKNILKSEESE 604
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------ELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 605 NRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVK 684
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 685 MEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEA 764
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260
....*....|....*....|....*...
gi 1034616907 765 LLVANRDKEYQSQIALQEKESEIQLLKE 792
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-847 |
7.59e-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: 66.23 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 219 ELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTT-----AHAIL 293
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 294 RRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTV 370
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 371 EKEMKSLAR-------------------KAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIM 431
Cdd:TIGR02168 406 EARLERLEDrrerlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 432 CLDEKID-------------NFTRQNIAQREEISILGGTLNDLAKEKECLQACLDK-----------KSENIA------- 480
Cdd:TIGR02168 486 QLQARLDslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvENLNAAkkaiafl 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 481 ---SLGESLAMKEKTISGMKNIIAEMEQASRQ--CTEALIVCEQDVSRMRR-------------QLDETNDELAQIARER 542
Cdd:TIGR02168 566 kqnELGRVTFLPLDSIKGTEIQGNDREILKNIegFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 543 DILAHDNDNLQEQFAKAKQENQALSKKLNdTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEnw 622
Cdd:TIGR02168 646 RIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-- 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 623 enkarQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALAD 702
Cdd:TIGR02168 723 -----ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 703 LSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQE 782
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616907 783 KESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 847
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-802 |
1.73e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 475 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQE 554
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 555 QFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNN 634
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 635 TLKLELITAEAEGNRLKEKVDSLNREVEQhlnaersyksqistLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLD 714
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 715 SSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqNLEALLVANRDkEYQSQIALQEK-ESEIQLLKEH 793
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN------LQERLSEEYSL-TLEEAEALENKiEDDEEEARRR 973
|
....*....
gi 1034616907 794 LCLAENKMA 802
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
525-844 |
4.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 525 RRQLDETNDELAQIArerDILAHDN---DNLQEQfAKAKQENQALSKKLNDTHNELndIKQKVQDTNLEVNKLKNILKSE 601
Cdd:TIGR02168 178 ERKLERTRENLDRLE---DILNELErqlKSLERQ-AEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 602 ESENRQMMEQLRKANEDAEnwENKARQSEADN--NTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLH 679
Cdd:TIGR02168 252 EEELEELTAELQELEEKLE--ELRLEVSELEEeiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 680 KSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISM 759
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 760 QNLEallvANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdVAQFRNVVTQLEAdLDITKRQLGTERFERERA 839
Cdd:TIGR02168 410 ERLE----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEE-LREELEEAEQALDAAERE 483
|
....*
gi 1034616907 840 VQELR 844
Cdd:TIGR02168 484 LAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-837 |
4.18e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 72 GLEEYVRKLLDSKEvvssqvdDLTSHNEHLCKELIKIDQLAEQL-----EKEKNFVVDSANKELEEAKIDLICQQNNIiv 146
Cdd:TIGR02169 164 GVAEFDRKKEKALE-------ELEEVEENIERLDLIIDEKRQQLerlrrEREKAERYQALLKEKREYEGYELLKEKEA-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 147 LEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRSRSKSPRRPsptargancdvelLKTTTR 226
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-------------IGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 227 DREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKsckspksttAHAILRRVETERDVAFTD 306
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---------LTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 307 LRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDE------RMEQMSN-MTLMKETISTVEKEMKSLAR 379
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEElqrlseELADLNAaIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 380 KAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLN 459
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 460 DLAKEKECLQACLD----KKSENIASLGESLA------MKEKTISGMK----NIIAEMEQASRQCTEA--------LIVC 517
Cdd:TIGR02169 529 QLGSVGERYATAIEvaagNRLNNVVVEDDAVAkeaielLKRRKAGRATflplNKMRDERRDLSILSEDgvigfavdLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 518 EQD--------------VSRMrrqldETNDELAQIAR----ERDIL--------AHDNDNLQEQFAKA-KQENQALSKKL 570
Cdd:TIGR02169 609 DPKyepafkyvfgdtlvVEDI-----EAARRLMGKYRmvtlEGELFeksgamtgGSRAPRGGILFSRSePAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 571 NDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRL 650
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 651 KEKVDSLNR---EVEQHLNA-ERSY-KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLV 725
Cdd:TIGR02169 764 EARIEELEEdlhKLEEALNDlEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 726 AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL------VANRDKEY-QSQIALQEKESEIQLLKEHLCLAE 798
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLrELERKIEELEAQIEKKRKRLSELK 923
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1034616907 799 NKMAIQSRDVAQFRNVVTQL----EADLDITKRQLGTERFERE 837
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-846 |
5.21e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 611 QLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQ 690
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 691 kvqfekvSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANR 770
Cdd:COG1196 313 -------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616907 771 DKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQ 846
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
373-702 |
2.41e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 373 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 452
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 453 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMkektiSGMKNIIAEMEQAsrqctealivcEQDVSRMRRQLDETN 532
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKL-----------EEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 533 DELAQIARERDILAHDNDNLQEQfakakqenqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL 612
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 613 RKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSqISTLHKSVVKMEEELQKV 692
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRV 963
|
330
....*....|
gi 1034616907 693 QfEKVSALAD 702
Cdd:TIGR02169 964 E-EEIRALEP 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-792 |
3.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 221 LKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmksckspksttahaiLRRVETER 300
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----------------LARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 301 DVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARK 380
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEE----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 381 AMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLND 460
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 461 LAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEA-LIVCEQDVSRMRRQLDETNDELAQIA 539
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 540 RERDILAHDNDNLQEQFAKAKQENQALSKKLNdthnelndikqkvQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDA 619
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------------RATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 620 ENWENKARQSEADnnTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSA 699
Cdd:COG1196 608 LREADARYYVLGD--TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 700 LADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQsqia 779
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---- 761
|
570
....*....|...
gi 1034616907 780 LQEKESEIQLLKE 792
Cdd:COG1196 762 LEELERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-845 |
3.63e-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: 57.37 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 230 ELKCMLEKYERHLAEIQgnVKVLKSERDKIFLLYEQAQEEITRLRREMmksckspksttahailrrveTERDVAFTDLRR 309
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAEL--------------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 310 MTTERDSLRERLKIAQETAFNEKAHLEQRIEELectvhnldDERMEQmsnmtlmketistVEKEMKSLARKAMDTESELG 389
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQIL--------RERLAN-------------LERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 390 RQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQ 469
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 470 ACLDKKSENIASLGESLAMKEK-----TISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 544
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 545 LAHDNDNLQEQFAKAKQENQALSkKLNDTHNELNDI------------------KQKVQDTNLE-VNKLKNILKSEESEN 605
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQS-GLSGILGVLSELisvdegyeaaieaalggrLQAVVVENLNaAKKAIAFLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 606 RQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAE--------------------AEGNRLKEKVDSLNREV---- 661
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 662 -------------EQHLNAERSYKSQISTLHKSVVKMEEELQkvqfEKVSALADLSSTRELcikLDSSKELLNRQLVAKD 728
Cdd:TIGR02168 653 dlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIA----ELEKALAELRKELEE---LEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 729 QEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDV 808
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034616907 809 AQFRNVVTQLEADLDITKRQLGTERFERERAVQELRR 845
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
448-732 |
9.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 448 REEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISgmkniiaEMEQASRQCTEALIVCEQDVSRMRRQ 527
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 528 LDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDtnlEVNKLKNILKSEESENRQ 607
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 608 MMEQLRKANEDaenwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEE 687
Cdd:COG1196 388 LLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034616907 688 ELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 732
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-829 |
7.69e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 242 LAEIQGNVKVLKSERDKiFLLYEQAQEEITRLRREMM----KSCKSpKSTTAHAILRRVETERDVAFTDLRRMTTERDSL 317
Cdd:COG1196 195 LGELERQLEPLERQAEK-AERYRELKEELKELEAELLllklRELEA-ELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 318 RERLKIAQEtAFNEK----AHLEQRIEELEcTVHNLDDERMEQmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKA 393
Cdd:COG1196 273 RLELEELEL-ELEEAqaeeYELLAELARLE-QDIARLEERRRE------LEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 394 ENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLD 473
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 474 KKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDIL--AHDNDN 551
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLleAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 552 LQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN--WENKARQ 628
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 629 SEADNNTLKLELITAEAEG-NRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTR 707
Cdd:COG1196 585 RAALAAALARGAIGAAVDLvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 708 ELCIKLDSSKELLNRQLVAKDQEIEMRENELdsahsEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEI 787
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELEL-----EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1034616907 788 QLLKEHLCLAENKMAIQSRDVaqfrnVVTQLEADLDITKRQL 829
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPP-----DLEELERELERLEREI 776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-632 |
2.44e-06 |
|
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: 50.92 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 403 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKK 475
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 476 SENIASLgeslamkektisgmkniIAEMEQASRQCTEALIVCEQDVSRMRRQLdetnDELAQIARERDILAHDNDNLQEQ 555
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616907 556 FAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEAD 632
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
107-692 |
2.73e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 107 KIDQLAEQLEKEKNfvvDSANKELEEAKID--LICQQNNIIVLEDTIKRLKSII------LDTEKAQ----NKSPSRLDS 174
Cdd:TIGR04523 34 EEKQLEKKLKTIKN---ELKNKEKELKNLDknLNKDEEKINNSNNKIKILEQQIkdlndkLKKNKDKinklNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 175 FVKTLEADKDHYKSEAQHLRKMMRSRSKSPRRPSPTARGANCDVELL----KTTTRDREELKCMLEKYERHLAEIQGNVK 250
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 251 VLKSERDKIFLLY---EQAQEEITRLRREMMKSCKSPKSTTAHAILRRVE-----TERDVAFTDLRRMTTERDSLRERLK 322
Cdd:TIGR04523 191 KIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEinektTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 323 IAQ---ETAFNEKAHLEQRIEELECTVHNLDDERMEQMSN------------MTLMKETISTVEKEMKSLARKAMDTESE 387
Cdd:TIGR04523 271 EKQkelEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKelkselknqekkLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 388 LGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKEC 467
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 468 LQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAH 547
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 548 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQdtNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN----WE 623
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeeKQ 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616907 624 NKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKV 692
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-614 |
4.99e-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: 50.45 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 264 EQAQEEITRLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 340
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 341 ELECTVHNLDD-----ERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRqkaennslrllyentekdlsdtqrh 415
Cdd:TIGR02169 769 ELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR------------------------- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 416 lakKKYELQLtqekimcLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG 495
Cdd:TIGR02169 824 ---LTLEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 496 MKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE--RDILAHDNDNLQEQFAKAKQENQALSKKLNDT 573
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034616907 574 HNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRK 614
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
228-836 |
1.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 228 REELKCMLEKYERHLAEIQgnvkVLKSERDKIfllyeqaQEEITrlrremmksckspksttahailrRVETERDVAFTDL 307
Cdd:PRK02224 236 RDEADEVLEEHEERREELE----TLEAEIEDL-------RETIA-----------------------ETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 308 RRMTTERDSLRERLKIAQETAFNEKAH---LEQRIEELECTVHNLDDERMEQmsnmtlmKETISTVEKEMKSLARKAMDT 384
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELRDRLEEC-------RVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 385 ESELGRQKAENNSLrllyentEKDLSDTQRHLAKKKYELQltqekimcldekidnftrqniAQREEISILGGTLNDLAKE 464
Cdd:PRK02224 355 EERAEELREEAAEL-------ESELEEAREAVEDRREEIE---------------------ELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 465 KECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQ--ASRQCTEalivCEQDV--SRMRRQLDETNDELAQIAR 540
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPE----CGQPVegSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 541 ERDILAHDNDNLQEQFAKAKQenqalskkLNDTHNELNDIKQKVQDtnleVNKLKNILKSEESENRQMMEQLRkanEDAE 620
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERRED----LEELIAERRETIEEKRERAEELR---ERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 621 NWENKARQSEADNNtlkleliTAEAEGNRLKEKVDSLNREVEQhLNAERSYKSQISTLHKSVVKMEEELQKVQfEKVSAL 700
Cdd:PRK02224 548 ELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLR-EKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 701 ADLSstrelciklDSSKELLnrqlvakdQEIEMRENELDSAHSE--IELLRSQMANERISMQNLEALLVANRDKEYQSQI 778
Cdd:PRK02224 619 AELN---------DERRERL--------AEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616907 779 ALQEKESEIQ----LLKEHLCLAENKMAIQS--RDVAQFRNVVTQLEADLditkRQLGTERFER 836
Cdd:PRK02224 682 EIGAVENELEeleeLRERREALENRVEALEAlyDEAEELESMYGDLRAEL----RQRNVETLER 741
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
518-688 |
1.47e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 518 EQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 597
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 598 LKSEE---------------SENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEK----VDSLN 658
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLS 188
|
170 180 190
....*....|....*....|....*....|
gi 1034616907 659 REVEQHLNAERSYKSQISTLHKSVVKMEEE 688
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
337-759 |
5.37e-05 |
|
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: 46.94 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 337 QRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 416
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 417 AKKKYELQLTQEKIM---CLDEKIDNFTRQNI--------------AQREEISILGGTLNDLAKEKECLQACLDKKSENI 479
Cdd:TIGR04523 197 LKLELLLSNLKKKIQknkSLESQISELKKQNNqlkdniekkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 480 ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIvcEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKA 559
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL--KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 560 KQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLE 639
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 640 LITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKEL 719
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034616907 720 LNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISM 759
Cdd:TIGR04523 515 LTKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
293-627 |
5.65e-05 |
|
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: 46.94 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 293 LRRVETERDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEK 372
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 373 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 452
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 453 ILGGTLNDLAKEKECLQACLDKKSENI--ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLdE 530
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 531 TNDELAqiarerdilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMME 610
Cdd:TIGR04523 607 EKEKKI-------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
330
....*....|....*..
gi 1034616907 611 QLRKANEDAENWENKAR 627
Cdd:TIGR04523 674 KIDDIIELMKDWLKELS 690
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-443 |
5.85e-05 |
|
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: 46.97 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 40 QNTLQLEQEVRNQDRFISTLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQVDDLTSHNEHLCKELIKIDQLAEQLEKEk 119
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 120 nfvVDSANKELEEAKIDLICQQNNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRS 199
Cdd:TIGR02168 749 ---IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 200 RSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmk 279
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE--- 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 280 sckspksttahaiLRRVETERdvaftdlRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQMSn 359
Cdd:TIGR02168 903 -------------LRELESKR-------SELRRELEELREKL-----------AQLELRLEGLEVRIDNLQERLSEEYS- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 360 mtLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDN 439
Cdd:TIGR02168 951 --LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
....
gi 1034616907 440 FTRQ 443
Cdd:TIGR02168 1029 EARE 1032
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
429-635 |
6.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 429 KIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG----MKNIIAEME 504
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 505 QASRQCTEALIVCEQD--------VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNE 576
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616907 577 LNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNT 635
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
446-646 |
6.54e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 446 AQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMR 525
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 526 RQLDETNDELA-------------------------QIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDI 580
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616907 581 KQKVQdtnlEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAE 646
Cdd:COG4942 177 EALLA----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
527-730 |
8.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 527 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS------ 600
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 601 EESENRQMMEQLRKANEDAE---NWENKARQSEADNNTLKlELITAEAEGNRLKEKVDSLNREVEQHL----NAERSYKS 673
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKaeleAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616907 674 QISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQE 730
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
319-838 |
1.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 319 ERLKIAQETAFNEKAHLEQRIEELEctvhnlddERMEQMSNMtlmKETISTVEKEMKSLARKAMDTESELGRQKAENNSL 398
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLE--------KFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 399 RLLYENTEKdlsdTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDL------AKEKECLQACL 472
Cdd:PRK03918 227 EKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 473 DKKSENIASLGESLAMKEKTISGMKNIIAEMEQasrqctealivceqdvsrMRRQLDETNDELAQIARERDILAHDNDNL 552
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 553 QEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANE--------------- 617
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgre 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 618 -DAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVdslnREVEQHLNAERSYKSQISTLhKSVVKMEEELQKVQFEK 696
Cdd:PRK03918 445 lTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL----RELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 697 VSALA-DLSSTRELCIKLDSSKELLNRQLVAKDQ---EIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDK 772
Cdd:PRK03918 520 LEKKAeEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616907 773 EYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERER 838
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
226-847 |
1.69e-04 |
|
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: 45.44 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 226 RDREELKCMLEKYERHLAEIQGNVKVLKSERDKIfLLYEQAQEEitrlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 305
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 306 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------SNMTLMKETISTVEKEMKSL 377
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 378 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGT 457
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 458 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QCTEALIVCEQDVSRMRRQLDE 530
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 531 TNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHN---ELNDIKQKVQdTNLEV---NKLKNILKSEESE 604
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGtvaQLGSVGERYA-TAIEVaagNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 605 NRQMMEQLRKANEDAENW--ENKARQSEADNNTLK--------LELITAE--------------------AEGNRLKEKV 654
Cdd:TIGR02169 560 AKEAIELLKRRKAGRATFlpLNKMRDERRDLSILSedgvigfaVDLVEFDpkyepafkyvfgdtlvvediEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 655 DSLNREVEQH---------LNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLV 725
Cdd:TIGR02169 640 RMVTLEGELFeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 726 AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHlcLAENKMAIQS 805
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQ 797
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1034616907 806 RDVAQFRNVVTQLEADLDITKRQLGTERFER---ERAVQELRRQN 847
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQR 842
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
651-779 |
1.81e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 651 KEKV-DSLNREVEQ---HLNAERSYKSQistlhksvvkMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVA 726
Cdd:PRK09039 51 KDSAlDRLNSQIAEladLLSLERQGNQD----------LQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034616907 727 KDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVA--NRDKEYQSQIA 779
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDAseKRDRESQAKIA 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
603-838 |
3.54e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 603 SENRQMMEQLRKANEDAENWENKARQSEADnntLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 682
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 683 VKMEEELQKVqfekVSALADLSSTRELCIKLDS-SKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQN 761
Cdd:COG4942 100 EAQKEELAEL----LRALYRLGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616907 762 LEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERER 838
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
526-754 |
4.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 526 RQLDETNDELAQIARERDILAHDNDnLQEQFAKAKQEnqalskklndtHNELNDIKQKVQdtnLEVNKLKNILKSEESEN 605
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE-LAERYAAARER-----------LAELEYLRAALR---LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 606 RQmmEQLRKANEDAEnwENKARQSEADNNTLKLELITAEAEGNR---LKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 682
Cdd:COG4913 300 LR--AELARLEAELE--RLEARLDALREELDELEAQIRGNGGDRleqLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034616907 683 VKMEEELQKVQFEKVSALADLSSTRElcikldsskELLNRQLVAKDQEIEMREnELDSAHSEIELLRSQMAN 754
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELE---------ALEEALAEAEAALRDLRR-ELRELEAEIASLERRKSN 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-328 |
5.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 107 KIDQLAEQLEKEKNfVVDSANKELEEAKIDLICQQNNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHY 186
Cdd:COG4942 21 AAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 187 KSEAQHLRKMMRSRSKSPRRPSPT-------ARGANCDVELLKTTTRDREELkcmLEKYERHLAEIQGNVKVLKSERDKI 259
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQ---AEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616907 260 FLLYEQAQEEITRLRREMmksckspksTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETA 328
Cdd:COG4942 177 EALLAELEEERAALEALK---------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
564-766 |
5.71e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 564 QALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITA 643
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 644 EAEGNRLKEKVDSLNREVEQH---------LNAERSYKSQ-----ISTLHKSVVKMEEELQKVQFEKVSALADLSSTREl 709
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616907 710 ciKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 766
Cdd:COG4942 175 --ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
363-665 |
6.94e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 363 MKETISTVEKEMKSLARKAMDTESELG-------RQKAENNSLRLLYENTEKDL---SDTQRHLAKK-----KYELQLTQ 427
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVqangeleKASREETFARTALKNARLDLrrlFDEKQSEKDKknkalAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 428 EKIMCLDEKIDNFTRQNIAQREEISilgGTLNDLAKEK-ECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQA 506
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQK---EQKREARTEKqAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 507 SRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAkakQENQALSKKLNDTHNELNDIKQ---- 582
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlar 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 583 KVQDTNLEVNKLKNILKSEESENRQMMEQLRKAnedaenwenKARQS-------EADNNTLKLELITAEAEGNRLKEKVD 655
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGL---------RCEMSklatlkeDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330
....*....|
gi 1034616907 656 SLNREVEQHL 665
Cdd:pfam12128 904 YLSESVKKYV 913
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
319-844 |
1.04e-03 |
|
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: 42.79 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 319 ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSlarkAMDTESELGRQKAENnsl 398
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA----TTCSLEELLRTEQQR--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 399 rllYENTEKDLSDTQRHLAKKKYELqltqekimcldEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 478
Cdd:pfam05483 372 ---LEKNEDQLKIITMELQKKSSEL-----------EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 479 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTealivceQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAK 558
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL-------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 559 AKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLR-KANEDAENwenkARQSEADNNTLK 637
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEEN----ARSIEYEVLKKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 638 LELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSK 717
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 718 ELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQnleallvanRDKEYQSQIALQEKESEIQLLKehlcla 797
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM---------EKHKHQYDKIIEERDSELGLYK------ 731
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034616907 798 eNKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELR 844
Cdd:pfam05483 732 -NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-541 |
1.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 330 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 409
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 410 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 478
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616907 479 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE 541
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
307-569 |
1.17e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 307 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEE---LECTVHNLDDERMEQMSNMTLMKETIS--TVEKEMKSLARKA 381
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktsLSASVASLEKQLLELTRVNELLKAKFSedGTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 382 MDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQREEIsilgGTLNDL 461
Cdd:pfam15905 162 MKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEEKSET----EKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 462 AKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEalivceqDVSRMRRQLDETNDELAQIARE 541
Cdd:pfam15905 228 ITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKLLESEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 1034616907 542 RDI-LAHDNDNLQEQFAKAKQENQALSKK 569
Cdd:pfam15905 301 KEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
307-662 |
1.60e-03 |
|
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: 42.27 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 307 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmsnmtlmketISTVEKEMKSLARKAMDTES 386
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 387 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKE 466
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 467 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILA 546
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 547 HDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKA 626
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034616907 627 RQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 662
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
672-846 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 672 KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQ 751
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 752 MAN-----ERISMQNLEALLV-------ANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdvaqfRNVVTQLE 819
Cdd:COG4942 106 LAEllralYRLGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE-----RAELEALL 180
|
170 180
....*....|....*....|....*..
gi 1034616907 820 ADLDITKRQLGTERFERERAVQELRRQ 846
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKE 207
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
37-774 |
3.28e-03 |
|
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: 41.58 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 37 ENYQNTLQLEQEVRN----------QDRFISTLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQ---VDDLTSHNEHLCK 103
Cdd:TIGR01612 569 EENEDSIHLEKEIKDlfdkyleiddEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNnayIDELAKISPYQVP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 104 ELIK-IDQLAEQLEKEKNFV----VDSANKELEEakidlICQQNNIIVLEDTIK--RLKSIILDT-EKAQNKSPSRLDSF 175
Cdd:TIGR01612 649 EHLKnKDKIYSTIKSELSKIyeddIDALYNELSS-----IVKENAIDNTEDKAKldDLKSKIDKEyDKIQNMETATVELH 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 176 VKTLEADKDHYKSEAQHLRKMMRSRSKspRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEI------QGNV 249
Cdd:TIGR01612 724 LSNIENKKNELLDIIVEIKKHIHGEIN--KDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIknhyndQINI 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 250 KVLKSERDKifLLYEQAQEEITRLrremmksckSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKiAQETAF 329
Cdd:TIGR01612 802 DNIKDEDAK--QNYDKSKEYIKTI---------SIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKID-SEHEQF 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 330 NE---KAHLEQRIEELECTVHNLDDERmeqmsnmTLMKETISTVEKEMKSL-ARKAMDTESELGRQKAEN-----NSLRL 400
Cdd:TIGR01612 870 AEltnKIKAEISDDKLNDYEKKFNDSK-------SLINEINKSIEEEYQNInTLKKVDEYIKICENTKESiekfhNKQNI 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 401 LYENTEKDLSDTQR-HLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISilggtlNDLAKEKECLQACLDKKSENI 479
Cdd:TIGR01612 943 LKEILNKNIDTIKEsNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKN------NELIKYFNDLKANLGKNKENM 1016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 480 asLGESLAMKEKTISgmkNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDEtndelaQIARERDILahdndnlqeqfaka 559
Cdd:TIGR01612 1017 --LYHQFDEKEKATN---DIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEK------EIGKNIELL-------------- 1071
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 560 kqeNQALSKKLNDTHNELNDIKQKVQDTNL-------------EVNKLKNILKSEESENRQMMEQLRKANEDAENWENka 626
Cdd:TIGR01612 1072 ---NKEILEEAEINITNFNEIKEKLKHYNFddfgkeenikyadEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYID-- 1146
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 627 rqsEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEElqKVQFEKVSALaDLSST 706
Cdd:TIGR01612 1147 ---EIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD--KTSLEEVKGI-NLSYG 1220
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616907 707 RELCI----KLDSSKELLNRQLVAKDQEIEmrenELDSAHSEIELLRSQMANERISMQNLEALLVAN-RDKEY 774
Cdd:TIGR01612 1221 KNLGKlfleKIDEEKKKSEHMIKAMEAYIE----DLDEIKEKSPEIENEMGIEMDIKAEMETFNISHdDDKDH 1289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
521-844 |
4.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 521 VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS 600
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 601 EESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQisTLHK 680
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 681 SVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQ 760
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 761 NLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAV 840
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
....
gi 1034616907 841 QELR 844
Cdd:COG4372 344 QLLL 347
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
527-787 |
4.19e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 527 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENR 606
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 607 QMMEQLRKANEdaenWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKME 686
Cdd:PRK01156 243 ELSSLEDMKNR----YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 687 EELQKVQfEKVSALADLSSTRELCIKLDSSKELLNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 766
Cdd:PRK01156 319 AEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQI----LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260
....*....|....*....|.
gi 1034616907 767 VANRDKEYQSQIALQEKESEI 787
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEI 414
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-631 |
5.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 37 ENYQNTLQLEQEVRnqdRFISTLKLQIEDLKQTNHGLEEYVRKLLDSKEVVSSQVDDLTSHNEHLCKELIKIDQLAEQLE 116
Cdd:PRK03918 158 DDYENAYKNLGEVI---KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 117 KEKNfvvdsankELEEAKIDLICQQNNIIVLEDTIKRLKSIILDTEKAQNKspsrLDSFVKTLEADKDhYKSEAQHLRKM 196
Cdd:PRK03918 235 ELKE--------EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE----LEEKVKELKELKE-KAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 197 MRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKsERDKIFLLYEQAQEEITRLRRE 276
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 277 mmKSCKSPKSttAHAILRRVETERDVAFTDLRRMTTERDSLRerlkiaqetafNEKAHLEQRIEELE--------CTVHN 348
Cdd:PRK03918 381 --LTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELK-----------KEIKELKKAIEELKkakgkcpvCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 349 LDDERMEQMSNMTLmkeTISTVEKEMKSLARKAMDTESELGR-QKAENNSLRLLyenTEKDLSDTQRHLAKKKYELQLtq 427
Cdd:PRK03918 446 TEEHRKELLEEYTA---ELKRIEKELKEIEEKERKLRKELRElEKVLKKESELI---KLKELAEQLKELEEKLKKYNL-- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 428 EKIMCLDEKIDNFTRQNIAQREEISILGGTL---NDLAKEKECLQACLDKKSENIASL-GESLAMKEKTISGMKNIIAEM 503
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 504 EQASRQCTEA-------------LIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDnlQEQFAKAKQENQALSKKL 570
Cdd:PRK03918 598 EPFYNEYLELkdaekelereekeLKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSREL 675
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034616907 571 NDTHNELNDIKQKVQDTNLEVNKLKNILKsEESENRQMMEQLRKANEDAENWENKARQSEA 631
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKYKA 735
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
548-621 |
5.34e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 5.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616907 548 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN 621
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK 350
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
306-725 |
7.62e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 306 DLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMD-T 384
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvT 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 385 ESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKE 464
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 465 KECLqacldkkSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 544
Cdd:TIGR00606 873 KLQI-------GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 545 LAHDNDNLQ------EQFAKAKQENQALSKK--LNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKAN 616
Cdd:TIGR00606 946 IKEKVKNIHgymkdiENKIQDGKDDYLKQKEteLNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 617 EDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVvkMEEELQKVQFEK 696
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL--REPQFRDAEEKY 1103
|
410 420
....*....|....*....|....*....
gi 1034616907 697 VSALADLSSTRELCIKLDSSKELLNRQLV 725
Cdd:TIGR00606 1104 REMMIVMRTTELVNKDLDIYYKTLDQAIM 1132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-847 |
7.62e-03 |
|
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: 40.04 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 630 EADNNTLKLELITAEaegnrLKEKVDSLNREVEQhlnAER--SYKSQISTLHKSVVKME-----EELQKVQFEKVSALAD 702
Cdd:TIGR02168 183 RTRENLDRLEDILNE-----LERQLKSLERQAEK---AERykELKAELRELELALLVLRleelrEELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 703 LSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQE 782
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616907 783 KESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 847
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-447 |
8.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 219 ELLKTTTRDREELKCMLEKYERHlAEIQGNVKVLKSERDKI-----FLLYEQAQEEITRLRREmmksckspksttahaiL 293
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAE----------------L 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 294 RRVETERDVAFTDLRRMTTERDSLRERLkiaQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 373
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616907 374 MKSLARKAMDTESELGRQKAEnnsLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFtRQNIAQ 447
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAE 451
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
335-693 |
8.94e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 335 LEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVE-------KEMKSLARKAMDTESELGRQKAENNSLRLLYENTEK 407
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEdqnsklsKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 408 DLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLndlAKEKECLQACLDKKSENIASLGESLa 487
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQKNNAL- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 488 mkeKTISGMKNIIAEME-----------QASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQF 556
Cdd:pfam01576 264 ---KKIRELEAQISELQedleseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616907 557 AKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILkseESENRQMMEQLRKANEDAENWENKARQSEADNNTL 636
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL---ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616907 637 KLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQ 693
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
|
| |
