|
Name |
Accession |
Description |
Interval |
E-value |
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
54-661 |
0e+00 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 664.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 54 RAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQ 133
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 134 CQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQA 213
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 214 SQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLREESA-LREMRETNGLLQEELEGLQRKLGRQ 292
Cdd:pfam05557 161 QQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKhLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 293 EKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEEL 372
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 373 RQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEME 452
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 453 AQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSflFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQG 532
Cdd:pfam05557 401 AQLSVAEEELGGYKQQAQTLERELQALRQQESLADPS--YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 533 DYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMErggtvpADLEAAAASLPSS-----KEVAELKKQV 607
Cdd:pfam05557 479 DYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE------DDLEQVLRLPETTstmnfKEVLDLRKEL 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2947031 608 ESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDC 661
Cdd:pfam05557 553 ESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYAEHPDDY 606
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-617 |
5.77e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVEREKMQMELShkRARVELERAAstsarnyerevDRNQELLTRIRQLQEREAGAEEKMQEQLE 129
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELE--ELRLELEELE-----------LELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 130 RNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQwsvMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQ 209
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 210 ELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELvRLPRLERELEQLREESALREMRETNGLLQEELEGLQRKL 289
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL-EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 290 GRQEKMQETLVGLELENERLLAKLQSWERLDQTMglsIRTPEDLSRFVVELQQreLALKDKNSAVTSSARGLEKARQQLQ 369
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEA---EADYEGFLEGVKAALL--LAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 370 EELRQVSGQLLeerkkretHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQkvhSHSA 449
Cdd:COG1196 541 EAALAAALQNI--------VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA---SDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 450 EMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRA 529
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 530 LQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLR--AMERGGTVPADLEAAAASLPSSKEVAELKKQV 607
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREelLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
570
....*....|
gi 2947031 608 ESAELKNQRL 617
Cdd:COG1196 770 ERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-630 |
4.54e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRA-RVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKM 124
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAeLEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 125 QEQLERNRQCQQNLDAASKRLREKEdsLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEA 204
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 205 NQKIQELQASQEARADHEQQIKDLEQKLS--------LQEQ-------------------DAAIVKNMKSELVRLPRLER 257
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELisvdegyeaaieaalggrlQAVVVENLNAAKKAIAFLKQ 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 258 ELEQLREESALREMRET--NGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDlSR 335
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPG-YR 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 336 FVV-------------------------------ELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERK 384
Cdd:TIGR02168 647 IVTldgdlvrpggvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 385 KRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGG 464
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 465 QKQRADMLEMEL--------------KMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLE---- 526
Cdd:TIGR02168 801 LREALDELRAELtllneeaanlrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEalln 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 527 --------RRALQGDYDQSRTKVLHMSLNPTSV--ARQRLREDHSQLQAECERLRGLL-----RAMERGGTVPADLEAAA 591
Cdd:TIGR02168 881 erasleeaLALLRSELEELSEELRELESKRSELrrELEELREKLAQLELRLEGLEVRIdnlqeRLSEEYSLTLEEAEALE 960
|
650 660 670
....*....|....*....|....*....|....*....
gi 2947031 592 ASLPSskEVAELKKQVESAELKNQRLKEVFQTKIQEFRK 630
Cdd:TIGR02168 961 NKIED--DEEEARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-616 |
2.88e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 94 RNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEdslaqagetinALKGRISELQWSV 173
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-----------ELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 174 MDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIK---DLEQKLSLQEQDAAIVKNMKSELV 250
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 251 RLprlereleqlreESALREMRETNGLLQEELEGLQRKLGRQEKMQETLvglelenERLLAKLQSWERLDQTmgLSIRTP 330
Cdd:PRK03918 328 ER------------IKELEEKEERLEELKKKLKELEKRLEELEERHELY-------EEAKAKKEELERLKKR--LTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 331 EDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQ---EELRQVSG-------QLLEERKKR--ETHEALARRLQK 398
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGkcpvcgrELTEEHRKEllEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 399 RVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEmeaQLSQALEELGGQKQRADMLEMELKM 478
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 479 LKSQSSSAEQsflfsreeadtLRLKVEELEGERSRLEEEKRMLEAQLERRALQG-DYDQSRTKvlhmSLNPTSVARQRLR 557
Cdd:PRK03918 544 LKKELEKLEE-----------LKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLK----ELEPFYNEYLELK 608
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2947031 558 EDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLpsSKEVAELKKQVESAELKNQR 616
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL--RKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-626 |
6.89e-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: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 346 ALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAE 425
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 426 YSP-QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKV 504
Cdd:TIGR02168 316 RQLeELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 505 EELEGERSRLEEEKRMLEAQLER-----RALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMER 579
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2947031 580 GGTVPADLEAAAASlpsskEVAELKKQVESAELKNQRLKEVFQTKIQ 626
Cdd:TIGR02168 476 ALDAAERELAQLQA-----RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-415 |
1.44e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 100 VDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMR 179
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 180 VKRLESEKQDVQEQLDLQHKKCQEANQKIQELQA-SQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLprlere 258
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEkLEELKEELESLEAELEELEAELEELESRLEELEEQLETL------ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 259 leqlreESALREMRETNGLLQEELEGLQRKLGRQEKMQETlvgLELENERLLAKLQSWERLDQTMGLsirtpEDLSRFVV 338
Cdd:TIGR02168 385 ------RSKVAQLELQIASLNNEIERLEARLERLEDRRER---LQQEIEELLKKLEEAELKELQAEL-----EELEEELE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2947031 339 ELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEAlarrLQKRVLLLTKERDGMRAILG 415
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGILG 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-523 |
5.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARN-YEREVDRNQELLTRIRQLQEREAGAEEKM 124
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeLEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 125 QEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEK-------QDVQEQLDLQ 197
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeeeealEEAAEEEAEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 198 HKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQ-----------EQDAAIVKNMK------------SELVRLPR 254
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllleaeadyEGFLEGVKAALllaglrglagavAVLIGVEA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 255 LERELEQLREESALRE-MRETNGLLQEELEGL-QRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPED 332
Cdd:COG1196 535 AYEAALEAALAAALQNiVVEDDEVAAAAIEYLkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 333 LSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERdgmra 412
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA----- 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 413 ilgsydseltpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLf 492
Cdd:COG1196 690 ----------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA- 752
|
490 500 510
....*....|....*....|....*....|.
gi 2947031 493 srEEADTLRLKVEELEGERSRLEEEKRMLEA 523
Cdd:COG1196 753 --LEELPEPPDLEELERELERLEREIEALGP 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-526 |
3.37e-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: 60.84 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 136 QNLDAA---SKRLREKEDSLAQAGETIN---ALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQ 209
Cdd:TIGR02168 629 DDLDNAlelAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 210 ELqasQEARADHEQQIKDLEQKLSLQEQDAAIVKNmkselvrlprlerelEQLREESALREMRETNGLLQEELEGLQRKL 289
Cdd:TIGR02168 709 EL---EEELEQLRKELEELSRQISALRKDLARLEA---------------EVEQLEERIAQLSKELTELEAEIEELEERL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 290 grqEKMQETLVGLELENERLLAKLqswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQ 369
Cdd:TIGR02168 771 ---EEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 370 EELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVHSHSA 449
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE------ELSEELRELESKRSELRRELE 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 450 EMEAQLSQALEELGGQKQRADML--------EMELKMLKSQSSSAEQSFLFSREEADTLRLKVEEL-------EGERSRL 514
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLqerlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEEL 998
|
410
....*....|..
gi 2947031 515 EEEKRMLEAQLE 526
Cdd:TIGR02168 999 KERYDFLTAQKE 1010
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
50-385 |
5.39e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELEraastsarnyEREvdrNQELLTRIRQLQEREAGAEEKMQEQLE 129
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL----------KKE---NQSYKQEIKNLESQINDLESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 130 RNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDL-----------QH 198
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrsinkikqnLE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 199 KKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELvrlprlerELEQLREESALREMRE--TNG 276
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK--------ESKISDLEDELNKDDFelKKE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 277 LLQEELEGLQRKLgrqEKMQETLVGLELENERL--LAKLQSWERLDQTMGLSIRTPEdlsrfVVELQQRELALKDKNSAV 354
Cdd:TIGR04523 558 NLEKEIDEKNKEI---EELKQTQKSLKKKQEEKqeLIDQKEKEKKDLIKEIEEKEKK-----ISSLEKELEKAKKENEKL 629
|
330 340 350
....*....|....*....|....*....|.
gi 2947031 355 TSSARGLEKARQQLQEELRQVSGQLLEERKK 385
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-527 |
7.42e-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: 59.70 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 146 REKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQasqearadheQQI 225
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----------ERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 226 KDLEQKLSLQEQDAAIVKNMKSELvrlprlereleqlreESALREMRETNGLLQEELEGLQRKLGRQ--EKMQETLVGLE 303
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKEL---------------EARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 304 LENERLLAKLQSwerLDQTMGLSIRTPEDLSRFVVELQQRELALKDKnsavtssarglEKARQQLQEELRQVSGQLLEER 383
Cdd:TIGR02169 805 EEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-----------IKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 384 KKretHEALARRLQKRVLLLTKERDGMRAILGsydseltpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELG 463
Cdd:TIGR02169 871 EE---LEAALRDLESRLGDLKKERDELEAQLR-------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2947031 464 -------------GQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLER 527
Cdd:TIGR02169 935 eiedpkgedeeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
41-313 |
1.47e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 41 LQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVE--LERAASTSARNYEREVDRnQELLTRIRQLQEREA 118
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqlEERIAQLSKELTELEAEI-EELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 119 GAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLaqagetiNALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQH 198
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 199 KKCQEANQKIQELqasQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELvrlprlereleqlreESALREMRETNGLL 278
Cdd:TIGR02168 852 EDIESLAAEIEEL---EELIEELESELEALLNERASLEEALALLRSELEEL---------------SEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*
gi 2947031 279 QEELEGLQRKLgrqEKMQETLVGLELENERLLAKL 313
Cdd:TIGR02168 914 RRELEELREKL---AQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-508 |
5.08e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 146 REKEDSLaqagETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQ-EANQKIQELQASQEARADHEQQ 224
Cdd:TIGR02169 170 RKKEKAL----EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 225 IKDLEQKLS-LQEQDAAIVKNMKSELVRLPRLERELEQLREESALReMRETNGLLQEELEGLQR----KLGRQEKMQETL 299
Cdd:TIGR02169 246 LASLEEELEkLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERsiaeKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 300 VGLELENERLLAKLQSWErldqtmglsiRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQL 379
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELE----------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 380 LEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQAL 459
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------ELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2947031 460 EELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELE 508
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-319 |
6.28e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 41 LQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARV-ELERA------------ASTSARNYEREVDRNQELL 107
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeELEEDlhkleealndleARLSHSRIPEIQAELSKLE 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 108 TRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEK 187
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 188 QDVQEQLDLQHKKCQEANQKIQELQASQEaraDHEQQIKDLEQKLS-LQEQDAAIVKNMKSEL----VRLPRLERELEQL 262
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIE---KKRKRLSELKAKLEaLEEELSEIEDPKGEDEeipeEELSLEDVQAELQ 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2947031 263 REESALREMRETNGLLQEELEGLQRKLGRQEKMQETlvgLELENERLLAKLQSWERL 319
Cdd:TIGR02169 962 RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK---LEEERKAILERIEEYEKK 1015
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
78-393 |
1.15e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 78 HKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEE----------------KMQEQLERnrqCQQNLDAA 141
Cdd:COG3096 283 LSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaasdhlnlvqtalRQQEKIER---YQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 142 SKRLREKEDSLAQAGEtinalkgRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKcqeANQKIQELQASQEARA-- 219
Cdd:COG3096 360 TERLEEQEEVVEEAAE-------QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTR---AIQYQQAVQALEKARAlc 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 220 ------------------DHEQQIK----DLEQKLSLQ-------EQDAAIVKNMKSELVRlprlerELEQLREESALRE 270
Cdd:COG3096 430 glpdltpenaedylaafrAKEQQATeevlELEQKLSVAdaarrqfEKAYELVCKIAGEVER------SQAWQTARELLRR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 271 MRETNGLLQeELEGLQRKLGrqekmqetlvglelENERLLAKLQSWERL----DQTMGLSIRTPEDLSRFVVELQQRELA 346
Cdd:COG3096 504 YRSQQALAQ-RLQQLRAQLA--------------ELEQRLRQQQNAERLleefCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2947031 347 LKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALA 393
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLR 615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-631 |
2.33e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 366 QQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVH 445
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY------ALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 446 SHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEqsflfsrEEADTLRLKVEELEGERSRLEEEKRMLEAQL 525
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 526 ERraLQGDYDQSRTKVLhmSLNPTsvaRQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKK 605
Cdd:TIGR02168 382 ET--LRSKVAQLELQIA--SLNNE---IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
250 260
....*....|....*....|....*.
gi 2947031 606 QVESAELKNQRLKEVFQTKIQEFRKA 631
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAA 480
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-569 |
2.43e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQElltRIRQLQEREAGAEE--K 123
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKAEEdkK 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 124 MQEQLERNRQCQQNLDAASKRLREKEDSlaqagetiNALKGRISELQWSvmdQEMRVKRLESEKQDVQEQLDLQHKKCQE 203
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKA--------DEAKKKAEEAKKA---DEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 204 ANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMREtngllqeele 283
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE---------- 1544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 284 glqrklgrQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRfvVELQQRELALKDKNSAVTSSARGLEK 363
Cdd:PTZ00121 1545 --------KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 364 ARQQLQ--EELRQVSgqllEERKKRETHEALARRLQKRVLLLTKERDgmrailgsyDSELTPAEYSPQLTRRMREAEDMv 441
Cdd:PTZ00121 1615 AEEAKIkaEELKKAE----EEKKKVEQLKKKEAEEKKKAEELKKAEE---------ENKIKAAEEAKKAEEDKKKAEEA- 1680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 442 QKVHSHSAEMEAQLSQALEElggqKQRADMLEmelKMLKSQSSSAEQsflfSREEADTLRLKVEELEGERsrlEEEKRML 521
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE----AKKAEELK---KKEAEEKKKAEE----LKKAEEENKIKAEEAKKEA---EEDKKKA 1746
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2947031 522 EA----QLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECER 569
Cdd:PTZ00121 1747 EEakkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
50-400 |
2.49e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVEREKMQMElshkraRVELERAASTSARNYEREVdrnQELLTRIRQLQEREAGAEEKMQEQLE 129
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRE------REKAERYQALLKEKREYEG---YELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 130 RNRQCQQNLDAASKRLREKEDSLAQAGETINALKG----RISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEAN 205
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 206 QKIQElqasqearaDHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLprlerELEQLREESALREMRETNGLLQEELEGL 285
Cdd:TIGR02169 332 DKLLA---------EIEELEREIEEERKRRDKLTEEYAELKEELEDL-----RAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 286 QRKL----GRQEKMQETLVGLELENERLLAKLQSWErldqtmglsirtpEDLSRFVVELQQRELALKDKNSAVTSSARGL 361
Cdd:TIGR02169 398 KREInelkRELDRLQEELQRLSEELADLNAAIAGIE-------------AKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2947031 362 EKARQQ---LQEELRQVSGQLLEERKKRETHEALARRLQKRV 400
Cdd:TIGR02169 465 SKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
44-642 |
2.79e-07 |
|
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: 54.28 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 44 QYQQSMQLEERAEQIRSKSHLIQ----------VERE---KMQMELSHKRARVELERAASTSARNY----------EREV 100
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQslatrleldgFERGpfsERQIKNFHTLVIERQEDEAKTAAQLCadlqskerlkQEQA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 101 DRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLaqagetinalkgRISELQWSVMDQEMRV 180
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL------------RKAERELSKAEKNSLT 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 181 KRLESEKQDVQ-EQLDLQHKKCQEAnQKIQELQASQEARADHEQQIKDleqKLSLQEQDAAIVKNMKSELVRLprLEREL 259
Cdd:TIGR00606 497 ETLKKEVKSLQnEKADLDRKLRKLD-QEMEQLNHHTTTRTQMEMLTKD---KMDKDEQIRKIKSRHSDELTSL--LGYFP 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 260 EQLREESALREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQS--------------WERLDQTMGL 325
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeesdLERLKEEIEK 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 326 SIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTK 405
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 406 ERDGMRAILGSYDSELtpaeysPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQ-RADMLEMELKMLKSQSS 484
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEI------PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcLTDVTIMERFQMELKDV 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 485 SAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQ 564
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 565 AECERLRGLLRAMERGGTVPADLEAAAASLPSSKEvaelKKQVESAELKNQR--LKEVFQTKIQEFRKACYTLTGYQIDI 642
Cdd:TIGR00606 885 QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE----KDQQEKEELISSKetSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
51-531 |
5.15e-07 |
|
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: 53.58 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 51 LEERAEQIRSKSHLIQVEREKMQMELSHK-----RARVELERAAStSARNYEREVDRNQEllTRIRQLQEREAGAEEKMQ 125
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQnsmymRQLSDLESTVS-QLRSELREAKRMYE--DKIEELEKQLVLANSELT 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 126 E-QLERNRQCQQ--NLDAASKRL------REKEDSLAQAG-------ETINALKgrISELQWSVMDQEMRVKRLE----S 185
Cdd:pfam15921 360 EaRTERDQFSQEsgNLDDQLQKLladlhkREKELSLEKEQnkrlwdrDTGNSIT--IDHLRRELDDRNMEVQRLEallkA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 186 EKQDVQEQLDLQHKKCQEANQK---------------------IQELQASQEARADHEQQIKDLEQklSLQEQDAAIvKN 244
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNESlekvssltaqlestkemlrkvVEELTAKKMTLESSERTVSDLTA--SLQEKERAI-EA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 245 MKSELVRL---------------PRLERELEQLREESALR-EMRETNG---LLQEELEGLQRKLGRQEK----MQETLVG 301
Cdd:pfam15921 515 TNAEITKLrsrvdlklqelqhlkNEGDHLRNVQTECEALKlQMAEKDKvieILRQQIENMTQLVGQHGRtagaMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 302 LELE-NERLLaKLQSWERLDQTMGLSIRtpeDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLl 380
Cdd:pfam15921 595 LEKEiNDRRL-ELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL- 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 381 eeRKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELtpaEYSPQLTRRMREAEDMVQKVhshSAEMEAQLSQALE 460
Cdd:pfam15921 670 --NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL---EQTRNTLKSMEGSDGHAMKV---AMGMQKQITAKRG 741
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2947031 461 ELGGQKQRADMLE-------MELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQ 531
Cdd:pfam15921 742 QIDALQSKIQFLEeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
46-565 |
6.82e-07 |
|
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: 53.20 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHliqvEREK-MQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQL----------- 113
Cdd:pfam15921 370 QESGNLDDQLQKLLADLH----KREKeLSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlkamksecqgq 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 114 QEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQ 193
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 194 LDLqhkkcqeanqKIQELQaSQEARADHEQQIKDLEQKLSLQ--EQDAAI------VKNMkSELVRLPRLERELEQLREE 265
Cdd:pfam15921 526 VDL----------KLQELQ-HLKNEGDHLRNVQTECEALKLQmaEKDKVIeilrqqIENM-TQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 266 SALREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELE--------NERLLAKLQSWERLDQTMGLSIRTPEDLSRFV 337
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 338 VELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSY 417
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 418 DSELTPAEYSPQLtrrMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQR--ADMLEMELKMLKSQSSSAEQSFLFSRE 495
Cdd:pfam15921 754 EEAMTNANKEKHF---LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRlkEKVANMEVALDKASLQFAECQDIIQRQ 830
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 496 EADTLRLKveelegersrleeekrmLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQA 565
Cdd:pfam15921 831 EQESVRLK-----------------LQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTA 883
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
79-374 |
7.37e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 79 KRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKM--QEQLERnrqCQQNLDAASKRLREKEDSLAQAG 156
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIER---YQADLEELEERLEEQNEVVEEAD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 157 ETINALKGRISELqwsvmdqEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQ-----------------ASQEARA 219
Cdd:PRK04863 376 EQQEENEARAEAA-------EEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALErakqlcglpdltadnaeDWLEEFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 220 DHEQQIKD----LEQKLSLQ-------EQDAAIVKNMKSELVRlprlerELEQLREESALREMRETNgLLQEELEGLQRK 288
Cdd:PRK04863 449 AKEQEATEellsLEQKLSVAqaahsqfEQAYQLVRKIAGEVSR------SEAWDVARELLRRLREQR-HLAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 289 LGRQEKMQEtlvgLELENERLLAKLQswerldQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQL 368
Cdd:PRK04863 522 LSELEQRLR----QQQRAERLLAEFC------KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
....*.
gi 2947031 369 QEELRQ 374
Cdd:PRK04863 592 QARIQR 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-440 |
9.16e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 87 RAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRI 166
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 167 SELQWSVMDQEMRVKRLESEKQDVQEQLDLQhkkcQEANQKIQELQASQEARADHEQqIKDLEQKLS-LQEQDAAIVKNM 245
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSR-IPEIQAELSkLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 246 KSELVRLPRLERELEQLREESA-----LREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQS-WERL 319
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQelqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKeRDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 320 DQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEElrqvSGQLLEERKKRETHEALARRLQKR 399
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI----PEEELSLEDVQAELQRVEEEIRAL 970
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2947031 400 vllltkERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDM 440
Cdd:TIGR02169 971 ------EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
94-531 |
1.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 94 RNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAAS--KRLREKEDSLAQAGETINALKGRISELQw 171
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 172 svmDQEMRVKRLESEKQDVQEQLDLQHKKC-----QEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDaaiVKNMK 246
Cdd:COG4717 160 ---ELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE---LEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 247 SELVRLPRLERELEQLREESALREMRETNGLLQEELEGLQRKLGrqekMQETLVGLELENERLLAKLQSWERLDQTMGLS 326
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG----VLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 327 IRTPEDLSRFVVELQQRELALKDKNSAvtSSARGLEKARQQLQEELRQVSGqlLEERKKRETHEALARRLQKRVLLltKE 406
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSP--EELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGV--ED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 407 RDGMRAILgsydseltpaeyspqltRRMREAEDMVQKVHSHSAEMEAQLSQALEELggQKQRADMLEMELKMLKSQSSSA 486
Cdd:COG4717 384 EEELRAAL-----------------EQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEEL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2947031 487 EQSFLFSREEADTLRLKVEELEGER--SRLEEEKRMLEAQLERRALQ 531
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
202-630 |
2.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 202 QEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLprlereleqlreeSALREMRETNGLLQEE 281
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-------------LQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 282 LEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWER-LDQTM-GLSIRTPEDLSRFVVELQQRELALKDknsavtssar 359
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEeLEELLeQLSLATEEELQDLAEELEELQQRLAE---------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 360 gLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTkeRDGMRAILGSYDSELTPAEYSP----------- 428
Cdd:COG4717 211 -LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI--AAALLALLGLGGSLLSLILTIAgvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 429 -----------QLTRRMREAEDMVQKVHSHSAEMEAQLSQ--------------ALEELGGQKQRADMLEMELKMLKSQS 483
Cdd:COG4717 288 llflllarekaSLGKEAEELQALPALEELEEEELEELLAAlglppdlspeelleLLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 484 SSAEQSFLFSR---EEADTLRLKVEELEgERSRLEEEKRMLEAQLERRA--LQGDYDQSRTKVLHMSLNPTSVARQRLRE 558
Cdd:COG4717 368 LEQEIAALLAEagvEDEEELRAALEQAE-EYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2947031 559 DHSQLQAECERLRGLLRAMERGGTVpADLEAAAASLpsSKEVAELKKQVESAELknqrLKEVFQTKIQEFRK 630
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGEL-AELLQELEEL--KAELRELAEEWAALKL----ALELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-590 |
2.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 361 LEKARQQLQ--EELRQVSGQLLEERKKRETHEALARRL-----QKRVLLLTKERDGMRAILGSYDSELTPAEyspQLTRR 433
Cdd:COG4913 244 LEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLE---ARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 434 MREAEDMVQKVHSHS-----AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRlkvEELE 508
Cdd:COG4913 321 LREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL---EALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 509 GERSRLEEEKRMLEAQLerralqgdydqsrtkvlhmslnptsvarQRLREDHSQLQAECERLRGllrameRGGTVPADLE 588
Cdd:COG4913 398 EELEALEEALAEAEAAL----------------------------RDLRRELRELEAEIASLER------RKSNIPARLL 443
|
..
gi 2947031 589 AA 590
Cdd:COG4913 444 AL 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-526 |
2.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 51 LEERAEQIRSKshLIQVEREKMQMElSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEK------M 124
Cdd:PRK03918 212 ISSELPELREE--LEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 125 QEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQwsvmDQEMRVKRLESEKQDVQ---EQLDLQHKKC 201
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEkrlEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 202 QEANQKIQELQASQEARADH-----EQQIKDLEQKLSLQEQDAAIVKNMKSELvrlprlerELEQLREESALREMRETNG 276
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 277 ----------------LLQE---ELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFV 337
Cdd:PRK03918 437 kcpvcgrelteehrkeLLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 338 VE-----------LQQRELALKDKNSAVTSSAR---GLEKARQQLQEELRQVsgqlleERKKRETHEALARRLQKRVLLL 403
Cdd:PRK03918 517 LEelekkaeeyekLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDEL------EEELAELLKELEELGFESVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 404 TKERDGMRAILGSYdSELTPAEyspqltRRMREAEDMVQKvhshsaeMEAQLSQALEELGGQKQRADMLEMELKMLKSqs 483
Cdd:PRK03918 591 EERLKELEPFYNEY-LELKDAE------KELEREEKELKK-------LEEELDKAFEELAETEKRLEELRKELEELEK-- 654
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2947031 484 ssaeqsfLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLE 526
Cdd:PRK03918 655 -------KYSEEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-628 |
3.12e-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: 50.84 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 268 LREMRETNGLLQEELEGLQRKLGRQEK-MQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELA 346
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 347 LKDKNSAVTSSARGLEKARQQLQEELRQvsgqlLEERKKRETHEALARRLQKrvllLTKERDGMRAILGSYDSELTPAEY 426
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALND-----LEARLSHSRIPEIQAELSK----LEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 427 SPQLtrrmreAEDMVQKVHSHSAEMEAQLS---QALEELGGQKQradmlEMElkmlksqsssaeqsflfsrEEADTLRLK 503
Cdd:TIGR02169 827 EKEY------LEKEIQELQEQRIDLKEQIKsieKEIENLNGKKE-----ELE-------------------EELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 504 VEELEGERSRLEEEKRMLEAQLerRALQGDYDQSRTKVlhmslnptsvarQRLREDHSQLQAECERLRGLLRAMERggTV 583
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQL--RELERKIEELEAQI------------EKKRKRLSELKAKLEALEEELSEIED--PK 940
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2947031 584 PADLEAAAASLPSSKevaeLKKQVESAELKNQRLKEVFQTKIQEF 628
Cdd:TIGR02169 941 GEDEEIPEEELSLED----VQAELQRVEEEIRALEPVNMLAIQEY 981
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
79-219 |
5.01e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.09 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 79 KRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAE-EKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGE 157
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQREEERLVQKEEQLDARAEKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2947031 158 TINALKGRISELQWSVMDQEMRVKRLESE--KQDVQEQLD--LQHKKCQEANQKIQELQASQEARA 219
Cdd:PRK12705 113 ALSARELELEELEKQLDNELYRVAGLTPEqaRKLLLKLLDaeLEEEKAQRVKKIEEEADLEAERKA 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-519 |
5.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHLIQVEREKMQmELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAE---E 122
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPerlE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 123 KMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETIN-ALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLdlqhkkc 201
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEEL------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 202 QEANQKIQELQASQEaRADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLReesalremretnGLLQEE 281
Cdd:COG4717 223 EELEEELEQLENELE-AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL------------GLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 282 LEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWerLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSAR-G 360
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLeE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 361 LEKARQQLQEELRQVSGQLLEER-KKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSpQLTRRMREAED 439
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAAlEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE-ELEEELEELEE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 440 MVQKVHSHSAEMEAQLSQALEElggqkQRADMLEMELKMLKSQSSSAEqsflfsrEEADTLRLKVEELEGERSRLEEEKR 519
Cdd:COG4717 447 ELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELA-------EEWAALKLALELLEEAREEYREERL 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
36-627 |
8.28e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 36 SAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELeRAASTSARNYEREVDRNQELLTRIRQLqe 115
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL-RARIEELRAQEAVLEETQERINRARKA-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 116 reagaeEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQA-GETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQL 194
Cdd:TIGR00618 293 ------APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 195 DLQHKKCQEANQkiQELQASQEARADHEQQIKDLEQKLSLQEQDAAIV-------KNMKSELVRLPRLERELEQLREESA 267
Cdd:TIGR00618 367 IREISCQQHTLT--QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsafRDLQGQLAHAKKQQELQQRYAELCA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 268 LREMRETNGLLQEE--LEGLQRKLGRQEKMQETLVGLELENERLlaKLQSWERLDQTMGLSIRTPEDLSRFVVELQQrel 345
Cdd:TIGR00618 445 AAITCTAQCEKLEKihLQESAQSLKEREQQLQTKEQIHLQETRK--KAVVLARLLELQEEPCPLCGSCIHPNPARQD--- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 346 alKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILgsyDSELTPAE 425
Cdd:TIGR00618 520 --IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI---PNLQNITV 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 426 YSPQLTRRMREAEDMVqKVHSHSAEMEAQLSQALEELGGQKQRadmLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVE 505
Cdd:TIGR00618 595 RLQDLTEKLSEAEDML-ACEQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 506 ELEGERSRLEEEKrmlEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRlREDHSQLQAecerlrgllrAMERGGTVPA 585
Cdd:TIGR00618 671 PKELLASRQLALQ---KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD-REFNEIENA----------SSSLGSDLAA 736
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2947031 586 DLEAAAASLPSSKEVAE--LKKQVESAELKNQRLKEVFQTKIQE 627
Cdd:TIGR00618 737 REDALNQSLKELMHQARtvLKARTEAHFNNNEEVTAALQTGAEL 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-359 |
8.41e-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: 48.99 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 88 AASTSARNYEREVDRNQElltRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRIS 167
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 168 ELQwsvmdqemrvKRLESEKQDVQEQLDLQHKKcqeANQKIQELQASQEARADHEQQIKDLEQklsLQEQDAAIVKNMKS 247
Cdd:COG4942 94 ELR----------AELEAQKEELAELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 248 ELVRLprlereleqlreesalremRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKL-QSWERLDQTMGLS 326
Cdd:COG4942 158 DLAEL-------------------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAEL 218
|
250 260 270
....*....|....*....|....*....|...
gi 2947031 327 IRTPEDLSRFVVELQQRELALKDKNSAVTSSAR 359
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-232 |
1.03e-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: 49.28 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 42 QMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQElltrIRQLQEREAGAE 121
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 122 EKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKC 201
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
170 180 190
....*....|....*....|....*....|.
gi 2947031 202 QEANQKIQELQASQEARAdhEQQIKDLEQKL 232
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEA--RRRLKRLENKI 981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
211-412 |
1.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 211 LQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRlprlERELEQLREESALREMRETNGLLQEELEGLQRKLG 290
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 291 RQEKMQETLVGLELENERLLAKLQSWERLDQTMGL--------SIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLE 362
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2947031 363 KARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRA 412
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
50-525 |
2.52e-05 |
|
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: 47.91 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVE---REKMQMELSH-KRARVELERA-ASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKM 124
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEfntLESAELRLSHlHFGYKSDETLiASRQEERQETSAELNQLLRTLDDQWKEKRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 125 QEQLERNRQCQQNLDAASKRLREKEDSLAqagETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLD-LQHKKCQE 203
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADI---ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNrRRSKIKEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 204 ANQKI----QELQASQEARADHEQQIKDLEQKLSLQEQDaaivknmkselvrlprlereleqlREESALREMRETNGLLQ 279
Cdd:pfam12128 388 NNRDIagikDKLAKIREARDRQLAVAEDDLQALESELRE------------------------QLEAGKLEFNEEEYRLK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 280 EELEGLQRKLGRQEKMQETLVGLELENERLlaklqswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSAR 359
Cdd:pfam12128 444 SRLGELKLRLNQATATPELLLQLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 360 GLEKARQQLQEELRQVSGQLLEERKKRET--HEALARRLQKRVLL-------LTKERDGMRAILGSYDSELTP------A 424
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEAPdwEQSIGKVISPELLHrtdldpeVWDGSVGGELNLYGVKLDLKRidvpewA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 425 EYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKqradmLEMELKMLKSQSSSAEQSFLFSREEADTLRLKv 504
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS-----REETFARTALKNARLDLRRLFDEKQSEKDKKN- 670
|
490 500
....*....|....*....|.
gi 2947031 505 EELEGERSRLEEEKRMLEAQL 525
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQL 691
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
339-579 |
2.79e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 339 ELQQRE--LALKDKNSAVTSSARgLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERD-GMRAILG 415
Cdd:TIGR02169 219 EKREYEgyELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 416 SYDSELTPAEYS-PQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLK-------SQSSSAE 487
Cdd:TIGR02169 298 ELEAEIASLERSiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 488 QSFLFSREEADTLRLKVE-------ELEGERSRLEEEKRMLEAQLE--RRALQGDYD-----QSRTKVLHMSLNPTSVAR 553
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEklkreinELKRELDRLQEELQRLSEELAdlNAAIAGIEAkinelEEEKEDKALEIKKQEWKL 457
|
250 260
....*....|....*....|....*.
gi 2947031 554 QRLREDHSQLQAECERLRGLLRAMER 579
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEK 483
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
363-526 |
3.65e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 363 KARQQLQEELRQVSGQLLEE--------RKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYS------- 427
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARkqnkydelVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKieqfqkv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 428 ----------PQLTRRMREAEDMVQKVHSHSAEMEAQLSQ---ALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSR 494
Cdd:PHA02562 278 ikmyekggvcPTCTQQISEGPDRITKIKDKLKELQHSLEKldtAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180 190
....*....|....*....|....*....|..
gi 2947031 495 EEADTLRLKVEELEGERSRLEEEKRMLEAQLE 526
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-631 |
4.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 40 SLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQmelSHKRARVELERAastsarNYEREVDRNQELLTRIRQLQEREAG 119
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIELLEPIRELAE---RYAAARERLAEL------EYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 120 AEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQA-GETINALKGRIselqwsvmdqemrvKRLESEKQDVQEQLDLQH 198
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREI--------------ERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 199 KKCQEANQKIQELQAS-QEARADHEQQIKDLEQKLSLQEQDAAivknmkselvrlprlerelEQLREESALREMRETngl 277
Cdd:COG4913 366 ALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALA-------------------EAEAALRDLRRELRE--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 278 LQEELEGLQRKL----GRQEKMQETL---VGLELENERLLAKL-------QSW----ERLDQTMGLSIRTPE----DLSR 335
Cdd:COG4913 424 LEAEIASLERRKsnipARLLALRDALaeaLGLDEAELPFVGELievrpeeERWrgaiERVLGGFALTLLVPPehyaAALR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 336 FVVELQQR--------ELALKDKNSAVTSSARGLEK-------ARQQLQEELRQVSGqlleeRKKRETHEALaRRLQKRV 400
Cdd:COG4913 504 WVNRLHLRgrlvyervRTGLPDPERPRLDPDSLAGKldfkphpFRAWLEAELGRRFD-----YVCVDSPEEL-RRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 401 LL--LTKERDGMRAIlgsydseltpaeyspQLTRRMREA----EDMVQKVhshsAEMEAQLSQALEELGGQKQRADMLEM 474
Cdd:COG4913 578 TRagQVKGNGTRHEK---------------DDRRRIRSRyvlgFDNRAKL----AALEAELAELEEELAEAEERLEALEA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 475 ELKMLKSQSSSAEQSFLFSREEADT--LRLKVEELEGERSRLEEEKRMLEA-QLERRALQGDYDQSRTKvlhmsLNPTSV 551
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDLAAlEEQLEELEAELEELEEE-----LDELKG 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 552 ARQRLREDHSQLQAECERLRGLLRAMERGGTVP------ADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKI 625
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM 793
|
....*.
gi 2947031 626 QEFRKA 631
Cdd:COG4913 794 RAFNRE 799
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
35-506 |
5.23e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 35 TSAPGSLQMQYQQSMQLEERAE---QIRSKSHLIQVEREKMQMELSHK----RARVELERAASTSA-----RNYEREVDR 102
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEedlQIATKTICQLTEEKEAQMEELNKakaaHSFVVTEFEATTCSleellRTEQQRLEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 103 NQELLTRIRQLQEREAGAEEKMQeQLERNRQCQqnLDAASKRLREKE---DSLAQAGETINALKGRISELQWSVMDQEMR 179
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMT-KFKNNKEVE--LEELKKILAEDEkllDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 180 VKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAI-VKNMKSELVRlprleRE 258
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLeLKKHQEDIIN-----CK 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 259 LEQLREESALREMRETNGLLQEELEGLQRKLGRQ--------EKMQETLVGLELENERLLAKLQSWERLDQTMGLSIrtp 330
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--- 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 331 EDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQvSGQLLEERKKRETHEALARRLQKRVLLLTKERDGM 410
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS-AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 411 RAilgsydSELTPAEYSPQLTRRMREAEdMVQKVHSHSAEMEAQLSQALEELGGQKQRAD-------MLEMELKMLKSQS 483
Cdd:pfam05483 683 IA------DEAVKLQKEIDKRCQHKIAE-MVALMEKHKHQYDKIIEERDSELGLYKNKEQeqssakaALEIELSNIKAEL 755
|
490 500
....*....|....*....|...
gi 2947031 484 SSAEQSFLFSREEADTLRLKVEE 506
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
41-627 |
5.44e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 41 LQMQYQQSMQLEERAE-QIRSKSHLIQVEREKMQMElshKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAG 119
Cdd:pfam15921 90 LQRRLNESNELHEKQKfYLRQSVIDLQTKLQEMQME---RDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 120 AEEKMQEQLERNRQCQQNL------------DAASKRLREKED-------SLAQA-GETINALKGRISELQWSVMDQEMR 179
Cdd:pfam15921 167 DSNTQIEQLRKMMLSHEGVlqeirsilvdfeEASGKKIYEHDSmstmhfrSLGSAiSKILRELDTEISYLKGRIFPVEDQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 180 VKRLESEKQDVQEQLDLQHKKCQEA--NQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAaivKNMKSELVRlprleR 257
Cdd:pfam15921 247 LEALKSESQNKIELLLQQHQDRIEQliSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA---RNQNSMYMR-----Q 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 258 ELEQLREESALR-EMRETNGLLQEELEGLQRKL---------GRQEK-------------MQETLVGL-ELENERLLAKL 313
Cdd:pfam15921 319 LSDLESTVSQLRsELREAKRMYEDKIEELEKQLvlanselteARTERdqfsqesgnlddqLQKLLADLhKREKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 314 QSWERLDQTMGLSIrTPEDLSRFV----VELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETH 389
Cdd:pfam15921 399 QNKRLWDRDTGNSI-TIDHLRRELddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 390 EALARRLQ-KRVLLLTKER----------DGMRAILGSyDSELTP----AEYSPQLTRRMREAEDMVQKVHSHSAEMEAQ 454
Cdd:pfam15921 478 RKVVEELTaKKMTLESSERtvsdltaslqEKERAIEAT-NAEITKlrsrVDLKLQELQHLKNEGDHLRNVQTECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 455 LS-------------QALEELGGQKQR-ADMLEMELKMLKSQSSSAE---QSFLFSREEADTlrlKVEELEGERSRLEEE 517
Cdd:pfam15921 557 MAekdkvieilrqqiENMTQLVGQHGRtAGAMQVEKAQLEKEINDRRlelQEFKILKDKKDA---KIRELEARVSDLELE 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 518 K-RMLEAQLERRALQGDYDQSRTKVLH------MSLNPTS----VARQRLREDHSQL--------------QAECERLRG 572
Cdd:pfam15921 634 KvKLVNAGSERLRAVKDIKQERDQLLNevktsrNELNSLSedyeVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRN 713
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2947031 573 LLRAMErggtvPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQE 627
Cdd:pfam15921 714 TLKSME-----GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-645 |
6.53e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 52 EERAEQIRSKSHLIQVEREKMQMELSHKRArvELERAASTSaRNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERN 131
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKER--ELEDAEERL-AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 132 RQ----CQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLdlqhkkcQEANQK 207
Cdd:TIGR02169 363 KEeledLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI-------AGIEAK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 208 IQELQASQEARADheqQIKDLEQKLslqEQDAAIVKNMKSELVRLprlereleqlreesalremRETNGLLQEELEGLQR 287
Cdd:TIGR02169 436 INELEEEKEDKAL---EIKKQEWKL---EQLAADLSKYEQELYDL-------------------KEEYDRVEKELSKLQR 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 288 KLGRQEKMQETLVGLELENER--------------LLAKLQSWERLDQTmGLSIRTPEDLSRFVVElqqrelalkdkNSA 353
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAveevlkasiqgvhgTVAQLGSVGERYAT-AIEVAAGNRLNNVVVE-----------DDA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 354 VTSSARGLEKARQ----------QLQEELRQVSGQLLE------------ERKKR-------------ETHEAlARRLQK 398
Cdd:TIGR02169 559 VAKEAIELLKRRKagratflplnKMRDERRDLSILSEDgvigfavdlvefDPKYEpafkyvfgdtlvvEDIEA-ARRLMG 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 399 RVLLLTKERDGMR---AILGSYDSELTPAEYSPQLTRRMREAEDMVQkvhshsaEMEAQLSQALEELGGQKQRADMLEME 475
Cdd:TIGR02169 638 KYRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 476 LKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERraLQGDYDQSRTKVLHMSLNPTSVARQR 555
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE--LEARIEELEEDLHKLEEALNDLEARL 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 556 LREDHSQLQAECERLRGLLRAMErggTVPADLEAAAASLPSSKEVAELK---KQVESAELKNQR------------LKEV 620
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIE---ARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIksiekeienlngKKEE 865
|
650 660
....*....|....*....|....*
gi 2947031 621 FQTKIQEFRKACYTLTGYQIDITTE 645
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKE 890
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
47-251 |
8.84e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 47 QSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAastSARNYEREVDR-NQELLTRIRQLQEREAG------ 119
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVE---EAKTIKAEIEElTDELLNLVMDIEDPSAAlnklnt 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 120 AEEKMQEQLERNRQ-------------CQQNLDAASKRLREKEDSLAQAGETINALKGRISELQwSVMDQemrVKRLESE 186
Cdd:PHA02562 263 AAAKIKSKIEQFQKvikmyekggvcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE-EIMDE---FNEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2947031 187 KQDVQEQLDLQH---KKCQEANQKIQ-ELQASQEARADHEQQIKDLEQKLSLqeqdaaiVKNMKSELVR 251
Cdd:PHA02562 339 LLELKNKISTNKqslITLVDKAKKVKaAIEELQAEFVDNAEELAKLQDELDK-------IVKTKSELVK 400
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-252 |
9.35e-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: 45.53 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 37 APGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVE-LERAASTSARNYEREVDRNQELLTRIRQLQE 115
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAaLERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 116 REAGAEEKMQEQLErnrQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLD 195
Cdd:COG4942 91 EIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2947031 196 LQHKKCQEANQKIQELQASQE----ARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRL 252
Cdd:COG4942 168 ELEAERAELEALLAELEEERAaleaLKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
51-525 |
9.95e-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: 45.78 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 51 LEERAEQIRSKSHLIQVEREKMQMELShkRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLER 130
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEIS--NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 131 NRQCQQNLDAASK-RLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLdlqhkkcQEANQKIQ 209
Cdd:TIGR04523 301 NNQKEQDWNKELKsELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 210 ELQASQEARADH----EQQIKDLEQKLSLQEQDAAI----VKNMKSELVRLPRLereleqlreesaLREMRETNGLLQEE 281
Cdd:TIGR04523 374 KLKKENQSYKQEiknlESQINDLESKIQNQEKLNQQkdeqIKKLQQEKELLEKE------------IERLKETIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 282 LEGLQrklgrqekmqETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDlsrfvvELQQRELALKDKNSAVTSsargL 361
Cdd:TIGR04523 442 IKDLT----------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ------NLEQKQKELKSKEKELKK----L 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 362 EKARQQLQEE---LRQVSGQLLEERKKREThealaRRLQKRVLLLTKERDgmraiLGSYDSELTpaeySPQLTRRMREAE 438
Cdd:TIGR04523 502 NEEKKELEEKvkdLTKKISSLKEKIEKLES-----EKKEKESKISDLEDE-----LNKDDFELK----KENLEKEIDEKN 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 439 DMVQKVHSHSAEMEAQLSQAleelggqKQRADMLEMELKMLKSQSSSAEQsflfsreeadtlrlKVEELEGERSRLEEEK 518
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEK-------QELIDQKEKEKKDLIKEIEEKEK--------------KISSLEKELEKAKKEN 626
|
....*..
gi 2947031 519 RMLEAQL 525
Cdd:TIGR04523 627 EKLSSII 633
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-252 |
1.02e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 104 QELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVM--------- 174
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 175 -------DQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQAS-QEARADHEQQIKDLEQKLS-LQEQDAAIVKNM 245
Cdd:COG1579 93 alqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAELEAELEeLEAEREELAAKI 172
|
....*..
gi 2947031 246 KSELVRL 252
Cdd:COG1579 173 PPELLAL 179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
50-564 |
1.19e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAA---------STSARNYERE------VDRNQELLTRIRQLQ 114
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAArqklqlekvTTEAKIKKLEedilllEDQNSKLSKERKLLE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 115 EREAGAEEKMQEQLERNRQCQQ-------NLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEK 187
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKlknkheaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 188 QDVQEQL-DLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRL-ERELEQLREE 265
Cdd:pfam01576 239 AKKEEELqAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTElEDTLDTTAAQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 266 SALREMRETngllqeELEGLQRKLGRQEKMQETLVGlELENERLLAKLQSWERLDQTmglsirtpedlSRFVVELQQREL 345
Cdd:pfam01576 319 QELRSKREQ------EVTELKKALEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQA-----------KRNKANLEKAKQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 346 ALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTP-A 424
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlS 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 425 EYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKV 504
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 505 EELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQ 564
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-611 |
1.47e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 82 RVELERAASTSARNYEREVDRNQEllTRIRQLQEREAGAEEK-MQEQLERNRQCQQNLDAASKRLREKEDslaQAGETIN 160
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEEKEEKdLHERLNGLESELAELDEEIERYEEQRE---QARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 161 ALKGRISELQwsvmDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQasqEARADHEQQIKDLEQKLSLQEQDAA 240
Cdd:PRK02224 238 EADEVLEEHE----ERREELETLEAEIEDLRETIAETEREREELAEEVRDLR---ERLEELEEERDDLLAEAGLDDADAE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 241 IVKNMKSELVRLPRLERELEQLREESALREMRETNGL------LQEELEGLQRKLGRQEK-MQETLVGLELENERLLAKL 313
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLredaddLEERAEELREEAAELESeLEEAREAVEDRREEIEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 314 QSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKAR---QQLQEELR-QVSGQLLEERKKRETH 389
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaEALLEAGKcPECGQPVEGSPHVETI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 390 EALARRLQKrvllLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRA 469
Cdd:PRK02224 471 EEDRERVEE----LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 470 DMLEMELKMLKSQSSSAeqsflfsREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQsrtkvlhmslnpt 549
Cdd:PRK02224 547 AELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED------------- 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2947031 550 svARQRLREDHSQLQAECERLRGLLRAM-ERGGTVPADLEAAAaslpsskeVAELKKQVESAE 611
Cdd:PRK02224 607 --EIERLREKREALAELNDERRERLAEKrERKRELEAEFDEAR--------IEEAREDKERAE 659
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
87-527 |
2.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 87 RAASTSARNYEREVDRNQELLTRIRQL---QEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAgETINALK 163
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLaaeQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 164 GRISELQWSVMDQEMRVkrlesekQDVQEQLDLQHKKCQEANQKIQELQASQearADHEQQIkDLEQKLSLQEQDAaivk 243
Cdd:PRK04863 355 ADLEELEERLEEQNEVV-------EEADEQQEENEARAEAAEEEVDELKSQL---ADYQQAL-DVQQTRAIQYQQA---- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 244 nmkselvrlprlereleqlreESALREMRETNG---LLQEELEGLQRKLGRQEKmQETLVGLELENERLLAKLQSwERLD 320
Cdd:PRK04863 420 ---------------------VQALERAKQLCGlpdLTADNAEDWLEEFQAKEQ-EATEELLSLEQKLSVAQAAH-SQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 321 QTMGLSIRTPEDLSRFVVELQQRELALKdknsavTSSARGLEKARQQLQEELRQVSGQLLEERkkreTHEALARRLQKRv 400
Cdd:PRK04863 477 QAYQLVRKIAGEVSRSEAWDVARELLRR------LREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKR- 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 401 llltkerdgmrailgsYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEME----- 475
Cdd:PRK04863 546 ----------------LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaaq 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2947031 476 --LKMLKSQSSSAeqsfLFSREEADTLR----LKVEELEGERSRLEEEKRMLEAQLER 527
Cdd:PRK04863 610 daLARLREQSGEE----FEDSQDVTEYMqqllERERELTVERDELAARKQALDEEIER 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-611 |
3.22e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 121 EEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRI-SELQWSVMDQEMRVkRLESEKQDVQEQLDLQHK 199
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqAETELCAEAEEMRA-RLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 200 KCQEANQKIQELQASqeaRADHEQQIKDLEQKLSlQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMRETNGLLQ 279
Cdd:pfam01576 83 RLEEEEERSQQLQNE---KKKMQQHIQDLEEQLD-EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 280 EELEGLQRKLGRQEKMQETLVGLELENERLLAKLQ--------SWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKN 351
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlkkeekGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 352 SA-----VTSSARGLEK--ARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILgsYDSELTPA 424
Cdd:pfam01576 239 AKkeeelQAALARLEEEtaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL--EDTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 425 EYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEElggQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKV 504
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK---HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 505 EELEGERSRLEEEKRMLEAQLERralqgdydqsrtkvLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRamerggtvp 584
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQE--------------LQARLSESERQRAELAEKLSKLQSELESVSSLLN--------- 450
|
490 500
....*....|....*....|....*..
gi 2947031 585 adlEAAAASLPSSKEVAELKKQVESAE 611
Cdd:pfam01576 451 ---EAEGKNIKLSKDVSSLESQLQDTQ 474
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
73-527 |
4.19e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 73 QMELSHKRAR--VELERAASTSARNYErevdrnqellTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLrEKED 150
Cdd:pfam01576 318 QQELRSKREQevTELKKALEEETRSHE----------AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL-ESEN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 151 slaqagetiNALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARAdheQQIKDLEQ 230
Cdd:pfam01576 387 ---------AELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS---SLLNEAEG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 231 KLSLQEQDAAivknmkselvrlprlereleqlreeSALREMRETNGLLQEELeglQRKLGRQEKMQEtlvgleLENERll 310
Cdd:pfam01576 455 KNIKLSKDVS-------------------------SLESQLQDTQELLQEET---RQKLNLSTRLRQ------LEDER-- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 311 AKLQswERLDQTMglsiRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHE 390
Cdd:pfam01576 499 NSLQ--EQLEEEE----EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 391 ALARRLQKRVLLLTKERDGMRAILGSY------------DSELTPAEYSPQLTRRMREAEDMVQKVHShsaemeaqLSQA 458
Cdd:pfam01576 573 KTKNRLQQELDDLLVDLDHQRQLVSNLekkqkkfdqmlaEEKAISARYAEERDRAEAEAREKETRALS--------LARA 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 459 LEELGGQKQRAD----MLEMELKMLKSQSSSA-------EQSFLFSREEADTLRLKVEELEGE-------RSRLEEEKRM 520
Cdd:pfam01576 645 LEEALEAKEELErtnkQLRAEMEDLVSSKDDVgknvhelERSKRALEQQVEEMKTQLEELEDElqatedaKLRLEVNMQA 724
|
....*..
gi 2947031 521 LEAQLER 527
Cdd:pfam01576 725 LKAQFER 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-230 |
5.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 51 LEERAEQIRSkshliqVEREKMQMELSHKRARVELERAasTSARNYEREVDRNQELLTRIRQL-QEREAGAEEKmQEQLE 129
Cdd:PRK02224 470 IEEDRERVEE------LEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLEELiAERRETIEEK-RERAE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 130 RNRQCQQNLDAASKRLRE----KEDSLAQAGETINALKG-------------RISELQWSVMDQEMRVKRLESEKQDVQE 192
Cdd:PRK02224 541 ELRERAAELEAEAEEKREaaaeAEEEAEEAREEVAELNSklaelkeriesleRIRTLLAAIADAEDEIERLREKREALAE 620
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2947031 193 QLDLQHKKCQEANQKIQELQAS------QEARADHEQQIKDLEQ 230
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEfdeariEEAREDKERAEEYLEQ 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
49-237 |
5.27e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 49 MQLEERA---EQIRSKSHLIQVER----EKMQMELSHK--RARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAG 119
Cdd:pfam17380 353 IRQEERKrelERIRQEEIAMEISRmrelERLQMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 120 AEEKMQ-------EQLERNRQCQQNLDAASKRLREKEDSLAQAG---ETINALKGRISELQWSVMDQEMRVKRLESEKQD 189
Cdd:pfam17380 433 RQREVRrleeeraREMERVRLEEQERQQQVERLRQQEEERKRKKlelEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2947031 190 VQEQldLQHKKCQEANQKIQELQASQEARADHEQQiKDLEQKLSLQEQ 237
Cdd:pfam17380 513 RKRK--LLEKEMEERQKAIYEEERRREAEEERRKQ-QEMEERRRIQEQ 557
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-539 |
5.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 51 LEERAEQIRSKSHLIQVEREKMQMELSHKRARV-ELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQE--- 126
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLeELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 127 -------QLERNRQCQQNLDAASKRLREK----EDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLD 195
Cdd:PRK02224 336 aaqahneEAESLREDADDLEERAEELREEaaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 196 LQHKKCQEANQKIQELQAS-QEARadheqqiKDLEQKLSLQEQDaaivknmkselvRLPRLERELEQLREESALREMRET 274
Cdd:PRK02224 416 ELREERDELREREAELEATlRTAR-------ERVEEAEALLEAG------------KCPECGQPVEGSPHVETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 275 NGLLQEELEGLQRKLGRQEKMQETLVGL-ELENERllaklqswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSA 353
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLvEAEDRI--------ERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 354 VTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTkERDGMRAILGSYdseltpAEYSPQLTRR 433
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERL------REKREALAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 434 MREAEDMVQKVHSHSAEMEAQLSQA-LEELGGQKQRADM----LEMELKMLksqsssaeqsflfsREEADTLRLKVEELE 508
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEyleqVEEKLDEL--------------REERDDLQAEIGAVE 687
|
490 500 510
....*....|....*....|....*....|..
gi 2947031 509 GERSRLEEEKRMLEAQLERR-ALQGDYDQSRT 539
Cdd:PRK02224 688 NELEELEELRERREALENRVeALEALYDEAEE 719
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
203-541 |
6.22e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 203 EANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMRETNGLLQEEL 282
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 283 EGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLdqtmgLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLE 362
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK-----LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 363 KARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQ 442
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 443 KVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLE 522
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330
....*....|....*....
gi 2947031 523 AQLERRALQGDYDQSRTKV 541
Cdd:pfam02463 488 LLLSRQKLEERSQKESKAR 506
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
41-351 |
6.87e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 41 LQMQYQQSMQleeRAEQIRSKSHLIQVEREkMQMELSHKRARVELERAASTSARNYEREVDR---------NQELLTRIR 111
Cdd:COG5022 760 LRRRYLQALK---RIKKIQVIQHGFRLRRL-VDYELKWRLFIKLQPLLSLLGSRKEYRSYLAciiklqktiKREKKLRET 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 112 QLQEREAGAEE------------KMQEQLERN---RQCQQNLDAASKRLREKEDslaqAGETINALKGRISELQWSVMDQ 176
Cdd:COG5022 836 EEVEFSLKAEVliqkfgrslkakKRFSLLKKEtiyLQSAQRVELAERQLQELKI----DVKSISSLKLVNLELESEIIEL 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 177 EMRVKRLESEKQDVQEQLDLQHKKcqeANQKIQ-ELQASQEARA-DHEQQIKDLEQKL-SLQEQDAAIVKNMKSELVRLp 253
Cdd:COG5022 912 KKSLSSDLIENLEFKTELIARLKK---LLNNIDlEEGPSIEYVKlPELNKLHEVESKLkETSEEYEDLLKKSTILVREG- 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 254 rlereleqlreESALREMRETNGLLQEELEGLQRklgrqekMQETLVGLElENERLLAKLQSWERLDQTMG--LSIRTPE 331
Cdd:COG5022 988 -----------NKANSELKNFKKELAELSKQYGA-------LQESTKQLK-ELPVEVAELQSASKIISSESteLSILKPL 1048
|
330 340
....*....|....*....|
gi 2947031 332 DLSRFVVELQQRELALKDKN 351
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKA 1068
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
114-571 |
8.37e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 114 QEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGET--------INALKGRISELQWSVMDQEMRVKRLES 185
Cdd:PRK10246 375 QTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAeqrplrqrLVALHGQIVPQQKRLAQLQVAIQNVTQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 186 EKQDVQEQLDLQHKKCQEANQKIQELQASQEaradHEQQIKDLEQKLSLQE--QDAAIVKNMKSELVRLPRLERELEQLR 263
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADVKTICE----QEARIKDLEAQRAQLQagQPCPLCGSTSHPAVEAYQALEPGVNQS 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 264 EESALRE----MRETNGLLQEELEGLQRKLGRQEKMQETLvgleLENERLLAklQSWERLDQTMGLSIRTPEDLSRFVVE 339
Cdd:PRK10246 531 RLDALEKevkkLGEEGAALRGQLDALTKQLQRDESEAQSL----RQEEQALT--QQWQAVCASLNITLQPQDDIQPWLDA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 340 LQQRE-------------LALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKK------RETHEALARRLQKRV 400
Cdd:PRK10246 605 QEEHErqlrllsqrhelqGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEaswlatRQQEAQSWQQRQNEL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 401 LLLTKERDGMRAILGSY-DSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQaleelggQKQRADMLEmelkml 479
Cdd:PRK10246 685 TALQNRIQQLTPLLETLpQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVL-------EAQRLQKAQ------ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 480 kSQSSSAEQSFLFSREEADTLRLKVEElegERSRLEEEKRMLEAQLER-RALQGDYDQSRTKVLHM---SLNPTSVARQR 555
Cdd:PRK10246 752 -AQFDTALQASVFDDQQAFLAALLDEE---TLTQLEQLKQNLENQRQQaQTLVTQTAQALAQHQQHrpdGLDLTVTVEQI 827
|
490
....*....|....*.
gi 2947031 556 lredHSQLQAECERLR 571
Cdd:PRK10246 828 ----QQELAQLAQQLR 839
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
50-628 |
8.87e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIRSKSHLIQVEREKMQ-MELSHKRARVELERAASTSaRNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQL 128
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQeLQFENEKVSLKLEEEIQEN-KDLIKENNATRHLCNLLKETCARSAEKTKKYEYER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 129 ERNRQCQQNLDAASKRLREKEDSLaqageTINALKGRIsELQWSVMDQEMRVKRLESEKQ----DVQEQLDLQHKKCQEA 204
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEEL-----RVQAENARL-EMHFKLKEDHEKIQHLEEEYKkeinDKEKQVSLLLIQITEK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 205 NQKIQELQASQEARADHEQQikdLEQKLSLQEQDAAIVKNMKSEL------VRLPRLERELEQLREESALREMRETNGLL 278
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQ---LEEKTKLQDENLKELIEKKDHLtkeledIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 279 QEELEGLQRKLGRQeKMQETLVGLELEnerllAKLQSWERLDQTMGLSIRTPED-LSRFVVELQQRELALKDKNSAVTSS 357
Cdd:pfam05483 330 TEEKEAQMEELNKA-KAAHSFVVTEFE-----ATTCSLEELLRTEQQRLEKNEDqLKIITMELQKKSSELEEMTKFKNNK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 358 ARGLEKARQQLQEElrqvsGQLLEERKKretHEALARRLQKRVLLLTkerdgmrAILGSYDSELTPAEYspQLTRRMREA 437
Cdd:pfam05483 404 EVELEELKKILAED-----EKLLDEKKQ---FEKIAEELKGKEQELI-------FLLQAREKEIHDLEI--QLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 438 EDMVQKVHSHSAEMEAQLSQALEelggQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEE 517
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIE----LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 518 KRMLEAQLE--RRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQ--LQAECERLRgllRAMERGGTVPADLEAAAAS 593
Cdd:pfam05483 543 EMNLRDELEsvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMkiLENKCNNLK---KQIENKNKNIEELHQENKA 619
|
570 580 590
....*....|....*....|....*....|....*
gi 2947031 594 LpSSKEVAElKKQVESAELKNQRLKEVFQTKIQEF 628
Cdd:pfam05483 620 L-KKKGSAE-NKQLNAYEIKVNKLELELASAKQKF 652
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
50-248 |
9.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 50 QLEERAEQIrskshliqVEREKMQMELSHKRARVELERAASTSARNYEREV-DRNQELltrirqlqereagaeekmQEQL 128
Cdd:PRK12704 35 EAEEEAKRI--------LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrERRNEL------------------QKLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 129 ERNRQCQQNLDAASKRLREKEDSLaqagetinalkgriselqwsvmdqEMRVKRLESEKQDVQEQLDLQHKKCQEANQKI 208
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEEL------------------------EKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2947031 209 QELQA--SQEARadhEQQIKDLEQKlsLQEQDAAIVKNMKSE 248
Cdd:PRK12704 145 ERISGltAEEAK---EILLEKVEEE--ARHEAAVLIKEIEEE 181
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
202-635 |
1.17e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 202 QEANQKIQELQAS-QEARADHEQQIKDLEQK---LSLQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMRETNGL 277
Cdd:pfam15921 81 EEYSHQVKDLQRRlNESNELHEKQKFYLRQSvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 278 LQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQswerldQTMGLSIRTPEDLSrfvvelqqrELALKDKNSAVTSS 357
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFE------EASGKKIYEHDSMS---------TMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 358 ARGLEKARQQLQEELRQVSGQLleerkkrethEALARRLQKRV-LLLTKERDGMRAILGSYDSELTpaeyspQLTRRMRE 436
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQL----------EALKSESQNKIeLLLQQHQDRIEQLISEHEVEIT------GLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 437 AEDMVQKVHSH----SAEMEAQLSQALEELGGQKQRADMLEMELK----MLKSQSSSAEQSFLFSREEADTLRLKVEELE 508
Cdd:pfam15921 290 ARSQANSIQSQleiiQEQARNQNSMYMRQLSDLESTVSQLRSELReakrMYEDKIEELEKQLVLANSELTEARTERDQFS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 509 GERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAM--ERGGTVPAD 586
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksECQGQMERQ 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2947031 587 LEAAAASLPSSKEVAELKKQVESAelknqrlKEVFQTKIQEFRKACYTL 635
Cdd:pfam15921 450 MAAIQGKNESLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTL 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-631 |
1.67e-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: 41.67 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 449 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERR 528
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 529 ------ALQGDYDQSRTKVLHMSLNPTSVAR--QRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSK-E 599
Cdd:COG4942 103 keelaeLLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLaE 182
|
170 180 190
....*....|....*....|....*....|..
gi 2947031 600 VAELKKQVESAELKNQRLKEVFQTKIQEFRKA 631
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
124-413 |
1.73e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 124 MQEQLERNR-QCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQdvQEQLDLQHKKCQ 202
Cdd:pfam12128 598 SEEELRERLdKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ--SEKDKKNKALAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 203 EANQKIQELQasqeaRADHEQQIKDLEQKLSLQEQdaaivKNMKSELVRLPRLERELEQLREESALREMRETNGLLQEEL 282
Cdd:pfam12128 676 RKDSANERLN-----SLEAQLKQLDKKHQAWLEEQ-----KEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 283 EGLQRKLgrQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSA-VTSSARGL 361
Cdd:pfam12128 746 KAELKAL--ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATqLSNIERAI 823
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2947031 362 EKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKrvlLLTKERDGMRAI 413
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE---NLRGLRCEMSKL 872
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
53-628 |
1.79e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 53 ERAEQIRSKshLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERnr 132
Cdd:pfam12128 347 EQLPSWQSE--LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALES-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 133 QCQQNLDAASKRLREKEDSLAQAgetINALKGRISELQWS---VMDQEMRVKRLESekqdVQEQLDLQHKKCQEANQKIQ 209
Cdd:pfam12128 423 ELREQLEAGKLEFNEEEYRLKSR---LGELKLRLNQATATpelLLQLENFDERIER----AREEQEAANAEVERLQSELR 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 210 ELQASQEARADHEQQIKD--LEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMRETNGLLQEELEGlqr 287
Cdd:pfam12128 496 QARKRRDQASEALRQASRrlEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDG--- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 288 klgrQEKMQETLVGLELENERLlaKLQSWERLDQTMGLSIRTPEDLSRFVVELQQR-ELALKDKNSAVTSSARGLEKARQ 366
Cdd:pfam12128 573 ----SVGGELNLYGVKLDLKRI--DVPEWAASEEELRERLDKAEEALQSAREKQAAaEEQLVQANGELEKASREETFART 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 367 QLQ---EELRQVSGQLL-EERKKRETHEALARRLQKRVLLLTKERD----GMRAILGSYDSELTPAEYSPQLTRRMREAE 438
Cdd:pfam12128 647 ALKnarLDLRRLFDEKQsEKDKKNKALAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 439 ------DMVQKVHSHSAEMEAQLSQ-------ALEELGGQKQRADMLEMELKMLKSQSSSAEQS-------FLFSRE--- 495
Cdd:pfam12128 727 ldaqlaLLKAAIAARRSGAKAELKAletwykrDLASLGVDPDVIAKLKREIRTLERKIERIAVRrqevlryFDWYQEtwl 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 496 --------EADTLRLKVEELEGERSRLEEEKRMLEAQLErralqgdydqsrtkvlhMSLNPTSVARQRLREDHSQLQAEC 567
Cdd:pfam12128 807 qrrprlatQLSNIERAISELQQQLARLIADTKLRRAKLE-----------------MERKASEKQQVRLSENLRGLRCEM 869
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2947031 568 ERLRGLlramerggTVPADLEAAAASLpsskevAELKKQVESAELKNQRLKEVFQTKIQEF 628
Cdd:pfam12128 870 SKLATL--------KEDANSEQAQGSI------GERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
278-590 |
2.16e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 278 LQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERL--DQTMGLSIRTPEDLSRFVVELQQRELALKdknsavT 355
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamERERELERIRQEERKRELERIRQEEIAME------I 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 356 SSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTK---ERDGMRAIlgsyDSELTPAEYSPQLTR 432
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQiraEQEEARQR----EVRRLEEERAREMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 433 RMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLfsrEEADTLRLKVEELEGERS 512
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2947031 513 RLEEEKRMLEAQLERRALQGDYDQSRTKVLHMslnptsvarqRLREDHSQLQAeCERLRGLLRAMERGGTVPADLEAA 590
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEERRRIQEQMR----------KATEERSRLEA-MEREREMMRQIVESEKARAEYEAT 594
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
46-225 |
2.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 46 QQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRN---QELLTRIRQLQEREAGAEE 122
Cdd:COG3206 205 NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviQQLRAQLAELEAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 123 KMQEQLERNRQCQQNLDAASKRLR-EKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLeSEKQdvQEQLDLQHKkc 201
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-PELE--AELRRLERE-- 359
|
170 180
....*....|....*....|....*.
gi 2947031 202 QEANQKIQE--LQASQEARADHEQQI 225
Cdd:COG3206 360 VEVARELYEslLQRLEEARLAEALTV 385
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
267-604 |
2.66e-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: 41.50 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 267 ALREMRETNGLLQ-----EELEGLQRKLGRQEK----MQETLVGLELENERLLAK-----LQSWERLDQTMGLSIRTPED 332
Cdd:pfam02463 175 LKKLIEETENLAEliidlEELKLQELKLKEQAKkaleYYQLKEKLELEEEYLLYLdylklNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 333 LSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELR--QVSGQLLEERKKRETHEALArRLQKRVLLLTKERDgm 410
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEeeLKSELLKLERRKVDDEEKLK-ESEKEKKKAEKELK-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 411 RAILGSYDSELTPAEYSPQLTRRMREAEDMVQK-VHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQS 489
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLqEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 490 FLFSREEADTLRLKVEELEgersRLEEEKRMLEAQLERRALQGDYDQSRTKVLHM---SLNPTSVARQRLREDHSQLQAE 566
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELE----ILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350
....*....|....*....|....*....|....*...
gi 2947031 567 CERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELK 604
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
214-619 |
3.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 214 SQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLprlereleqlreESALREMRETNGLLQEELEGLQRKLGRQE 293
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV------------LREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 294 KMQETLVGLELENERLL-------AKLQSWERLDQTMGLSIRTPED-----------------LSRFVVELQQRELALKD 349
Cdd:PRK03918 235 ELKEEIEELEKELESLEgskrkleEKIRELEERIEELKKEIEELEEkvkelkelkekaeeyikLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 350 KNSAVTSSARGLEKARQQLQE---ELRQVSGQLLEERKKRETHEALARRLQkRVLLLTKERDGMRAILGSYDSELTPAEY 426
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 427 SpQLTRRMREAEDMVQKVHSHSAEME---AQLSQALEELGGQKQRADMLEMELkmlksqsSSAEQSFLFSR--EEADTLR 501
Cdd:PRK03918 394 E-ELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAKGKCPVCGREL-------TEEHRKELLEEytAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 502 LKVEELEGERSRLEEEKRMLEAQLERralqgdydQSRTKVLHMSLNPTSVARQRLRE-DHSQLQAECERLRGLLramERG 580
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKK--------ESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK---EKL 534
|
410 420 430
....*....|....*....|....*....|....*....
gi 2947031 581 GTVPADLEAAAASLpssKEVAELKKQVESAELKNQRLKE 619
Cdd:PRK03918 535 IKLKGEIKSLKKEL---EKLEELKKKLAELEKKLDELEE 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
305-519 |
3.14e-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: 40.52 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 305 ENERLLAKLQswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVtssaRGLEKARQQLQEELRQVSGQLLE-ER 383
Cdd:COG4942 24 EAEAELEQLQ--QEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAElRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 384 KKRETHEALARRLqkRVLLLTKERDGMRAILGSYDSELTP------AEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQ 457
Cdd:COG4942 98 ELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2947031 458 ALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKR 519
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
187-489 |
4.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 187 KQDVQEQLD-LQHKKCQEANQK--IQELQASQE---ARADHEQQIKDLEQKLslqEQDAAIVKNMKSELVRLPrlerele 260
Cdd:PRK11281 38 EADVQAQLDaLNKQKLLEAEDKlvQQDLEQTLAlldKIDRQKEETEQLKQQL---AQAPAKLRQAQAELEALK------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 261 qlreESALREMRETNGLLqeELEGLQRKLG-RQEKMQETLVGLELENERLLAkLQSwerldqtmgLSIRTPEDLSRFVVE 339
Cdd:PRK11281 108 ----DDNDEETRETLSTL--SLRQLESRLAqTLDQLQNAQNDLAEYNSQLVS-LQT---------QPERAQAALYANSQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 340 LQQRELALKDKN---SAVTSSARGLEKARQQL---QEELRQvsgQLLE--------ERKKRETHEALARRLQKRVLLLTK 405
Cdd:PRK11281 172 LQQIRNLLKGGKvggKALRPSQRVLLQAEQALlnaQNDLQR---KSLEgntqlqdlLQKQRDYLTARIQRLEHQLQLLQE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 406 ERDGMRAILgsydSELTPAEY-SPQLTRRMrEAEDMVQKvhshsaEMEA--QLSQALEElggQKQRADMLEMELKMLKSQ 482
Cdd:PRK11281 249 AINSKRLTL----SEKTVQEAqSQDEAARI-QANPLVAQ------ELEInlQLSQRLLK---ATEKLNTLTQQNLRVKNW 314
|
....*..
gi 2947031 483 SSSAEQS 489
Cdd:PRK11281 315 LDRLTQS 321
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
75-355 |
4.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 75 ELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQ 154
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 155 AG-------ETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKD 227
Cdd:COG4372 92 AQaelaqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 228 LEQKLSLQEQDAAIVKNMKSELVRLPRLERELEQLREESALREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENE 307
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2947031 308 RLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVT 355
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
344-539 |
5.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 344 ELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKK-------RETHEALAR--RLQKRVLLLTKERDGMRAIL 414
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlsEEAKLLLQQlsELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 415 GSYDSELtpAEYSPQLTRRMREAEdmVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSR 494
Cdd:COG3206 243 AALRAQL--GSGPDALPELLQSPV--IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2947031 495 E-EADTLRLKVEELEGERSRLEEE-KRMLEAQLERRALQGDYDQSRT 539
Cdd:COG3206 319 EaELEALQAREASLQAQLAQLEARlAELPELEAELRRLEREVEVARE 365
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
406-620 |
6.49e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 406 ERDGMRAILGSYDSeltpaeYSPQLTRRMREAEDMVQKvhshsAEMEAQ------LSQALEELggqkqRADMLEMELKML 479
Cdd:COG2433 334 ERDALAAALKAYDA------YKNKFERVEKKVPPDVDR-----DEVKARvirglsIEEALEEL-----IEKELPEEEPEA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 480 KSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERraLQGDYDQSRTKvlhmslnptsvARQRLRED 559
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--LERELSEARSE-----------ERREIRKD 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2947031 560 H--SQLQAECERLRgllramerggtvpadleaaaaslpssKEVAELKKQVESAELKNQRLKEV 620
Cdd:COG2433 465 ReiSRLDREIERLE--------------------------RELEEERERIEELKRKLERLKEL 501
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
36-523 |
6.70e-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: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 36 SAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKM---QMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQ 112
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVqehQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 113 LQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGET-INALKGRISELQWSVMDQEMRVKRLESEKQDVQ 191
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKmEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 192 EQLDLQHKKCQEANQKIQELQASQ-----EARADHEQQIKDLEQKLSLQ--------EQDAAIVKNMKSeLVRLPRLERE 258
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQgrlqlQADRHQEHIRARDSLIQSLAtrleldgfERGPFSERQIKN-FHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 259 LEQLREESALREMRETNGLLQEELEGLQ-RKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRfv 337
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK-- 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 338 velQQRELALKDKNSAVTSsargLEKARQQLQEELRQVSGQLleeRKKRETHEALARRLQKRVLLLTKERDGMRAILGSY 417
Cdd:TIGR00606 483 ---AERELSKAEKNSLTET----LKKEVKSLQNEKADLDRKL---RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 418 DSEltpAEYSPQLTRRM------REAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSfL 491
Cdd:TIGR00606 553 KIK---SRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK-L 628
|
490 500 510
....*....|....*....|....*....|..
gi 2947031 492 FSREEADTLRLKVEELEGERSRLEEEKRMLEA 523
Cdd:TIGR00606 629 FDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-592 |
6.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 352 SAVTSSARGLEKARQQL---QEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKErdgmraiLGSYDSELTpaeysp 428
Cdd:COG4942 13 LAAAAQADAAAEAEAELeqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELA------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 429 QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRAdmlemELKMLKSQSSSAEQSFLFS---------REEADT 499
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP-----PLALLLSPEDFLDAVRRLQylkylaparREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 500 LRLKVEELEGERSRLEEEKRMLEAQL-----ERRALQGDYDQSRTKvlhmsLNPTSVARQRLREDHSQLQAECERLRGLL 574
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLaeleeERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 2947031 575 RAMERGGTVPADLEAAAA 592
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-398 |
7.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 45 YQQSMQLEERAEQIRSKSHLIQVER-EKMQMELSHKRARVELERaastsarnyerevdrnQELLTRIRQLQEREAGAEEK 123
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEI----------------SKITARIGELKKEIKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 124 MQEQLERNRQC------------QQNLDAASKRLREKEDSLAQAGETINALKGRISELQwSVMDQEMRVKRL-------- 183
Cdd:PRK03918 428 IEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLkelaeqlk 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 184 ---ESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELE 260
Cdd:PRK03918 507 eleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 261 QLREESALREM----RETNGLLQEELEgLQRKLGRQEKMQETLVGLELENERLLAKLQSwerldqtmgLSIRTPEDLSRF 336
Cdd:PRK03918 587 VEELEERLKELepfyNEYLELKDAEKE-LEREEKELKKLEEELDKAFEELAETEKRLEE---------LRKELEELEKKY 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2947031 337 VVE----LQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQK 398
Cdd:PRK03918 657 SEEeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-660 |
8.02e-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: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 99 EVDRNQELLTRIRQLQEREAGAEEKMqEQLERNRQCQQNLDAASKRLREKEDSLA-----QAGETINALKGRISELqwsv 173
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEEL---- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 174 mdqEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARAdhEQQIKDLEQKLSLQEQDAAIVKNMKSELvRLP 253
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL--EREIERLERELEERERRRARLEALLAAL-GLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 254 RLERELEQLREESALREMRETnglLQEELEGLQRKLGRQEKmqeTLVGLELENERLLAKLQSWER----LDQTMgLSIR- 328
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEA---ALRDLRRELRELEAEIASLERrksnIPARL-LALRd 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 329 --------TPEDLsRFVVELqqreLALKDKNSAVTSSARG-LEKARQQL---QEELRQVSgqlleeRKKRETHeaLARRL 396
Cdd:COG4913 448 alaealglDEAEL-PFVGEL----IEVRPEEERWRGAIERvLGGFALTLlvpPEHYAAAL------RWVNRLH--LRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 397 Q-KRVLLLTKERDGMRAILGSYDSELT--PAEYSPQLTRRMREAEDmVQKVHShsaemEAQLSQ---ALEELGGQKQRAD 470
Cdd:COG4913 515 VyERVRTGLPDPERPRLDPDSLAGKLDfkPHPFRAWLEAELGRRFD-YVCVDS-----PEELRRhprAITRAGQVKGNGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 471 MLEMelkmlKSQSSSAEQSFL-FSREEadtlrlKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRtkvlhmslnpt 549
Cdd:COG4913 589 RHEK-----DDRRRIRSRYVLgFDNRA------KLAALEAELAELEEELAEAEERLEALEAELDALQER----------- 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 550 SVARQRLRE------DHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLpsSKEVAELKKQVESAELKNQRLKEVFQT 623
Cdd:COG4913 647 REALQRLAEyswdeiDVASAEREIAELEAELERLDASSDDLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQ 724
|
570 580 590
....*....|....*....|....*....|....*..
gi 2947031 624 KIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGD 660
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
138-250 |
8.52e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 138 LDAASKRLREKEDSLAQAgetINALKGRISEL----QWSVMDQEM----RVKRLESEKQDVQEQLDLQHKKCQEANQKIQ 209
Cdd:COG0542 395 IDEAAARVRMEIDSKPEE---LDELERRLEQLeiekEALKKEQDEasfeRLAELRDELAELEEELEALKARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2947031 210 ELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELV 250
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
29-240 |
8.82e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 29 SGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQveREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLt 108
Cdd:PRK10246 402 ITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ--KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLA- 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 109 RIRQLQEREAGAE--EKMQEQLERNRQC---------------QQNLDAASKRLREKEDSLAQAGETINALKGRISELQW 171
Cdd:PRK10246 479 DVKTICEQEARIKdlEAQRAQLQAGQPCplcgstshpaveayqALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTK 558
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2947031 172 SVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAA 240
Cdd:PRK10246 559 QLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAA 627
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
157-526 |
9.01e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 157 ETINALKGRISELQWSVMDQEMRVKRLESEKQDVQEQLDLQHKKCQEANQKIQELqasqearadhEQQIKDLEQKLSL-- 234
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL----------EKQLNQLKSEISDln 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 235 QEQDAAIVKNMKSELvrlprLERELEQLREESALREMRETNGLLQEELEGLQRklgrqekmqeTLVGLELENERLLAKLQ 314
Cdd:TIGR04523 302 NQKEQDWNKELKSEL-----KNQEKKLEEIQNQISQNNKIISQLNEQISQLKK----------ELTNSESENSEKQRELE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 315 swERLDQtmglsirtpedlsrfvVELQQRELA-LKDKNSAVTSSARGLEKARQQLQEELRQVSGQLleeRKKRETHEALA 393
Cdd:TIGR04523 367 --EKQNE----------------IEKLKKENQsYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI---KKLQQEKELLE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 394 RRLQKRVLLLTKERDGMrailgsydSELTPAEYSPQLTrrMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLE 473
Cdd:TIGR04523 426 KEIERLKETIIKNNSEI--------KDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2947031 474 MELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLE 526
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
328-488 |
9.83e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 328 RTPEDLSRFVVELQQRELALKDKNSAVTSSArglekARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKER 407
Cdd:PRK10929 72 QVIDNFPKLSAELRQQLNNERDEPRSVPPNM-----STDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2947031 408 DGMRAILGSYDSEL----TPAEYSPQLTRRMREAEDMVQKVHSHSAEMeAQLS----QALEELGGQ--KQRADMLEMELK 477
Cdd:PRK10929 147 TEARRQLNEIERRLqtlgTPNTPLAQAQLTALQAESAALKALVDELEL-AQLSannrQELARLRSElaKKRSQQLDAYLQ 225
|
170
....*....|.
gi 2947031 478 MLKSQSSSAEQ 488
Cdd:PRK10929 226 ALRNQLNSQRQ 236
|
|
| |
