|
Name |
Accession |
Description |
Interval |
E-value |
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
64-624 |
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: 632.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 64 HTTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQ 143
Cdd:pfam05557 103 REVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 144 EQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQ 223
Cdd:pfam05557 183 EQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 224 SWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALAR 303
Cdd:pfam05557 263 SWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 304 RLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEM 383
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLER 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 384 ELKMLKSQSSSAEQSflFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQ 463
Cdd:pfam05557 423 ELQALRQQESLADPS--YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQ 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 464 RLREDHSQLQAECERLRGLLRAMErggtvpADLEAAAASLPSS-----KEVAELKKQVESAELKNQRLKEVFQTKIQEFR 538
Cdd:pfam05557 501 QRKNQLEKLQAEIERLKRLLKKLE------DDLEQVLRLPETTstmnfKEVLDLRKELESAELKNQRLKEVFQAKIQEFR 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 539 KACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLE 618
Cdd:pfam05557 575 DVCYMLTGYQIDITTNSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLIDLHLAAQKSIPAFLSALTLE 654
|
....*.
gi 751557638 619 LFSRQT 624
Cdd:pfam05557 655 LFSRQT 660
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-526 |
7.64e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQasQEARADHEQQIKDLEQKLSLQEQD 146
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 147 AAIVKNMKSELVRLPRLERELKQLREESAHLREMRETngLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWE 226
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEE--LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 227 RLDQTMGLSIRTPEDLSRFVVELQQRELALkdKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALA---- 302
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaal 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 303 ------------RRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQkvhSHSAEMEAQLSQALEE 370
Cdd:COG1196 545 aaalqnivveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA---SDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 371 LGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKV 450
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751557638 451 LHMSLNPTSVARQRLREDHSQLQAECERLRGLLR--AMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRL 526
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREelLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
84-528 |
1.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 84 QEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQ----ASQEARADHEQQIKDLEQKLSLQEQDAaivknmKSELVR 159
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELEleleEAQAEEYELLAELARLEQDIARLEERR------RELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 160 LPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLgrQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTP 239
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 240 EDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGM 319
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 320 RAILGSYDSELTPAEYSPQLTRRMREAED--------------------MVQKVHSHSAEMEAQLSQALEELGGQKQRAD 379
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEgflegvkaalllaglrglagAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 380 MLEMElkmlksqssSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTS 459
Cdd:COG1196 556 DEVAA---------AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751557638 460 VARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKE 528
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-539 |
2.45e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 248 ELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYD 327
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 328 SELTpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMEL--------------KMLKSQSS 393
Cdd:TIGR02168 761 AEIE------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 394 SAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLE------------RRALQGDYDQSRTKVLHMSLNPTSV- 460
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallnerasleeaLALLRSELEELSEELRELESKRSELr 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 461 -ARQRLREDHSQLQAECERLRGLL-----RAMERGGTVPADLEAAAASLPSskEVAELKKQVESAELKNQRLKEVFQTKI 534
Cdd:TIGR02168 915 rELEELREKLAQLELRLEGLEVRIdnlqeRLSEEYSLTLEEAEALENKIED--DEEEARRRLKRLENKIKELGPVNLAAI 992
|
....*
gi 751557638 535 QEFRK 539
Cdd:TIGR02168 993 EEYEE 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-435 |
2.49e-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: 67.00 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 80 SVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELqasQEARADHEQQIKDLEQKLSLQEQDAAIVKN-MKSELV 158
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL---EEELEQLRKELEELSRQISALRKDLARLEAeVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 159 RLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLgrQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRT 238
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 239 PEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDG 318
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 319 MRAILGsydseltpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELggqkqrADMLEMELKMLKSQSSSAEQS 398
Cdd:TIGR02168 906 LESKRS-------------ELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLEEAEALENKIEDD 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 751557638 399 FLFSREEADTLRLKVEEL-------EGERSRLEEEKRMLEAQLE 435
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-520 |
3.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 163 LERELKQLREESAHLREMREtnglLQEELEGLQRKL---------GRQEKMQETLVGLELENERLLAKLQSWERLDQTMG 233
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE----LKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 234 LSIrtpEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLT 313
Cdd:COG1196 274 LEL---EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 314 KERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSS 393
Cdd:COG1196 351 EELEEAEAELAEAEEALL------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 394 SAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQ 473
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 751557638 474 A------ECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAE 520
Cdd:COG1196 505 GflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-525 |
6.78e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 69 ALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQklslqeqdaa 148
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE---------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 149 iVKNMKSEL-VRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLvglelenERLLAKLQSWER 227
Cdd:PRK03918 305 -YLDELREIeKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-------EEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 228 LDQTmgLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQ---EELRQVSG-------QLLEERKKR-- 295
Cdd:PRK03918 377 LKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGkcpvcgrELTEEHRKEll 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 296 ETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEmeaQLSQALEELGGQK 375
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 376 QRADMLEMELKMLKSQSSSAEQsflfsreeadtLRLKVEELEGERSRLEEEKRMLEAQLERRALQG-DYDQSRTKvlhmS 454
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEE-----------LKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLK----E 596
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 751557638 455 LNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLpsSKEVAELKKQVESAELKNQR 525
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL--RKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-535 |
8.64e-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: 65.46 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 255 ALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAE 334
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 335 YSP-QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKV 413
Cdd:TIGR02168 316 RQLeELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 414 EELEGERSRLEEEKRMLEAQLER-----RALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMER 488
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 751557638 489 GGTVPADLEAAAASlpsskEVAELKKQVESAELKNQRLKEVFQTKIQ 535
Cdd:TIGR02168 476 ALDAAERELAQLQA-----RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-436 |
3.25e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 84 QEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQAsqeARADHEQQIKDLEQKLSLQEQDAAIVKNMKSEL-VRLPR 162
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ---ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 163 LERELKQLREESAHLR----EMRETNGLLQEELEGLQRKLGRQ--EKMQETLVGLELENERLLAKLQSwerLDQTMGLSI 236
Cdd:TIGR02169 749 LEQEIENVKSELKELEarieELEEDLHKLEEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLRE---IEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 237 RTPEDLSRFVVELQQRELALKDKnsavtssarglEKARQQLQEELRQVSGQLLEERKKretHEALARRLQKRVLLLTKER 316
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQ-----------IKSIEKEIENLNGKKEELEEELEE---LEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 317 DGMRAILGsydseltpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELG-------------GQKQRADMLEM 383
Cdd:TIGR02169 892 DELEAQLR-------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiedpkgedeeipEEELSLEDVQA 958
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 751557638 384 ELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLER 436
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
83-487 |
3.56e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 83 DQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRlpR 162
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--A 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 163 LERELKQLREESAHLREMRETNGLLQEELEGLQRKL--GRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPE 240
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 241 DLSRFVVELQQR-----ELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEA------LARRLQKRV 309
Cdd:COG1196 510 VKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpldKIRARAALA 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 310 LLLTKERDGMRAILGSYDSELTPAEYSP-------------QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQ 376
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVlgdtllgrtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 377 RADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLN 456
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
410 420 430
....*....|....*....|....*....|.
gi 751557638 457 PTSVARQRLREDHSQLQAECERLRGLLRAME 487
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-417 |
5.21e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 73 RISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQ-EANQKIQELQASQEARADHEQQIKDLEQKLS-LQEQDAAIV 150
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEkLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 151 KNMKSELVRLPRLERELKQLREESAhlREMRETNGLLQEELEGLQR----KLGRQEKMQETLVGLELENERLLAKLQSWE 226
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 227 rldqtmglsiRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQ 306
Cdd:TIGR02169 343 ----------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 307 KRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELK 386
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKIN------ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350
....*....|....*....|....*....|.
gi 751557638 387 MLKSQSSSAEQSFLFSREEADTLRLKVEELE 417
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-331 |
2.24e-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: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEAradHEQQIKDLE-QKLSLQEQ 145
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA---LANEISRLEqQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 146 DAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSW 225
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEE---LKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 226 ERLDQTMGLSIRtpEDLSRFVVELQQRELALKDKNSAVTSSARGLEKA-RQQLQEELRQVSGQLLEERKKRETHEALARR 304
Cdd:TIGR02168 388 VAQLELQIASLN--NEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260
....*....|....*....|....*..
gi 751557638 305 LQKRVLLLTKERDGMRAILGSYDSELT 331
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-324 |
3.35e-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: 60.07 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 65 TTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEA----RADHEQQIKDLEQKL 140
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 141 SLQEQDAAIVKNMKSELvrLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKL----GRQEKMQETLVGLELENE 216
Cdd:TIGR02168 333 DELAEELAELEEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqleLQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 217 RLLAKLQSW--ERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKK 294
Cdd:TIGR02168 411 RLEDRRERLqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
250 260 270
....*....|....*....|....*....|...
gi 751557638 295 RETHEALARRLQKR---VLLLTKERDGMRAILG 324
Cdd:TIGR02168 491 LDSLERLQENLEGFsegVKALLKNQSGLSGILG 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-528 |
1.72e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 137 EQKLSLQEQDAAIVKNMKSELV-RLPRLERELKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLVGLELEN 215
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDLHeRLNGLESELAELDEEIERYEEQREQ---ARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 216 ERLLAKLQSWErldqtmglsiRTPEDLSRFVVELQQRELALKDKNSAVTS-------SARGLEKARQQLQEELRQVSGQL 288
Cdd:PRK02224 261 EDLRETIAETE----------REREELAEEVRDLRERLEELEEERDDLLAeaglddaDAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 289 LEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYS--------PQLTRRMREAEDMVQKVHSHSAEM 360
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedrreeiEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 361 EAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQ---------------------SFLFSREEADTLRLKVEELEGE 419
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 420 RSRLE------EEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLL--------RA 485
Cdd:PRK02224 491 VEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaeaeeeaeEA 570
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 751557638 486 MERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKE 528
Cdd:PRK02224 571 REEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-440 |
6.64e-08 |
|
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: 55.89 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 70 LKGRISELQwSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKI-QELQASQEARADHEQQIKDLEQklSLQEQDAA 148
Cdd:pfam15921 435 LKAMKSECQ-GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVvEELTAKKMTLESSERTVSDLTA--SLQEKERA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 149 IvKNMKSELVRL-PRLE---RELKQLREESAHLR-----------EMRETNG---LLQEELEGLQRKLGRQEK----MQE 206
Cdd:pfam15921 512 I-EATNAEITKLrSRVDlklQELQHLKNEGDHLRnvqtecealklQMAEKDKvieILRQQIENMTQLVGQHGRtagaMQV 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 207 TLVGLELE-NERLLaKLQSWERLDQTMGLSIRtpeDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVS 285
Cdd:pfam15921 591 EKAQLEKEiNDRRL-ELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 286 GQLleeRKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELtpaEYSPQLTRRMREAEDMVQKVhshSAEMEAQLS 365
Cdd:pfam15921 667 NEL---NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL---EQTRNTLKSMEGSDGHAMKV---AMGMQKQIT 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 366 QALEELGGQKQRADMLE-------MELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRA 438
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
..
gi 751557638 439 LQ 440
Cdd:pfam15921 818 LQ 819
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
119-321 |
8.22e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 119 LQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVR-LPRLERELKQLREEsahLREMRETNGLLQEELEGLQRk 197
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKqLAALERRIAALARR---IRALEQELAALEAELAELEK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 198 lgRQEKMQETLVGLELENERLLAKLQSWERLDQTMGL--------SIRTPEDLSRFVVELQQRELALKDKNSAVTSSARG 269
Cdd:COG4942 91 --EIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 751557638 270 LEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRA 321
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
74-536 |
2.54e-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: 53.97 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 74 ISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEAN----QKIQELQAS--------QEARADHEQQIKDLEQKLS 141
Cdd:pfam15921 273 ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTvsqlrselREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 142 L---------------QEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGL----LQEELEGLQRKLGRQE 202
Cdd:pfam15921 353 LanseltearterdqfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSItidhLRRELDDRNMEVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 203 KMQETLVG-LELENERLLAKLQSW-ERLDQTMGLSIR---TPEDLSRFVVELQQRELALKdknsavtSSARGLEKARQQL 277
Cdd:pfam15921 433 ALLKAMKSeCQGQMERQMAAIQGKnESLEKVSSLTAQlesTKEMLRKVVEELTAKKMTLE-------SSERTVSDLTASL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 278 QEELRQVSGQLLEERKKRETHEALARRLQKrvllLTKERDGMRAILGSYDS-ELTPAEYSPQLTRRMREAEDMVQKVHSH 356
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDLKLQELQH----LKNEGDHLRNVQTECEAlKLQMAEKDKVIEILRQQIENMTQLVGQH 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 357 ---SAEMEAQLSQALEELGGQKqradmLEM-ELKMLKSQSSSaeqsflfsreeadtlrlKVEELEGERSRLEEEK-RMLE 431
Cdd:pfam15921 582 grtAGAMQVEKAQLEKEINDRR-----LELqEFKILKDKKDA-----------------KIRELEARVSDLELEKvKLVN 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 432 AQLERRALQGDYDQSRTKVLH------MSLNPTS----VARQRLREDHSQL--------------QAECERLRGLLRAME 487
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNevktsrNELNSLSedyeVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLKSME 719
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 751557638 488 rggtvPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQE 536
Cdd:pfam15921 720 -----GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-540 |
2.98e-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: 53.91 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 275 QQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVH 354
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY------ALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 355 SHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEqsflfsrEEADTLRLKVEELEGERSRLEEEKRMLEAQL 434
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 435 ERraLQGDYDQSRTKVLhmSLNPTsvaRQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKK 514
Cdd:TIGR02168 382 ET--LRSKVAQLELQIA--SLNNE---IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
250 260
....*....|....*....|....*.
gi 751557638 515 QVESAELKNQRLKEVFQTKIQEFRKA 540
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAA 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-539 |
3.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 86 MRVKRLESEKQEL-----------QEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDaaivKNMK 154
Cdd:COG4717 46 MLLERLEKEADELfkpqgrkpelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE----LEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 155 SELVRLPRLERELKQLREESAHlremretnglLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLdqtmgL 234
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAE----------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ-----L 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 235 SIRTPEDLSRFVVELQQRELALKDknsavtssargLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTk 314
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAE-----------LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 315 eRDGMRAILGSYDSELTPAEYSP----------------------QLTRRMREAEDMVQKVHSHSAEMEAQLSQ------ 366
Cdd:COG4717 255 -AAALLALLGLGGSLLSLILTIAgvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAAlglppd 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 367 --------ALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSR---EEADTLRLKVEELEgERSRLEEEKRMLEAQLE 435
Cdd:COG4717 334 lspeelleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAE-EYQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 436 RRA--LQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVpADLEAAAASLpsSKEVAELK 513
Cdd:COG4717 413 ELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-AELLQELEEL--KAELRELA 489
|
490 500
....*....|....*....|....*.
gi 751557638 514 KQVESAELknqrLKEVFQTKIQEFRK 539
Cdd:COG4717 490 EEWAALKL----ALELLEEAREEYRE 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-537 |
4.72e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 171 REESAHLREMRETNGLLQEELEGLQRKLGRQEK-MQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVEL 249
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 250 QQRELALKDKNSAVTSSARGLEKARQQLQEELRQvsgqlLEERKKRETHEALARRLQKrvllLTKERDGMRAILGSYDSE 329
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALND-----LEARLSHSRIPEIQAELSK----LEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 330 LTPAEYSPQLtrrmreAEDMVQKVHSHSAEMEAQLSQaleelggQKQRADMLEMELKMLKsqsssaeqsflfsrEEADTL 409
Cdd:TIGR02169 821 LNRLTLEKEY------LEKEIQELQEQRIDLKEQIKS-------IEKEIENLNGKKEELE--------------EELEEL 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 410 RLKVEELEGERSRLEEEKRMLEAQLerRALQGDYDQSRTKVlhmslnptsvarQRLREDHSQLQAECERLRGLLRAMERg 489
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQL--RELERKIEELEAQI------------EKKRKRLSELKAKLEALEEELSEIED- 938
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 751557638 490 gTVPADLEAAAASLPSSKevaeLKKQVESAELKNQRLKEVFQTKIQEF 537
Cdd:TIGR02169 939 -PKGEDEEIPEEELSLED----VQAELQRVEEEIRALEPVNMLAIQEY 981
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
66-437 |
5.17e-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: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQ-----------------LDLQHKKCQEANQK-IQELQASQEARA 127
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmaaiqgkneslekvssLTAQLESTKEMLRKvVEELTAKKMTLE 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 128 DHEQQIKDLEQklSLQEQDAAIvKNMKSELVRL-PRLE---RELKQLREESAHLR-----------EMRETNG---LLQE 189
Cdd:pfam15921 493 SSERTVSDLTA--SLQEKERAI-EATNAEITKLrSRVDlklQELQHLKNEGDHLRnvqtecealklQMAEKDKvieILRQ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 190 ELEGLQRKLGRQEK----MQETLVGLELE-NERLLaKLQSWERLDQTMGLSIRtpeDLSRFVVELQQRELALKDKNSAVT 264
Cdd:pfam15921 570 QIENMTQLVGQHGRtagaMQVEKAQLEKEiNDRRL-ELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERL 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 265 SSARGLEKARQQLQEELRQVSGQLleeRKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELtpaEYSPQLTRRMR 344
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNEL---NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL---EQTRNTLKSME 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 345 EAEDMVQKVhshSAEMEAQLSqaleelgGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLE 424
Cdd:pfam15921 720 GSDGHAMKV---AMGMQKQIT-------AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
410
....*....|...
gi 751557638 425 EEKRMLEAQlERR 437
Cdd:pfam15921 790 GELEVLRSQ-ERR 801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-551 |
9.70e-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: 51.98 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 64 HTTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQEL-QASQEARADHEQQIKDLEQKLSL 142
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELeSRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 143 QEQDAAIVKNMKSelvRLPRLERELKQLREESAHLREMRETNgllqeELEGLQRKLGRQEKMQETLVGLELENERLLAKL 222
Cdd:TIGR02168 395 IASLNNEIERLEA---RLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 223 QSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAvtsSARGLEKARQQLqEELRQVSGQLLEERKKRET--HEA 300
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE---GVKALLKNQSGL-SGILGVLSELISVDEGYEAaiEAA 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 301 LARRLQKRVL-----------LLTKERDGMRAILgsydsELT--PAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQA 367
Cdd:TIGR02168 543 LGGRLQAVVVenlnaakkaiaFLKQNELGRVTFL-----PLDsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 368 LEELGGQKQRADMLEMELKMLKS-----------------------QSSSAEQSFLFSREEADTLRLKVEELEGERSRLE 424
Cdd:TIGR02168 618 LSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 425 EEKRMLEAQL-----ERRALQGDYDQSRTKV--LHMSLNPTSVARQRLREDHSQLQAECERLRG--LLRAMERGGTVPAD 495
Cdd:TIGR02168 698 KALAELRKELeeleeELEQLRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELEAeiEELEERLEEAEEEL 777
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 751557638 496 LEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDI 551
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
270-499 |
1.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 270 LEKARQQLQ--EELRQVSGQLLEERKKRETHEALARRL-----QKRVLLLTKERDGMRAILGSYDSELTPAEyspQLTRR 342
Cdd:COG4913 244 LEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLE---ARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 343 MREAEDMVQKVHSHS-----AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRlkvEELE 417
Cdd:COG4913 321 LREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL---EALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 418 GERSRLEEEKRMLEAQLerralqgdydqsrtkvlhmslnptsvarQRLREDHSQLQAECERLRGllrameRGGTVPADLE 497
Cdd:COG4913 398 EELEALEEALAEAEAAL----------------------------RDLRRELRELEAEIASLER------RKSNIPARLL 443
|
..
gi 751557638 498 AA 499
Cdd:COG4913 444 AL 445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
67-488 |
2.22e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQ--WSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQE 144
Cdd:COG4717 104 LEELEAELEELReeLEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 145 QDAAIvknmkSELVRLPRLERELKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLVglelENERLLAKLQS 224
Cdd:COG4717 184 EQLSL-----ATEEELQDLAEELEELQQRLAELEEELEE---AQEELEELEEELEQLENELEAAA----LEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 225 WERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARR 304
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 305 LQKRVLLLTKERDGMRAILgSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEME 384
Cdd:COG4717 332 PDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 385 LKMLKSQSSSAEQSFLFS--REEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKvlhmslnptsvaR 462
Cdd:COG4717 411 LEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQE------------L 478
|
410 420
....*....|....*....|....*.
gi 751557638 463 QRLREDHSQLQAECERLRGLLRAMER 488
Cdd:COG4717 479 EELKAELRELAEEWAALKLALELLEE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-280 |
2.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMRVKRLESEKQELQEQLdlqhkkcqEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQD 146
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERR--------EALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 147 AAIVKNMKSELVrlpRLERELKQLREEsahLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKlqswE 226
Cdd:COG4913 684 SDDLAALEEQLE---ELEAELEELEEE---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE----E 753
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 751557638 227 RLDQTMGlsirtPEDLSRFVVELQQRelaLKDKNSAVTSSARGLEKARQQLQEE 280
Cdd:COG4913 754 RFAAALG-----DAVERELRENLEER---IDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-288 |
2.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 87 RVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQdaaivknmkselvrLPRLERE 166
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE--------------IAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 167 LKQLREESAHLREMRETNGLLQEELEGLQRKLgrqEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEdlsRFV 246
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEEL---DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL---RAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 751557638 247 VELQQRELALKDKNSAVtssARGLEKARQQLQEELRQVSGQL 288
Cdd:COG4913 751 LEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEEL 789
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
83-439 |
4.40e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 83 DQEMRVKRLESEKQELQEQLDLQHKK-CQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQdaaivkNMKSELVRLP 161
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTiCQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE------LLRTEQQRLE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 162 RLERELK----QLREESAHLREMRETNGLLQEELEGLQRKLGRQ----------EKMQETLVGLELENERLL-AKLQSWE 226
Cdd:pfam05483 374 KNEDQLKiitmELQKKSSELEEMTKFKNNKEVELEELKKILAEDeklldekkqfEKIAEELKGKEQELIFLLqAREKEIH 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 227 RLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQ 306
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 307 KRVLLLTKERDGMRAILGSYDSELTPA--EYSPQLTR---RMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADML 381
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKgdEVKCKLDKseeNARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 751557638 382 EMELKMLKSQSSSAEQSFLFSREEADTLRLkveELEGERSRLEEEKRMLEAQLERRAL 439
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKVNKLEL---ELASAKQKFEEIIDNYQKEIEDKKI 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-316 |
5.58e-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: 49.68 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMR-----VKRLESEKQELQEQLDLQHKKCQEANQKIQELqasQEARADHEQQIKDLEQKls 141
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELSkleeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIEKE-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 142 lQEQDAAIVKNMKSElvrLPRLERELKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETlvgLELENERLLAK 221
Cdd:TIGR02169 856 -IENLNGKKEELEEE---LEELEAALRDLESRLGDLKKERDE---LEAQLRELERKIEELEAQIEK---KRKRLSELKAK 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 222 LQSWERLDQTMGLSIRTPEDLSRFVVELQQrelaLKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEAL 301
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEEELSLED----VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
250
....*....|....*
gi 751557638 302 ARRLQKRVLLLTKER 316
Cdd:TIGR02169 1002 RKAILERIEEYEKKK 1016
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
74-397 |
7.64e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 74 ISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAaivKNM 153
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEE---RKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 154 KSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGlQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMG 233
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 234 LSIRTPEDLSRFVVELQQRElalkdknsavtssaRGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQK-----R 308
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQ--------------QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 309 VLLLTKERDgmRAILGSYDSELTPAEYSPQlTRRMREAEDMVQKVHSHSAEMEAQLSQALEElggqKQRADMLEMELKML 388
Cdd:pfam17380 506 QAMIEEERK--RKLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEE----RSRLEAMEREREMM 578
|
....*....
gi 751557638 389 KSQSSSAEQ 397
Cdd:pfam17380 579 RQIVESEKA 587
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
96-309 |
7.85e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.92 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 96 QELQEQLDLQHKKCQEANQKIQELQASQEARADHEQ----QIKDLEqKLSLQE--------------------QDAAIVK 151
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDllrfQLEELE-AAALQPgeeeeleeerrrlsnaeklrEALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 152 NMKSE-----LVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQekmqetLVGLELENERLlAKLQswE 226
Cdd:COG0497 233 EALSGgeggaLDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRY------LDSLEFDPERL-EEVE--E 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 227 RLDQTMGLSIR---TPEDLSRFVVELQQRELALKDKNSAVtssaRGLEKARQQLQEELRQVSGQLLEERKKretheaLAR 303
Cdd:COG0497 304 RLALLRRLARKygvTVEELLAYAEELRAELAELENSDERL----EELEAELAEAEAELLEAAEKLSAARKK------AAK 373
|
....*.
gi 751557638 304 RLQKRV 309
Cdd:COG0497 374 KLEKAV 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
94-569 |
8.99e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 94 EKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQikdleQKLSLQEQdaaivknmkselvRLPRLERELKQLREE 173
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEA-------------ELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 174 SAHLREMRETnglLQEELEGLQRKL-----GRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSI-RTPEDLSRFVV 247
Cdd:COG4913 311 LERLEARLDA---LREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 248 ELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQL--LEERKKR------ETHEALARRLQKR----------V 309
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIasLERRKSNiparllALRDALAEALGLDeaelpfvgelI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 310 LLLTKERDGMRAI---LGSYD-SELTPAEYSPQLTR-------RMR------------------EAEDMVQKV----HSH 356
Cdd:COG4913 468 EVRPEEERWRGAIervLGGFAlTLLVPPEHYAAALRwvnrlhlRGRlvyervrtglpdperprlDPDSLAGKLdfkpHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 357 SAEMEAQLSQA--------LEEL---------GGQ-KQRADMLEMelkmlKSQSSSAEQSFL-FSREEadtlrlKVEELE 417
Cdd:COG4913 548 RAWLEAELGRRfdyvcvdsPEELrrhpraitrAGQvKGNGTRHEK-----DDRRRIRSRYVLgFDNRA------KLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 418 GERSRLEEEKRMLEAQLERRALQGDYDQSRtkvlhmslnptSVARQRLRE------DHSQLQAECERLRGLLRAMERGGT 491
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQER-----------REALQRLAEyswdeiDVASAEREIAELEAELERLDASSD 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 751557638 492 VPADLEAAAASLpsSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGD 569
Cdd:COG4913 686 DLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-228 |
1.21e-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: 48.53 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEaraDHEQQIKDLEQKLS-LQE 144
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE---KKRKRLSELKAKLEaLEE 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 145 QDAAI---VKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETlvgLELENERLLAK 221
Cdd:TIGR02169 932 ELSEIedpKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK---LEEERKAILER 1008
|
....*..
gi 751557638 222 LQSWERL 228
Cdd:TIGR02169 1009 IEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
84-478 |
1.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 84 QEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVR-LPR 162
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 163 LERELKQLREESAHLREMRETNGLLQEeleglQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQtmglsIRTPEDL 242
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADE-----AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 243 SRF--VVELQQRELALKDKNSAVTSS--ARGLEKARQQLQEELRQVSGQL-LEERKKRETHEALARRLQKRvlllTKERD 317
Cdd:PTZ00121 1558 KKAeeKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKA----EEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 318 GMRAILGSYDSELTPAEyspqltrRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQ 397
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAE-------ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 398 SFLFSREE---ADTLR-------LKVEELEGERsrlEEEKRMLEA----QLERRALQGDYDQSRTKVLHMSLNPTSVARQ 463
Cdd:PTZ00121 1707 LKKKEAEEkkkAEELKkaeeenkIKAEEAKKEA---EEDKKKAEEakkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
410
....*....|....*
gi 751557638 464 RLREDHSQLQAECER 478
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDK 1798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
66-316 |
2.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELqasqearadhEQQIKDLEQKLSlqeq 145
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------EQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 146 daaivknmkselvrlpRLERELKQLREESAHLREmretngLLQEELEGLQRkLGRQEKMQETLVGLE-LENERLLAKLQS 224
Cdd:COG4942 87 ----------------ELEKEIAELRAELEAQKE------ELAELLRALYR-LGRQPPLALLLSPEDfLDAVRRLQYLKY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 225 WERLDQTMGLSIR-TPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALAR 303
Cdd:COG4942 144 LAPARREQAEELRaDLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|...
gi 751557638 304 RLQKRVLLLTKER 316
Cdd:COG4942 224 ELEALIARLEAEA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-424 |
2.44e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 69 ALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAA 148
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 149 IVKNMK---------SELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGL-QRKLGRQEKMQETLVGLELENERL 218
Cdd:COG1196 512 AALLLAglrglagavAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKIRARAALAAA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 219 LAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETH 298
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 299 EALARRLQKRVLLLTKERDGMRAilgsydseltpaeyspqLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRA 378
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELE-----------------LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 751557638 379 DMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLE 424
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
111-450 |
3.01e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 111 EANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVrlpRLERELKQLREESAHLREMRETNGLLQEE 190
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE---LEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 191 LEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDqtmGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGL 270
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 271 EKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMV 350
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 351 QKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRML 430
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340
....*....|....*....|
gi 751557638 431 EAQLERRALQGDYDQSRTKV 450
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKAR 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-488 |
3.94e-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: 46.98 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 248 ELQQRE--LALKDKNSAVTSSARgLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERD-GMRAILG 324
Cdd:TIGR02169 219 EKREYEgyELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 325 SYDSELTPAEYS-PQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLK-------SQSSSAE 396
Cdd:TIGR02169 298 ELEAEIASLERSiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 397 QSFLFSREEADTLRLKVE-------ELEGERSRLEEEKRMLEAQLE--RRALQGDYD-----QSRTKVLHMSLNPTSVAR 462
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEklkreinELKRELDRLQEELQRLSEELAdlNAAIAGIEAkinelEEEKEDKALEIKKQEWKL 457
|
250 260
....*....|....*....|....*.
gi 751557638 463 QRLREDHSQLQAECERLRGLLRAMER 488
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEK 483
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
272-435 |
5.40e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 272 KARQQLQEELRQVSGQLL--------EERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYS------- 336
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIarkqnkydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKieqfqkv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 337 ----------PQLTRRMREAEDMVQKVHSHSAEMEAQLSQ---ALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSR 403
Cdd:PHA02562 278 ikmyekggvcPTCTQQISEGPDRITKIKDKLKELQHSLEKldtAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180 190
....*....|....*....|....*....|..
gi 751557638 404 EEADTLRLKVEELEGERSRLEEEKRMLEAQLE 435
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-222 |
5.84e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 65 TTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHkkcQEANQKIQELQASQEARADHEQQIKDLEQKL-SLQ 143
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIeELS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 144 EQDAAIVKNMKSELVRLPRLERELKQLREE------------------SAHLREMRETNGLLQEELEGLQRKLgrqEKMQ 205
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNErasleealallrseleelSEELRELESKRSELRRELEELREKL---AQLE 928
|
170
....*....|....*..
gi 751557638 206 ETLVGLELENERLLAKL 222
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERL 945
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
66-474 |
5.87e-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: 46.26 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLqhkkcqeanqKIQELQaSQEARADHEQQIKDLEQKLSLQ-- 143
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL----------KLQELQ-HLKNEGDHLRNVQTECEALKLQma 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 144 EQDAAI------VKNMK-----------SELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLgRQEKMQE 206
Cdd:pfam15921 559 EKDKVIeilrqqIENMTqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKL 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 207 TLVGleleNERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSG 286
Cdd:pfam15921 638 VNAG----SERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 287 QLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLtrrMREAEDMVQKVHSHSAEMEAQLSQ 366
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF---LKEEKNKLSQELSTVATEKNKMAG 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 367 ALEELGGQKQR--ADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKveelegersrleeekrmLEAQLERRALQGDYD 444
Cdd:pfam15921 791 ELEVLRSQERRlkEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK-----------------LQHTLDVKELQGPGY 853
|
410 420 430
....*....|....*....|....*....|
gi 751557638 445 QSRTKVLHMSLNPTSVARQRLREDHSQLQA 474
Cdd:pfam15921 854 TSNSSMKPRLLQPASFTRTHSNVPSSQSTA 883
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-513 |
7.50e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 137 EQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREmrETNGLLQEELEGLQRKLGRQEKMQETLVGLELENE 216
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 217 RLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQ-QLQEELRQVSGQLLEERKKR 295
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 296 ETHEALARRLQKRVLLLTKERDgmRAILGSYDSELTPAEYSPQLTRRMREAEDMVQK-VHSHSAEMEAQLSQALEELGGQ 374
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELK--KEKEEIEELEKELKELEIKREAEEEEEEELEKLqEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 375 KQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEgersRLEEEKRMLEAQLERRALQGDYDQSRTKVLHM- 453
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE----ILEEEEESIELKQGKLTEEKEELEKQELKLLKd 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751557638 454 --SLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELK 513
Cdd:pfam02463 464 elELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII 525
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
136-499 |
8.16e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 136 LEQKLSLQEQDAAIVKNMKSElvRLPRLERE-LKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLVGLELE 214
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQE--KFEKMEQErLRQEKEEKAREVERRRK---LEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 215 NERLLAKLQSWER-------LDQTMGLSIRTPEDLSRFVVELQQrelalkdKNSAVTSSARGLEKARQQLQEELRQVSGQ 287
Cdd:pfam17380 346 RERELERIRQEERkreleriRQEEIAMEISRMRELERLQMERQQ-------KNERVRQELEAARKVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 288 LLEERKKRETHEAlARRLQKRVLLLTKERdgmrailgsydseltpaeyspQLTRRMREAEDMVQKVHSHSAEMEAQLSQA 367
Cdd:pfam17380 419 KVEMEQIRAEQEE-ARQREVRRLEEERAR---------------------EMERVRLEEQERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 368 LEELGGQKQRADMLEMELKMLKSQSSSAEQSFLfsrEEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSR 447
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRR 553
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 751557638 448 TKVLHMslnptsvarqRLREDHSQLQAeCERLRGLLRAMERGGTVPADLEAA 499
Cdd:pfam17380 554 IQEQMR----------KATEERSRLEA-MEREREMMRQIVESEKARAEYEAT 594
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
89-556 |
9.44e-05 |
|
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: 45.73 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 89 KRLESEKQELQEQLDLQHKKCQ----EANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLE 164
Cdd:TIGR00618 201 LRSQLLTLCTPCMPDTYHERKQvlekELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 165 ---------RELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERldQTMGLS 235
Cdd:TIGR00618 281 etqerinraRKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS--QEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 236 IRTPEDLSRFVV-----ELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVL 310
Cdd:TIGR00618 359 DAHEVATSIREIscqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 311 LLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQkqradmlemELKMLKS 390
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE---------PCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 391 QSSSAEQSFLFSREEADTLRlkVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHS 470
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRR--MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 471 QLQAECERLRGLLRAMERggtvpadleaAAASLPSSKEVAELKKQVesaELKNQRLKEVFQTKIQEFRKACYTLTGYQID 550
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSE----------AEDMLACEQHALLRKLQP---EQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
....*.
gi 751557638 551 ITTENQ 556
Cdd:TIGR00618 655 LTQERV 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-215 |
1.22e-04 |
|
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: 45.43 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 65 TTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQAS----QEARADHEQQIKDL-EQK 139
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieelEELIEELESELEALlNER 882
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751557638 140 LSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLVGLELEN 215
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ---LELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
82-480 |
1.88e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 82 MDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEAR----ADHEQQIKDLEQKL----SLQEQDAAIvKNM 153
Cdd:PRK10246 415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRnaalNEMRQRYKEKTQQLadvkTICEQEARI-KDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 154 KSELVRLP--------------------------------RLERELKQLREESAHLRemretngllqEELEGLQRKLGRQ 201
Cdd:PRK10246 494 EAQRAQLQagqpcplcgstshpaveayqalepgvnqsrldALEKEVKKLGEEGAALR----------GQLDALTKQLQRD 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 202 EKMQETLvgleLENERLLAklQSWERLDQTMGLSIRTPEDLSRFVVELQQRE-------------LALKDKNSAVTSSAR 268
Cdd:PRK10246 564 ESEAQSL----RQEEQALT--QQWQAVCASLNITLQPQDDIQPWLDAQEEHErqlrllsqrhelqGQIAAHNQQIIQYQQ 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 269 GLEKARQQLQEELRQVSGQLLEERKK------RETHEALARRLQKRVLLLTKERDGMRAILGSY-DSELTPAEYSPQLTR 341
Cdd:PRK10246 638 QIEQRQQQLLTALAGYALTLPQEDEEaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLpQSDDLPHSEETVALD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 342 RMREAEDMVQKVHSHSAEMEAQLSQaleelggQKQRADMLEmelkmlkSQSSSAEQSFLFSREEADTLRLKVEElegERS 421
Cdd:PRK10246 718 NWRQVHEQCLSLHSQLQTLQQQDVL-------EAQRLQKAQ-------AQFDTALQASVFDDQQAFLAALLDEE---TLT 780
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751557638 422 RLEEEKRMLEAQLER-RALQGDYDQSRTKVLHM---SLNPTSVARQRlredHSQLQAECERLR 480
Cdd:PRK10246 781 QLEQLKQNLENQRQQaQTLVTQTAQALAQHQQHrpdGLDLTVTVEQI----QQELAQLAQQLR 839
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
73-204 |
1.94e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 73 RISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSlqeqdaaivkn 152
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIE----------- 475
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 751557638 153 mkselvrlpRLERELKQLREESAHLREmretnglLQEELEGLQRKLGRQEKM 204
Cdd:COG2433 476 ---------RLERELEEERERIEELKR-------KLERLKELWKLEHSGELV 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
87-445 |
2.00e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 87 RVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEAR---------ADHEQQIKDLEQKLS-----LQEQDAAIVK- 151
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInrarkaaplAAHIKAVTQIEQQAQrihteLQSKMRSRAKl 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 152 -----NMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWE 226
Cdd:TIGR00618 327 lmkraAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 227 RLDQTMGLSIRTPEDL------SRFVVELQQRELALKDKNSAVTSSARGLEKARQQ--------LQEELRQVSGQLLEER 292
Cdd:TIGR00618 407 REQATIDTRTSAFRDLqgqlahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQesaqslkeREQQLQTKEQIHLQET 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 293 KKRETHEALARRLQKRVLLLTKErdgmraiLGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELG 372
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGS-------CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 751557638 373 GQKQRADMLEMELKMLKSQSSSaeqsflfSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQ 445
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNR-------SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
105-222 |
2.09e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 105 QHKKCQEANQKI----QELQASQEARADHEQQIKDLEQKLS-LQEQDAAIVKNMKSELVRLPRLERELKQLREEsahLRE 179
Cdd:pfam08614 48 QSASIQSLEQLLaqlrEELAELYRSRGELAQRLVDLNEELQeLEKKLREDERRLAALEAERAQLEEKLKDREEE---LRE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 751557638 180 MRETNGLLQEELEGLQRKLGRQEkmqETLVGLELENERLLAKL 222
Cdd:pfam08614 125 KRKLNQDLQDELVALQLQLNMAE---EKLRKLEKENRELVERW 164
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
128-544 |
2.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 128 DHEQQIKDLEQKLS----LQEQDAAIVKNmkselvRLPRLERELKQLREESAHLREMRETNGLLQEELeglqrklgrQEK 203
Cdd:pfam15921 82 EYSHQVKDLQRRLNesneLHEKQKFYLRQ------SVIDLQTKLQEMQMERDAMADIRRRESQSQEDL---------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 204 MQETLVGLE----LENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQ---RELALKDKNSAVTSSARG--LEKAR 274
Cdd:pfam15921 147 LQNTVHELEaakcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEasgKKIYEHDSMSTMHFRSLGsaISKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 275 QQLQEELRQVSGQLLEERKKRETHEALARrlQKRVLLLTKERDGMRAILGSYDSELTpaeyspQLTRRMREAEDMVQKVH 354
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQ--NKIELLLQQHQDRIEQLISEHEVEIT------GLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 355 SH----SAEMEAQLSQALEELGGQKQRADMLEMELK----MLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEE 426
Cdd:pfam15921 299 SQleiiQEQARNQNSMYMRQLSDLESTVSQLRSELReakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 427 KRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAM--ERGGTVPADLEAAAASLP 504
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksECQGQMERQMAAIQGKNE 458
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 751557638 505 SSKEVAELKKQVESAelknqrlKEVFQTKIQEFRKACYTL 544
Cdd:pfam15921 459 SLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTL 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
71-520 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 71 KGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEA----------NQKIQELQASQEARADHE---------- 130
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEeersqqlqne 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 131 -----QQIKDLEQKLslqEQDAAIVKNMKSELV----RLPRLERELKQLREESAHLREMREtngLLQEELEGLQRKLGRQ 201
Cdd:pfam01576 98 kkkmqQHIQDLEEQL---DEEEAARQKLQLEKVtteaKIKKLEEDILLLEDQNSKLSKERK---LLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 202 EKMQETLVGLELENERLLAKLQ--------SWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSA-----VTSSAR 268
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEerlkkeekGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 269 GLEK--ARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILgsYDSELTPAEYSPQLTRRMREA 346
Cdd:pfam01576 252 LEEEtaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL--EDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 347 EDMVQKVHSHSAEMEAQLSQALEElggQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEE 426
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQK---HTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 427 KRMLEAQLERralqgdydqsrtkvLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRamerggtvpadlEAAAASLPSS 506
Cdd:pfam01576 407 RKKLEGQLQE--------------LQARLSESERQRAELAEKLSKLQSELESVSSLLN------------EAEGKNIKLS 460
|
490
....*....|....
gi 751557638 507 KEVAELKKQVESAE 520
Cdd:pfam01576 461 KDVSSLESQLQDTQ 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-349 |
3.05e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMRVKRLESEKQELQEQLdlqhkkcqeanQKIQELQASQEARADHEQqIKDLEQKLS-LQEQ 145
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-----------HKLEEALNDLEARLSHSR-IPEIQAELSkLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 146 DAAIVKNMKSELVRLPRLERELKQLREESAHL----REMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAK 221
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 222 LQS-WERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEElrqvSGQLLEERKKRETHEA 300
Cdd:TIGR02169 887 LKKeRDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI----PEEELSLEDVQAELQR 962
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 751557638 301 LARRLQKRvllltkERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDM 349
Cdd:TIGR02169 963 VEEEIRAL------EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-284 |
3.27e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 70 LKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEAR----ADHEQQIKDLEQKLSLQEQ 145
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELeeelEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 146 DaaiVKNMKSELVRLPRLERELK-QLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQS 224
Cdd:TIGR02169 890 E---RDELEAQLRELERKIEELEaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 225 WERLDQTMGLSIRTPEdlsrfvvELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQV 284
Cdd:TIGR02169 967 IRALEPVNMLAIQEYE-------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-528 |
3.33e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 338 QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELE 417
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 418 GERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLnptSVARQRLREDHSQLQAECERLRGLLRamerggtvpADLE 497
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEELEELAE---------ELLE 390
|
170 180 190
....*....|....*....|....*....|.
gi 751557638 498 AAAASLPSSKEVAELKKQVESAELKNQRLKE 528
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-317 |
3.33e-04 |
|
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: 43.89 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQAsqearadheqQIKDLEQKL-SLQE 144
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----------ELTLLNEEAaNLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 145 QDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELE-GLQRKLGRQEKMQETLVGLELENERLLAKLQ 223
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEsELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 224 SWERLdqtmglsirtpedlsrfVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRE-THEALA 302
Cdd:TIGR02168 905 ELESK-----------------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDE 967
|
250
....*....|....*
gi 751557638 303 RRLQKRVLLLTKERD 317
Cdd:TIGR02168 968 EEARRRLKRLENKIK 982
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
91-479 |
3.36e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 91 LESEKQELQEQLDLQHkkcQEANQKIQELQASQEARADHEQQIKDLEQKLSLQeQDAAIVKNmkselvrlpRLERELKQL 170
Cdd:PRK04863 291 LRRELYTSRRQLAAEQ---YRLVEMARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQE---------KIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 171 REESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVG--------LELENERLLAKLQSWERLDQTMGLsirtpedl 242
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSqladyqqaLDVQQTRAIQYQQAVQALERAKQL-------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 243 srfvveLQQRELALKdknsavtssarGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGM--- 319
Cdd:PRK04863 430 ------CGLPDLTAD-----------NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrs 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 320 ------RAILGSYDSELTPAEYSPQLTRRMREAEdmvQKVHSHsAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSS 393
Cdd:PRK04863 493 eawdvaRELLRRLREQRHLAEQLQQLRMRLSELE---QRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 394 SAEQSFLFSREEADTLRLKVEELEGERSRLEE-EKRMLEAQ--LER-RALQGDYDQSRTKVLHMSLN------PTSVARQ 463
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAArAPAWLAAQdaLARlREQSGEEFEDSQDVTEYMQQllererELTVERD 648
|
410
....*....|....*.
gi 751557638 464 RLREDHSQLQAECERL 479
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
65-434 |
3.52e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 65 TTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELqasqearadhEQQIKDLEQKLSL-- 142
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL----------EKQLNQLKSEISDln 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 143 QEQDAAIVKNMKSELV------------------RLPRLERELKQLREESAHLREmreTNGLLQEELEGLQRKLGRQEKM 204
Cdd:TIGR04523 302 NQKEQDWNKELKSELKnqekkleeiqnqisqnnkIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 205 QE----TLVGLELENERLLAKLQSWERLDQTMGLSIRTPE-----------DLSRFVVELQQRELALKDKNSAVTSSARG 269
Cdd:TIGR04523 379 NQsykqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekellekeieRLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 270 LEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKER---DGMRAILGSYDSELTPAEysPQLTRRMREA 346
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKkelEEKVKDLTKKISSLKEKI--EKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 347 EDMVQKVHSHSAEMEAQLSQAL--EELGGQKQRADMLEMELKMLKSQSSSA-------EQSFLFSREEADTLRLKVEELE 417
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKqelidqkEKEKKDLIKEIEEKEKKISSLE 616
|
410
....*....|....*..
gi 751557638 418 GERSRLEEEKRMLEAQL 434
Cdd:TIGR04523 617 KELEKAKKENEKLSSII 633
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-268 |
3.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 67 INALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEA-RADHEQQIKDLE------QK 139
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAellralYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 140 LSLQEQDAAIVKN-----MKSELVRLPRLERELKQLREE-SAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLEL 213
Cdd:COG4942 116 LGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 751557638 214 ENERLLAKL-QSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSAR 268
Cdd:COG4942 196 ERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-473 |
7.93e-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: 42.85 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 66 TINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQAsqearadheqQIKDLEQKLSLQEQ 145
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA----------QISELQEDLESERA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 146 DAAIVKNMKSEL-VRLPRLERELKQLREESAHLREMRETNgllQEELEGLQRKLGRQEKMQETLVGlELENERLLAKLQS 224
Cdd:pfam01576 286 ARNKAEKQRRDLgEELEALKTELEDTLDTTAAQQELRSKR---EQEVTELKKALEEETRSHEAQLQ-EMRQKHTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 225 WERLDQTmglsirtpedlSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARR 304
Cdd:pfam01576 362 TEQLEQA-----------KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 305 LQKRVLLLTKERDGMRAILGSYDSELTP-AEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEM 383
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKlSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 384 ELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQ 463
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
|
410
....*....|
gi 751557638 464 RLREDHSQLQ 473
Cdd:pfam01576 591 HQRQLVSNLE 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
64-520 |
8.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 64 HTTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEAN---QKIQELQASQEA----RADHEQQIKDL 136
Cdd:PRK02224 205 HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAEtereREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 137 EQKLS--------------LQEQDAAIVKNMKSEL-VRLPRLERELKQLREE-SAHLRE---MRETNGLLQEELEGLQRK 197
Cdd:PRK02224 285 RERLEeleeerddllaeagLDDADAEAVEARREELeDRDEELRDRLEECRVAaQAHNEEaesLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 198 LGRQEK-MQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKAR-- 274
Cdd:PRK02224 365 AAELESeLEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVee 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 275 -QQLQEELR-QVSGQLLEERKKRETHEALARRLQKrvllLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQK 352
Cdd:PRK02224 445 aEALLEAGKcPECGQPVEGSPHVETIEEDRERVEE----LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 353 VHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAeqsflfsREEADTLRLKVEELEGERSRLEEEKRMLEA 432
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 433 QLERRALQGDYDQsrtkvlhmslnptsvARQRLREDHSQLQAECERLRGLLRAM-ERGGTVPADLEAAAaslpsskeVAE 511
Cdd:PRK02224 594 IRTLLAAIADAED---------------EIERLREKREALAELNDERRERLAEKrERKRELEAEFDEAR--------IEE 650
|
....*....
gi 751557638 512 LKKQVESAE 520
Cdd:PRK02224 651 AREDKERAE 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-540 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 358 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERR 437
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 438 ------ALQGDYDQSRTKVLHMSLNPTSVAR--QRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSK-E 508
Cdd:COG4942 103 keelaeLLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLaE 182
|
170 180 190
....*....|....*....|....*....|..
gi 751557638 509 VAELKKQVESAELKNQRLKEVFQTKIQEFRKA 540
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
85-331 |
1.10e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 85 EMRVKRLESEKQELQEQLDlQHKKcqEANQKIQELQASQEARADHEQQIKDLEQKL-SLQEQDAAIVKNMKSELVRLPRL 163
Cdd:COG1340 7 SSSLEELEEKIEELREEIE-ELKE--KRDELNEELKELAEKRDELNAQVKELREEAqELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 164 ERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVgLELENER-LLAKLQSWERLDQTMglsiRTPEDL 242
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-LSPEEEKeLVEKIKELEKELEKA----KKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 243 SRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAI 322
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
....*....
gi 751557638 323 LGSYDSELT 331
Cdd:COG1340 239 LRELRKELK 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
73-534 |
1.15e-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: 42.34 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 73 RISELQWSVMDQEMRVKRLESEKQELQ-EQLDLQHKKCQEAnQKIQELQASQEARADHEQQIKDleqKLSLQEQDAAIVK 151
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQnEKADLDRKLRKLD-QEMEQLNHHTTTRTQMEMLTKD---KMDKDEQIRKIKS 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 152 NMKSELVRL-------PRLERELKQLREEsahLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLL----- 219
Cdd:TIGR00606 557 RHSDELTSLlgyfpnkKQLEDWLHSKSKE---INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcg 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 220 --AKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRET 297
Cdd:TIGR00606 634 sqDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 298 HEALARRLQKRVLLLTKERDGMRAILGSYDSELtpaeysPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQK-- 375
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI------PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvc 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 376 -------QRADMLEMELKMLKSQSSSAEQSFLFSREEADtLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRT 448
Cdd:TIGR00606 788 ltdvtimERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ-VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 449 KVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVES--AELKNQRL 526
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkAQDKVNDI 946
|
....*...
gi 751557638 527 KEVFQTKI 534
Cdd:TIGR00606 947 KEKVKNIH 954
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
84-306 |
1.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 84 QEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQAS------QEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSEL 157
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 158 VRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGR--------QEKMQETLVGLELENERLLAKLQSwerld 229
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialRAQIAALRAQLQQEAQRILASLEA----- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751557638 230 qtmglsirtpedlsrFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVsgqlleeRKKRETHEALARRLQ 306
Cdd:COG3206 321 ---------------ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV-------EVARELYESLLQRLE 375
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
156-505 |
1.62e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 156 ELVRLPRLERELKQLREESAHLREMRETNGLlqeELEGLQR--KLGRQEK--MQETLVGLELENERL----LAKLQSWER 227
Cdd:pfam07111 71 QLQELRRLEEEVRLLRETSLQQKMRLEAQAM---ELDALAVaeKAGQAEAegLRAALAGAEMVRKNLeegsQRELEEIQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 228 LDQtmglsirtpEDLSRFVvelQQRELALkdknSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQK 307
Cdd:pfam07111 148 LHQ---------EQLSSLT---QAHEEAL----SSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 308 RVLLLTKERDGMRAILGsydsELTPAEYSPQLTRRMR-EAEDMVQKVHSHSAEMEAQ--------------LSQALEELG 372
Cdd:pfam07111 212 ELEAQVTLVESLRKYVG----EQVPPEVHSQTWELERqELLDTMQHLQEDRADLQATvellqvrvqslthmLALQEEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 373 GQKQRADMLEMEL--KMLKSQSSSAEQSF----------LFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQ 440
Cdd:pfam07111 288 RKIQPSDSLEPEFpkKCRSLLNRWREKVFalmvqlkaqdLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAE 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751557638 441 GDYDQSRTKVLHMSLNPTSVARQRLREdhsQLQAECERLRGLLRAMERGG----TVPADLEAAAASLPS 505
Cdd:pfam07111 368 VEVERMSAKGLQMELSRAQEARRRQQQ---QTASAEEQLKFVVNAMSSTQiwleTTMTRVEQAVARIPS 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
122-528 |
1.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 122 SQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELvrlprlERELKQLREESAHLREMREtngllqeELEGLQRKLGRQ 201
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEL------EEVLREINEISSELPELRE-------ELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 202 EKMQETLVGLELENERLL-------AKLQSWERLDQTMGLSIRTPED-----------------LSRFVVELQQRELALK 257
Cdd:PRK03918 234 EELKEEIEELEKELESLEgskrkleEKIRELEERIEELKKEIEELEEkvkelkelkekaeeyikLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 258 DKNSAVTSSARGLEKARQQLQE---ELRQVSGQLLEERKKRETHEALARRLQkRVLLLTKERDGMRAILGSYDSELTPAE 334
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 335 YSpQLTRRMREAEDMVQKVHSHSAEME---AQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQsflfsREEADTLRL 411
Cdd:PRK03918 393 LE-ELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEY-----TAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 412 KVEELEGERSRLEEEKRMLEAQLERralqgdydQSRTKVLHMSLNPTSVARQRLRE-DHSQLQAECERLRGLLramERGG 490
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKK--------ESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLK---EKLI 535
|
410 420 430
....*....|....*....|....*....|....*...
gi 751557638 491 TVPADLEAAAASLpssKEVAELKKQVESAELKNQRLKE 528
Cdd:PRK03918 536 KLKGEIKSLKKEL---EKLEELKKKLAELEKKLDELEE 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
214-428 |
1.93e-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: 40.90 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 214 ENERLLAKLQswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVtssaRGLEKARQQLQEELRQVSGQLLE-ER 292
Cdd:COG4942 24 EAEAELEQLQ--QEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAElRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 293 KKRETHEALARRLqkRVLLLTKERDGMRAILGSYDSELTP------AEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQ 366
Cdd:COG4942 98 ELEAQKEELAELL--RALYRLGRQPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751557638 367 ALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKR 428
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
85-302 |
2.08e-03 |
|
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: 41.48 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 85 EMRVKRLESEKQELQEQLDLQHKKcqeANQKIQELQASQEARA--------------------DHEQQIK----DLEQKL 140
Cdd:COG3096 388 EEEVDSLKSQLADYQQALDVQQTR---AIQYQQAVQALEKARAlcglpdltpenaedylaafrAKEQQATeevlELEQKL 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 141 SLQ-------EQDAAIVKNMKSELVRLPRLERELKQLRE--ESAHLREMRETnglLQEELEGLQRKLGRQEKMQETLvgl 211
Cdd:COG3096 465 SVAdaarrqfEKAYELVCKIAGEVERSQAWQTARELLRRyrSQQALAQRLQQ---LRAQLAELEQRLRQQQNAERLL--- 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 212 elenerllaklqswERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEE 291
Cdd:COG3096 539 --------------EEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
250
....*....|.
gi 751557638 292 RKKRETHEALA 302
Cdd:COG3096 605 LAAQDALERLR 615
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-539 |
2.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 83 DQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADH----EQQIKDLEQKLSLQEQDAAIVKNMKSELV 158
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 159 RLPRLERELKQLREESAHLREMRETngllQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERldqtmglsiRT 238
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---------KK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 239 PEDLSRFVVELQQRELALKDknsavTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDG 318
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKK-----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 319 MRAILGSYDSELTPAEySPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQS 398
Cdd:PTZ00121 1534 KKADEAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 399 flfsrEEADTLRLKVEEL--EGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVlhmslnptSVARQRLREDHSQLQAEc 476
Cdd:PTZ00121 1613 -----KKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI--------KAAEEAKKAEEDKKKAE- 1678
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751557638 477 erlrgLLRAMERGGTVPAdlEAAAASLPSSKEVAELKKQVESAELKNQRLK---EVFQTKIQEFRK 539
Cdd:PTZ00121 1679 -----EAKKAEEDEKKAA--EALKKEAEEAKKAEELKKKEAEEKKKAEELKkaeEENKIKAEEAKK 1737
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-536 |
2.46e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 86 MRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLER 165
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 166 ELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEK-MQETLVGLELEN-------ERLLAKLQSWERLDQTMGLSIR 237
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaITCTAQCEKLEKihlqesaQSLKEREQQLQTKEQIHLQETR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 238 TPEDLSRFVVELQQRELALKDKNS-------------AVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARR 304
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIhpnparqdidnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 305 LQKRVLLLTKERDGMRAILgsyDSELTPAEYSPQLTRRMREAEDMVqKVHSHSAEMEAQLSQALEELGGQKQRadmLEME 384
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDI---PNLQNITVRLQDLTEKLSEAEDML-ACEQHALLRKLQPEQDLQDVRLHLQQ---CSQE 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 385 LKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKrmlEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQR 464
Cdd:TIGR00618 641 LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ---KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751557638 465 lREDHSQLQAecerlrgllrAMERGGTVPADLEAAAASLPSSKEVAE--LKKQVESAELKNQRLKEVFQTKIQE 536
Cdd:TIGR00618 718 -REFNEIENA----------SSSLGSDLAAREDALNQSLKELMHQARtvLKARTEAHFNNNEEVTAALQTGAEL 780
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
85-306 |
2.75e-03 |
|
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: 41.09 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 85 EMRVKRLESEKQELQEQLDLQHKKCQEANQKiqeLQASQEARADHEQQIKDLEQKLSLQEQDAAIVK---------NMKS 155
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQK---LSVADAARRQFEKAYELVCKIAGEVERSQAWQTarellrryrSQQA 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 156 ELVRLPRLERELKQLREESAHLREMREtngLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQswERLDQTMGLS 235
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAER---LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA--EAVEQRSELR 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 236 iRTPEDLSRFVVELQQRELALKDKNSAVTS----------SARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRL 305
Cdd:COG3096 585 -QQLEQLRARIKELAARAPAWLAAQDALERlreqsgealaDSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
.
gi 751557638 306 Q 306
Cdd:COG3096 664 S 664
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
70-415 |
2.88e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 70 LKGRISELQWSVMDQEMRVKRLE--------SEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDL-EQKL 140
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEiqltaiktSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAsDMTL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 141 SLQEQDAAIVKNMKSElvrlprlERELKQLREesahlreMRETNGLLQEELEGLQRKLGRQ--------EKMQETLVGLE 212
Cdd:pfam05483 514 ELKKHQEDIINCKKQE-------ERMLKQIEN-------LEEKEMNLRDELESVREEFIQKgdevkcklDKSEENARSIE 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 213 LENERLLAKLQSWERLDQTMGLSIrtpEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQvSGQLLEER 292
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQI---ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS-AKQKFEEI 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 293 KKRETHEALARRLQKRVLLLTKERDGMRAilgsydSELTPAEYSPQLTRRMREAEdMVQKVHSHSAEMEAQLSQALEELG 372
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEEVEKAKAIA------DEAVKLQKEIDKRCQHKIAE-MVALMEKHKHQYDKIIEERDSELG 728
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 751557638 373 GQKQRAD-------MLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEE 415
Cdd:pfam05483 729 LYKNKEQeqssakaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
65-280 |
3.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 65 TTINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARadhEQQIKDLEQKL---- 140
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 141 -SLQEQDAAI------------------VKNMKSELVRLPRLERELKQLREESAHLREMretnglLQEELEGLQRKLGRQ 201
Cdd:COG3883 93 rALYRSGGSVsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAE------LEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 751557638 202 EKMQETLVGLELENERLLAKLQSWERLDQtmglsirtpEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEE 280
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAE---------AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
110-435 |
4.15e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 110 QEANQKIQELQASQEARADHEQQIKDLEQKLS-LQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLRE-MRETNGLL 187
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQqLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEiLHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 188 QEELEGLQRKLGRQEKMQETLVGLElenerllAKLQSWERLDQTMGLSIRTPEDLsrfVVELQQRELALKDKNSAvtssa 267
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLE-------EQLDEEEAARQKLQLEKVTTEAK---IKKLEEDILLLEDQNSK----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 268 rgLEKARQQLQEELRQVSGQLLEERKK-------RETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTP-------- 332
Cdd:pfam01576 150 --LSKERKLLEERISEFTSNLAEEEEKakslsklKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDlqeqiael 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 333 ----AEYSPQLTRRMREAEDMVQKVHSHSA----------EMEAQLSQALEEL--------GGQKQRADMLEmELKMLK- 389
Cdd:pfam01576 228 qaqiAELRAQLAKKEEELQAALARLEEETAqknnalkkirELEAQISELQEDLeseraarnKAEKQRRDLGE-ELEALKt 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 751557638 390 ----SQSSSAEQSFLFSREEADTLRLKveelegerSRLEEEKRMLEAQLE 435
Cdd:pfam01576 307 eledTLDTTAAQQELRSKREQEVTELK--------KALEEETRSHEAQLQ 348
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-501 |
4.39e-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: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 261 SAVTSSARGLEKARQQL---QEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKErdgmraiLGSYDSELTpaeysp 337
Cdd:COG4942 13 LAAAAQADAAAEAEAELeqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELA------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 338 QLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRAdmlemELKMLKSQSSSAEQSFLFS---------REEADT 408
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP-----PLALLLSPEDFLDAVRRLQylkylaparREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 409 LRLKVEELEGERSRLEEEKRMLEAQL-----ERRALQGDYDQSRTKvlhmsLNPTSVARQRLREDHSQLQAECERLRGLL 483
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLaeleeERAALEALKAERQKL-----LARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 751557638 484 RAMERGGTVPADLEAAAA 501
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
87-482 |
5.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 87 RVKRLESEKQELQEQLDLQHKKCQEANQKIQElqaSQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELV-RLPRLER 165
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVED---RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELReERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 166 ELKQLREESAHLREMRETNGLLQEE---------------LEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQ 230
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 231 TMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKrvl 310
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE--- 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 311 lLTKERDGMRAILGSYDselTPAEYSPQLTRRMREAEDMvqkvhshsAEMEAQLSQALEELGGQKQ--RADMLEMELKML 388
Cdd:PRK02224 584 -LKERIESLERIRTLLA---AIADAEDEIERLREKREAL--------AELNDERRERLAEKRERKRelEAEFDEARIEEA 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 389 KSQSSSAEQSFlfsrEEADTlrlKVEELEGERSRLEEEKRMLEAQLERRAlqgdydqsrtkvlhmslnptsvarqRLRED 468
Cdd:PRK02224 652 REDKERAEEYL----EQVEE---KLDELREERDDLQAEIGAVENELEELE-------------------------ELRER 699
|
410
....*....|....
gi 751557638 469 HSQLQAECERLRGL 482
Cdd:PRK02224 700 REALENRVEALEAL 713
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
253-448 |
5.63e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 253 ELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKK-------RETHEALAR--RLQKRVLLLTKERDGMRAIL 323
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlsEEAKLLLQQlsELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 324 GSYDSELtpAEYSPQLTRRMREAEdmVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSR 403
Cdd:COG3206 243 AALRAQL--GSGPDALPELLQSPV--IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 751557638 404 E-EADTLRLKVEELEGERSRLEEE-KRMLEAQLERRALQGDYDQSRT 448
Cdd:COG3206 319 EaELEALQAREASLQAQLAQLEARlAELPELEAELRRLEREVEVARE 365
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
112-479 |
6.68e-03 |
|
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: 39.55 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 112 ANQKIQELQASQEARADHEQqikdlEQKLSLQEQDAAIvkNMKSELVRLPRLERELKQ-LREESAHLREMR------ETN 184
Cdd:COG3096 277 ANERRELSERALELRRELFG-----ARRQLAEEQYRLV--EMARELEELSARESDLEQdYQAASDHLNLVQtalrqqEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 185 GLLQEELEGLQRKLGRQEKMQETLVGLELENE-RLLAKLQSWERLDQTMGlsirtpeDLSRFVVELQQRELALKdknSAV 263
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEaRLEAAEEEVDSLKSQLA-------DYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 264 tssaRGLEKAR-----------------QQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGM------- 319
Cdd:COG3096 420 ----QALEKARalcglpdltpenaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVersqawq 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 320 --RAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHshsaEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQ 397
Cdd:COG3096 496 taRELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQ----NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 398 SFLFSREEADTLRLKVEELEGERSRLEE-EKRMLEAQ--LERRALQ--------GDYDQSRTKVLHmSLNPTSVARQRLR 466
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAArAPAWLAAQdaLERLREQsgealadsQEVTAAMQQLLE-REREATVERDELA 650
|
410
....*....|...
gi 751557638 467 EDHSQLQAECERL 479
Cdd:COG3096 651 ARKQALESQIERL 663
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
87-169 |
6.71e-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: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 87 RVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQD-----------------AAI 149
Cdd:COG0542 441 RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEElaelapllreevteediAEV 520
|
90 100
....*....|....*....|....*....
gi 751557638 150 V---------KNMKSELVRLPRLERELKQ 169
Cdd:COG0542 521 VsrwtgipvgKLLEGEREKLLNLEEELHE 549
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
364-529 |
8.57e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 364 LSQALEELggqkqRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERraLQGDY 443
Cdd:COG2433 378 IEEALEEL-----IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--LEREL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 444 DQSRTKvlhmslnptsvARQRLREDH--SQLQAECERLRgllramerggtvpadleaaaaslpssKEVAELKKQVESAEL 521
Cdd:COG2433 451 SEARSE-----------ERREIRKDReiSRLDREIERLE--------------------------RELEEERERIEELKR 493
|
....*...
gi 751557638 522 KNQRLKEV 529
Cdd:COG2433 494 KLERLKEL 501
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
95-313 |
8.71e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 95 KQELQEQLD-LQHKKCQEANQK--IQELQASQE---ARADHEQQIKDLEQKLslqEQDAAIVKNMKSELVRLPRLERELK 168
Cdd:PRK11281 38 EADVQAQLDaLNKQKLLEAEDKlvQQDLEQTLAlldKIDRQKEETEQLKQQL---AQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557638 169 QLREESAHLREmretnglLQEELEGLQRKLGRqekMQETLVglelENERLLAKLQSwerldqtmgLSIRTPEDLSRFVVE 248
Cdd:PRK11281 115 RETLSTLSLRQ-------LESRLAQTLDQLQN---AQNDLA----EYNSQLVSLQT---------QPERAQAALYANSQR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751557638 249 LQQRELALKDKNsavTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLT 313
Cdd:PRK11281 172 LQQIRNLLKGGK---VGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLT 233
|
|
| |
