|
Name |
Accession |
Description |
Interval |
E-value |
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
54-715 |
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: 694.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 54 QAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQMEMNKS 133
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 134 YKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQA 213
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 214 SQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARFPKMERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERY 293
Cdd:pfam05557 161 QQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 294 EKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEI 373
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 374 LSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQKLHAHNAELE 453
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 454 AQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTvvTKEEVDTLRLKIEELEAERSKLAEENRSLEMKLEKLTLQG 533
Cdd:pfam05557 401 AQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY--SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 534 DYDPSRTKVLHLSMNPMSLAKQQRKEEQQQLQEECERLRELVRVLKGGGSLSGELEGVGAFQSPQEVAELKKQVESAELK 613
Cdd:pfam05557 479 DYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 614 NQRLKEVFQTKIQEFRKVCYTLTGYQIDITTENQYRLSSIYAEHQGDCLLFKASSSSGGKMQLLETEFSRTVRELIELHL 693
Cdd:pfam05557 559 NQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLIDLHL 638
|
650 660
....*....|....*....|..
gi 525013811 694 LRQDSIPAFLSALTLDLFSRQT 715
Cdd:pfam05557 639 AAQKSIPAFLSALTLELFSRQT 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-532 |
1.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 277 GLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSwekldQSTGLNIRTPDdLSRQIVALQQRELALKEQNSTFM 356
Cdd:TIGR02168 228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE-----KLEELRLEVSE-LEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 357 NSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELspaehsPQLSRRMR 436
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL------EELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 437 EAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVvtKEEVDTLRLKIEELEAERSKLA 516
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQ 453
|
250
....*....|....*.
gi 525013811 517 EENRSLEMKLEKLTLQ 532
Cdd:TIGR02168 454 EELERLEEALEELREE 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-532 |
1.91e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 50 QLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARN-YEREADRNQELLTRIKQYQEREAEAENKLKEQM 128
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeLEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 129 EMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDiekKKWQEASQQI 208
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 209 QTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARfpKMERELRQLKEENAYFREMKENNGLLKEEVEGLQR 288
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE--EEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 289 KLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQ---STGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKA 365
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 366 RQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQKL 445
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 446 HAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERSKLAEENRSLEMK 525
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
....*..
gi 525013811 526 LEKLTLQ 532
Cdd:COG1196 711 EAEEERL 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-529 |
2.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 104 QELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQ 183
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 184 DSEKQELMEQLDIEKKKWQEASQQIQTLQASqslLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARfpKMERELRQLK 263
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEE--ELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 264 EENAYFREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQQ 343
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 344 RELALKEQNSTFMNSARMLEKARQQLQEEILsVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSels 423
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAE-ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--- 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 424 pAEHSPQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRL 503
Cdd:COG1196 546 -AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
410 420
....*....|....*....|....*.
gi 525013811 504 KIEELEAERSKLAEENRSLEMKLEKL 529
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVT 650
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-530 |
1.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 46 QQRMQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARI--------ELEKAANTNARNYEREADRNQELLTRIKQYQERE 117
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRreleerleELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 118 AEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQL--- 194
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALael 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 195 ----DIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARFPKMERELRQLKEENAYFR 270
Cdd:COG1196 434 eeeeEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 271 EMKENNGLLKEEVEGLQRKLERYEKV-----QAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQQRE 345
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAAleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 346 LALKEQNSTFMNSARMLEKARQQLQEEILSVQSqllDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESydSELSPA 425
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRT---LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL--TGGSRR 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 426 EHSPQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKI 505
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
490 500
....*....|....*....|....*
gi 525013811 506 EELEAERSKLAEENRSLEMKLEKLT 530
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-399 |
2.87e-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: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 110 IKQYQEREAEAENKLkEQMEMN-----------KSYKKSMETMSKK----------------------IQEKESKLAEAN 156
Cdd:TIGR02168 167 ISKYKERRKETERKL-ERTRENldrledilnelERQLKSLERQAEKaerykelkaelrelelallvlrLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 157 ETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQAS--------QSLLAEYEQKIKDL 228
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerlANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 229 EQKLSQQEHDALIVKNMKAELARF-PKMERELRQLKEENAYFREMKENNGLLKEEVEGLQRKL----ERYEKVQAQLVTV 303
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqleLQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 304 ELENEKLLGKLQSW--EKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLL 381
Cdd:TIGR02168 406 EARLERLEDRRERLqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330
....*....|....*...
gi 525013811 382 DEKKKREHQEALVRRLQK 399
Cdd:TIGR02168 486 QLQARLDSLERLQENLEG 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
51-509 |
3.03e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 51 LEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARNY----EREADRNQELLTRI-KQYQEREAEAE--NK 123
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekQKELEQNNKKIKELeKQLNQLKSEISdlNN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 124 LKEQmEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQE 203
Cdd:TIGR04523 303 QKEQ-DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 204 ASQQIQTLqasqsllaeyEQKIKDLEQKLSQQEHDA-LIVKNMKAELARFPKMERELRQLKEE----NAYFREMKENNGL 278
Cdd:TIGR04523 382 YKQEIKNL----------ESQINDLESKIQNQEKLNqQKDEQIKKLQQEKELLEKEIERLKETiiknNSEIKDLTNQDSV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 279 LKEEVEGLQRKLErYEKVQAQLVTVELENEKllgklQSWEKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNS 358
Cdd:TIGR04523 452 KELIIKNLDNTRE-SLETQLKVLSRSINKIK-----QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 359 ARMLEKARQQLQEEILSVQSQL--LDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILEsydselspaehspQLSRRMR 436
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE-------------EKQELID 592
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525013811 437 EAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELE 509
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-426 |
6.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 110 IKQYQEREAEAENKLkEQMEMNksykksMETMSKKIQEKESKLA-------------EANETITVLKGKISELQWNIMNQ 176
Cdd:COG1196 167 ISKYKERKEEAERKL-EATEEN------LERLEDILGELERQLEplerqaekaeryrELKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 177 EM-----QMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQ-ASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELA 250
Cdd:COG1196 240 ELeeleaELEELEAELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 251 RfpkMERELRQLKEENAYFREMKENnglLKEEVEGLQRKLERYEKVQAQLVTVELE-NEKLLGKLQSWEKLDQSTGLNIR 329
Cdd:COG1196 320 E---LEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 330 TPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERD 409
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330
....*....|....*..
gi 525013811 410 GMRAILESYDSELSPAE 426
Cdd:COG1196 474 LLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-525 |
1.39e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 162 LKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEYEQK----IKDLEQKLSQQEH 237
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKlkerLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 238 DALIVKNMKAEL-ARFPKMERELRQLKEENAYFREMkenngLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQS 316
Cdd:TIGR02169 752 EIENVKSELKELeARIEELEEDLHKLEEALNDLEAR-----LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 317 WEKLdqstglnirtpddLSRQIVALQQRELALKEQnstfmnsarmlekaRQQLQEEILSVQSQLLDEKKKREHQEALVRR 396
Cdd:TIGR02169 827 EKEY-------------LEKEIQELQEQRIDLKEQ--------------IKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 397 LQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSR-RMREAEDMVQKLHAHNAELEAQLSQVLEEVGSH------KQR 469
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAE 959
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 525013811 470 AEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERSKLAEENRSLEMK 525
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-408 |
2.04e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 29 SGLATPGSSQSSLQMQYQQrmQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARI-ELEKAANTNARNYEREADRNQELL 107
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSR--SEPAELQRLRERLEGLKRELSSLQSELRRIENRLdELSQELSDASRKIGEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 108 TRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQmtSQDSEK 187
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS--KLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 188 QELMEQLD----IEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQklsQQEHDALIVKNMKAELARFPKMERELR-QL 262
Cdd:TIGR02169 808 SRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLEsRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 263 KEENAYFREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQ 342
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525013811 343 QRELALKEQNStfmnsarmleKARQQLQEeilsVQSQLLDEKKKREHQEALVRRLQKRVVLLTKER 408
Cdd:TIGR02169 965 EEIRALEPVNM----------LAIQEYEE----VLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-535 |
2.38e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 256 ERELRQLKEEnayFREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQ-SWEKLDQSTGLNIRTPDDL 334
Cdd:TIGR02168 676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 335 SRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAI 414
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 415 LESYDSELSpaehspQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEqstvvt 494
Cdd:TIGR02168 833 IAATERRLE------DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS------ 900
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 525013811 495 kEEVDTLRLKIEELEAERSKLAEENRSLEMKLEKLTLQGDY 535
Cdd:TIGR02168 901 -EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-529 |
1.85e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 46 QQRMQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLK 125
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 126 EQMEMNKSYKKSMETMSKKIQEKESKlAEANETITVLKGKISELQwniMNQEMQMTSQDSEKQELMEQLDIEKKKWQEAS 205
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 206 QQIQTLQASQSLLAEYEQKIKDLEQKLSQQEhdalivKNMKAELARfpkMERELRQLKEENAYFREMKENNGLLKEEVeg 285
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEE------AKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEE-- 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 286 lQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARM-LEK 364
Cdd:PTZ00121 1533 -AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEE 1611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 365 ARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVV-LLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQ 443
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 444 KLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQqctAEQStvvtKEEVDTLRLKIEEL---EAERSKLAEENR 520
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK---AEEA----KKEAEEDKKKAEEAkkdEEEKKKIAHLKK 1764
|
....*....
gi 525013811 521 SLEMKLEKL 529
Cdd:PTZ00121 1765 EEEKKAEEI 1773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-529 |
2.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 85 LEKAANtNARNYEREADRNQElltRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEAN---ETITV 161
Cdd:PRK03918 160 YENAYK-NLGEVIKEIKRRIE---RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 162 LKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQKLSQqehdali 241
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 242 VKNMKAELARFpkmERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERYEKvqaqlvtVELENEKLLGKLQSWEKLd 321
Cdd:PRK03918 309 LREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-------RHELYEEAKAKKEELERL- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 322 qSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQS---------QLLDEkkkrEHQEA 392
Cdd:PRK03918 378 -KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTE----EHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 393 LVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQKLHahnaELEAQLSQV-LEEVGSHKQRAE 471
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK----ELEEKLKKYnLEELEKKAEEYE 528
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 525013811 472 MLEVEMKVLKSQQCTAEQSTvvtkEEVDTLRLKIEELEAERSKLAEENRSLEMKLEKL 529
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-409 |
1.44e-06 |
|
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: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 52 EEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAantnarnyereADRNQELLTRIKQYQEREAEAENKLKEQMEMN 131
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAEL-----------RKELEELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 132 KSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTL 211
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 212 QASqslLAEYEQKIKDLEQKLSQQEhdalivknmkaelARFPKMERELRQLKEENA-YFREMKENNGLLKEEVEGLQRKL 290
Cdd:TIGR02168 816 NEE---AANLRERLESLERRIAATE-------------RRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 291 ERYEKVQAQLVTVELENEKLLGKLQSWEKldqstglnirtpddlsrQIVALQQRELALKEQNSTFMNSARMLEKARQQLQ 370
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELES-----------------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 525013811 371 EEILSVQSQLLDE-KKKREHQEALVRRLQKRVVLLTKERD 409
Cdd:TIGR02168 943 ERLSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-402 |
2.04e-06 |
|
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: 51.21 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 77 SHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEAN 156
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 157 ETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKwqeasqqiqtLQASQSLLAEYEQKIKDLEQKLSQQE 236
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 237 HD-ALIVKNMKAELARFPKMERELRQLkeenayfremKENNGLLKEEVEGLQRKLERYEK--VQAQLVTVELENEKLLGK 313
Cdd:TIGR02168 386 SKvAQLELQIASLNNEIERLEARLERL----------EDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 314 L----QSWEKLDQSTGLNIRTPDDLSRQIVALQQRELALK---EQNSTFMNSARMLEKARQQLqEEILSVQSQLL--DEK 384
Cdd:TIGR02168 456 LerleEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSGL-SGILGVLSELIsvDEG 534
|
330
....*....|....*...
gi 525013811 385 KKREHQEALVRRLQKRVV 402
Cdd:TIGR02168 535 YEAAIEAALGGRLQAVVV 552
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
132-529 |
6.71e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 132 KSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTL 211
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 212 QAsqsLLAEYEQKIKDLEQKLSQQehdalIVKNMKAELARFPKMERELR-QLKEENAYFREMKENNGLLKEEVEGL---- 286
Cdd:TIGR04523 287 EK---QLNQLKSEISDLNNQKEQD-----WNKELKSELKNQEKKLEEIQnQISQNNKIISQLNEQISQLKKELTNSesen 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 287 QRKLERYEKVQAQLVTVELENEKllgKLQSWEKLDQSTglnirtpDDLSRQIVALQQRELALKEQNSTFMNSARMLEKAR 366
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQS---YKQEIKNLESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 367 QQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSpaehspQLSRRMREAEDMVQKLH 446
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE------QKQKELKSKEKELKKLN 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 447 AHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLK--IEELEAERSKLAEENRSLEM 524
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeIDEKNKEIEELKQTQKSLKK 582
|
....*
gi 525013811 525 KLEKL 529
Cdd:TIGR04523 583 KQEEK 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
50-527 |
9.91e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 50 QLEEQAGQIHSKSQLLQVEREKMQMELShkRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQME 129
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQ--LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 130 MNKSYK--KSMETMSKKIQEKESKLAEANETITVL--KGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEAS 205
Cdd:TIGR00618 255 QLKKQQllKQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 206 QQIQTLQASQSLLAEYeqkikdleqklsQQEHDALIVKNMKAELARfpkmeRELRQLKEENAYFREMKENNGLLKEEVEG 285
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTL------------HSQEIHIRDAHEVATSIR-----EISCQQHTLTQHIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 286 LQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQstglnirtpddlsrqivaLQQRELALKEQNSTFMNSARMLEKA 365
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE------------------LQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 366 RQQLQEEILSVQSQLLDEKKKREHQEALVRRLQ-KRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQK 444
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 445 LHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERSKLAEENRSLEM 524
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
...
gi 525013811 525 KLE 527
Cdd:TIGR00618 620 KLQ 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-562 |
1.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 42 QMQYQQRMQLEEQAGQIHSKSQLLQVEREKMQMEL--SHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAE 119
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 120 AENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQwnIMNQEMQMTSQDSEKQELMEQLDIEKK 199
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK--KADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 200 KWQEASQQIQTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARfpkMERELRQLKEENAYFREMKENNGLL 279
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADEAKKKAEEAKKADEAKKKAEEA 1495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 280 KEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQS-TGLNIRTPDDLS-----RQIVALQQRELALKEQNS 353
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkKAEEKKKADELKkaeelKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 354 TFMnSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLsr 433
Cdd:PTZ00121 1576 KNM-ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-- 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 434 rmREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERS 513
Cdd:PTZ00121 1653 --KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 525013811 514 KLAEENRSLEMKLEKLTLQGDYDPSRTKVLHLSMNPMSLAKQQRKEEQQ 562
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-532 |
1.25e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 106 LLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLK---------------------G 164
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlsekqkeleqnnK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 165 KISELQWNIMNQEMQMTSQDSEKQElmeqlDIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKN 244
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQ-----DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 245 MKAELAR-FPKMERELRQLKEENAYFREMKENnglLKEEVEGLQRKLERYEKV----QAQLVTVELENEKLLgklQSWEK 319
Cdd:TIGR04523 357 ENSEKQReLEEKQNEIEKLKKENQSYKQEIKN---LESQINDLESKIQNQEKLnqqkDEQIKKLQQEKELLE---KEIER 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 320 LDQSTGLNIRTPDDLSRQIVA-------LQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKrehqea 392
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVkeliiknLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE------ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 393 lVRRLQKRVVLLTKERDGMRAILESYDSELSpaehspQLSRRMREAEDMVQKLhahnaELEAQLSQVLEEVGSHKQRAEM 472
Cdd:TIGR04523 505 -KKELEEKVKDLTKKISSLKEKIEKLESEKK------EKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 473 LEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERSKLAEENRSLEMKLEKLTLQ 532
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
67-416 |
1.58e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 67 VEREKMQMELSHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQ 146
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 147 EKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEYEQKIK 226
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 227 DLEQKLSQQEhdalIVKNMKAELARFPKMERELRQLKEENAYFREMKENngllKEEVEGLQRKLERYEKVQAQLVTVELE 306
Cdd:pfam02463 313 EEKLKESEKE----KKKAEKELKKEKEEIEELEKELKELEIKREAEEEE----EEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 307 NEKLLGKLQSWEKLDQSTGLNIRTP-DDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKK 385
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLlLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350
....*....|....*....|....*....|.
gi 525013811 386 KREHQEALVRRLQKRVVLLTKERDGMRAILE 416
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
44-310 |
1.84e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 44 QYQQRMQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARNYEREADRNQElLTRIKQyQEREAEAENK 123
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE-LERIRQ-EERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 124 LKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQM----TSQDSEKQELMEQLDIEKK 199
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMeqirAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 200 K--------WQEASQQIQTL--QASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARFPKMERELRQLKEE---- 265
Cdd:pfam17380 446 RemervrleEQERQQQVERLrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeer 525
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 525013811 266 -NAYFREMKENNGllkEEVEGLQRKLERYEKVQAQLVTVELENEKL 310
Cdd:pfam17380 526 qKAIYEEERRREA---EEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
50-517 |
5.84e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 50 QLEEQAGQIHS--KSQLLQVEREKMQMELSHKRARIELEKAANTN-ARNYEREADRNQELLTRIKQYQEREAEAENKLKE 126
Cdd:PRK03918 277 ELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEeINGIEERIKELEEKEERLEELKKKLKELEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 127 ------QMEMNKSYKKSMETMSKKIQEKE-SKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKK 199
Cdd:PRK03918 357 leerheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 200 KWQEASQQIqTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARFPKMERELRQLKEENAYFREMKENngLL 279
Cdd:PRK03918 437 KCPVCGREL-TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEK--LK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 280 KEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALqqrelaLKEQNSTFMNSA 359
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESV 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 360 RMLEKARQQLQE------EILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHspqlsr 433
Cdd:PRK03918 588 EELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY------ 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 434 rmREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQqctaeqstvvtKEEVDTLRLKIEELEAERS 513
Cdd:PRK03918 662 --EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA-----------KKELEKLEKALERVEELRE 728
|
....
gi 525013811 514 KLAE 517
Cdd:PRK03918 729 KVKK 732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
37-532 |
9.92e-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: 45.88 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 37 SQSSLQMQYQQRMQLEEQAGQIHSKSQLLQVEREKMQMELS---HKRARIELEKAANTNARNYEREA--DRNQELLTRIK 111
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekEQNKRLWDRDTGNSITIDHLRREldDRNMEVQRLEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 112 QYQEREAEAENKLKEQMEMNKSYKKSMETMSkkiqekeSKLAEANETITVLKGKISELqwniMNQEMQMTSQDSEKQELM 191
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLEKVS-------SLTAQLESTKEMLRKVVEEL----TAKKMTLESSERTVSDLT 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 192 EQLDIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQKL--SQQEHDALivknmKAELARFPKMERELRQLKEEnayf 269
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLrnVQTECEAL-----KLQMAEKDKVIEILRQQIEN---- 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 270 reMKENNGLLKEEVEGLQRKLERYEKvqaqlvtvELENEKLlgKLQSWEKLDQSTGLNIRtpdDLSRQIVALQQRELALK 349
Cdd:pfam15921 574 --MTQLVGQHGRTAGAMQVEKAQLEK--------EINDRRL--ELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLV 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 350 EQNSTFMNSARMLEKARQQLQEEILSVQSQLldeKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSP 429
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTSRNEL---NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 430 QL-----SRRMREAEDMVQKLHAHNAELEAQLS--QVLEEVGSHKQRAEMLEVEMKVLKSQqctaEQSTVVTkeEVDTLR 502
Cdd:pfam15921 716 KSmegsdGHAMKVAMGMQKQITAKRGQIDALQSkiQFLEEAMTNANKEKHFLKEEKNKLSQ----ELSTVAT--EKNKMA 789
|
490 500 510
....*....|....*....|....*....|
gi 525013811 503 LKIEELEAERSKLAEENRSLEMKLEKLTLQ 532
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-309 |
1.40e-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: 44.75 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 104 QELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQE------ 177
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelael 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 178 ---MQMTSQDSEKQELMEQLDIEKKKWQEASQQiQTLQASQSLLAEYEQKIKDLEQKLSQQEHDALIVKNMKAELARfpK 254
Cdd:COG4942 110 lraLYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--E 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 525013811 255 MERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENEK 309
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
89-265 |
1.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 89 ANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKE---------QMEMNKSYKKSMETMSKKIQEKESKLAEANETI 159
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 160 TVLKGKISELQWNI--MNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQA------------SQSLLAEYEQKI 225
Cdd:COG3206 243 AALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAqiaalraqlqqeAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 525013811 226 KDLEQKLSQQEHDaliVKNMKAELARFPKMERELRQLKEE 265
Cdd:COG3206 323 EALQAREASLQAQ---LAQLEARLAELPELEAELRRLERE 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-536 |
1.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 123 KLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEmqmtsQDSEKQELMEQLDIEKKKWQ 202
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 203 EASQQIQTLQASQSLLAEYEQKIKDLEQKLSQQEHDALivknmkaelarfPKMERELRQLKEEnayFREMKENNGLLKEE 282
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLS------------LATEEELQDLAEE---LEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 283 VEGLQRKLERYEKVQAQLVTvELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARML 362
Cdd:COG4717 215 LEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 363 EKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMV 442
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 443 QKLHAHNAELEAQLSQVLEevgsHKQRAEMLEVEMKVLKSQ---------QCTAEQSTVVTKEEVDTLRLKIEELEAERS 513
Cdd:COG4717 374 ALLAEAGVEDEEELRAALE----QAEEYQELKEELEELEEQleellgeleELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420
....*....|....*....|...
gi 525013811 514 KLAEENRSLEMKLEKLTLQGDYD 536
Cdd:COG4717 450 ELREELAELEAELEQLEEDGELA 472
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
228-528 |
2.60e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 228 LEQKLSQQEHDALIVKNMKAElaRFPKMERE-LRQLKEENAyfREMkENNGLLKEEVEGLQRKLERYEKVQAQLVTVELE 306
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQE--KFEKMEQErLRQEKEEKA--REV-ERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 307 NEKLLGKLQSWEKldqstglnirtpddlSRQIVALQQRELA-----LKEQNSTFMNSARMLEKARQQLQEeilSVQSQLL 381
Cdd:pfam17380 346 RERELERIRQEER---------------KRELERIRQEEIAmeisrMRELERLQMERQQKNERVRQELEA---ARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 382 DEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELS-----PAEHSPQLSR-RMREAEDMVQKLHAHNAELEAQ 455
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMErvrleEQERQQQVERlRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525013811 456 LSQvleevgshKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIeeLEAERSKLAEENRSLEMKLEK 528
Cdd:pfam17380 488 RAE--------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEE 550
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-529 |
4.65e-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: 43.52 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 248 ELARFPKMERELRQLKEENAYFRE-MKENNGLLKEEVEGLQR-KLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTG 325
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEEnIERLDLIIDEKRQQLERlRREREKAERYQALLKEKREYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 326 LNIRTPDDLSRQI----VALQQRELALKEQNSTFMNSARMLEKARQ----QLQEEILSVQSQLLDEKKKREHQEALVRRL 397
Cdd:TIGR02169 241 AIERQLASLEEELekltEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 398 QKRVVLLTKERDGMRAILESYDSEL-SPAEHSPQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVE 476
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIeEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 477 MKVLKSQQCTAEQSTVVTKEEVDTLRLKIE-------ELEAERSKLAEENRSLEMKLEKL 529
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAgieakinELEEEKEDKALEIKKQEWKLEQL 460
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
93-200 |
5.62e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 93 ARNYER-EADRNQELLTRIKQ-YQEREAEAENKlKEQMEMNKSYKKSMETMSKKIQEKESKLaeanetitvlkgKISELQ 170
Cdd:cd03406 165 RRNYEAmEAEKTKLLIAEQHQkVVEKEAETERK-RAVIEAEKDAEVAKIQMQQKIMEKEAEK------------KISEIE 231
|
90 100 110
....*....|....*....|....*....|
gi 525013811 171 wNIMNQEMQMTSQDSEKQELMEQLDIEKKK 200
Cdd:cd03406 232 -DEMHLAREKARADAEYYRALREAEANKLK 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
46-473 |
7.69e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 46 QQRMQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARnyEREADRNQElltRIKQYQEREAEAENKLK 125
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNL--VQTALRQQE---KIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 126 EQMEMnksykksMETMSKKIQEKESKLAEANETITVLKGKISELQW--------NIMNQEMQMTSQDSEKQELMEQLDIE 197
Cdd:COG3096 365 EQEEV-------VEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldvqqtrAIQYQQAVQALEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 198 K-KKWQEASQQiQTLQASQSLLaEYEQKIKDLEQKLSQQEHDALIVKNMKAELARFPKMERElRQLKEENAYFREMKENN 276
Cdd:COG3096 438 NaEDYLAAFRA-KEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTA-RELLRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 277 GLLKEEVEGLQRKLERYEKVQAQLvtvelenekllgklqswEKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFM 356
Cdd:COG3096 515 QQLRAQLAELEQRLRQQQNAERLL-----------------EEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 357 NSARMLEKARQQLQEEILSVQSQlldEKKKREHQEALVrRLQKRVVlltkerdgmrailESYDSELSPAEHSPQLSRRMR 436
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAAR---APAWLAAQDALE-RLREQSG-------------EALADSQEVTAAMQQLLERER 640
|
410 420 430
....*....|....*....|....*....|....*..
gi 525013811 437 EAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEML 473
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
84-452 |
8.80e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 84 ELEKAANTNARNYEREADRNQELLTRIKQ---YQEREAEAENKLKEQmEMNKSYKKSMETMSKKIQEKES------KLAE 154
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDELDKSEKLIKKIKDdinLEECKSKIESTLDDK-DIDECIKKIKELKNHILSEESNidtyfkNADE 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 155 ANETITVLKGKI----SELQWNIMNQEMQMTS-QDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDL- 228
Cdd:TIGR01612 1448 NNENVLLLFKNIemadNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELl 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 229 --------EQKLSQQEHDA-LIVKNMKAELARF----PKMERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERYEK 295
Cdd:TIGR01612 1528 nkysalaiKNKFAKTKKDSeIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEN 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 296 VQAQLVTVELENEKLLGKLQSWEKldQSTGLNIRTPD----DLSRQIVALQQRELALKEQNSTFMNSARMLEkarqQLQE 371
Cdd:TIGR01612 1608 KFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDtelkENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDS 1681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 372 EILSVQSQLldEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLsrrmrEAEDMVQKLHAHNAE 451
Cdd:TIGR01612 1682 EIEKIEIDV--DQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDL-----EGIDPNEKLEEYNTE 1754
|
.
gi 525013811 452 L 452
Cdd:TIGR01612 1755 I 1755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-425 |
8.90e-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: 42.06 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 182 SQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLaeyEQKIKDLEQKLSQQEHDaliVKNMKAELArfpKMERELRQ 261
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARR---IRALEQELA---ALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 262 LKEENAYFREMKENnglLKEEVEGLQRKLERYEkvQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRTPDDLSRQIVAL 341
Cdd:COG4942 88 LEKEIAELRAELEA---QKEELAELLRALYRLG--RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 342 QQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYDSE 421
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 525013811 422 LSPA 425
Cdd:COG4942 243 TPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
69-516 |
9.03e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 69 REKMQMELSHKRARIELEKAANTNARNYEREADRNqELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETmskkIQEK 148
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELA-ELDEEIERYEEQREQARETRDEADEVLEEHEERREE----LETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 149 ESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSllaEYEQKIkdL 228
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE---ELRDRL--E 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 229 EQKLSQQEHdalivkNMKAELARfpkmeRELRQLKEENAyfrEMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENE 308
Cdd:PRK02224 332 ECRVAAQAH------NEEAESLR-----EDADDLEERAE---ELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 309 KLLGKLQswEKLDQSTGLNirtpDDLSRQIVALQQRElalKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKkkrE 388
Cdd:PRK02224 398 ERFGDAP--VDLGNAEDFL----EELREERDELRERE---AELEATLRTARERVEEAEALLEAGKCPECGQPVEGS---P 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 389 HQEALVRRlQKRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQ 468
Cdd:PRK02224 466 HVETIEED-RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 525013811 469 RAEMLEVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEELEAERSKLA 516
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-518 |
1.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 253 PKMERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVElENEKLLGKLQSWEKldqstglnirtpd 332
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLA-ELEYLRAALRLWFA------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 333 dlSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLldekkkREHQEALVRRLQKRVVLLTKERDGMR 412
Cdd:COG4913 287 --QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 413 AILESYDSELSPAEHSPQLSRRmrEAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLevemkvlksqqctaeqstv 492
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAE--EFAALRAEAAALLEALEEELEALEEALAEAEAALRDL------------------- 417
|
250 260
....*....|....*....|....*.
gi 525013811 493 vtKEEVDTLRLKIEELEAERSKLAEE 518
Cdd:COG4913 418 --RRELRELEAEIASLERRKSNIPAR 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-296 |
1.25e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 35 GSSQSSLQMQYQQRMQLEEQAGQIhsKSQLLQVEREKMQMELSHKRARIELEKAANTnARNYEREADRNQELLTRIKQYQ 114
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQL--KEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 115 EREAEAENKLKEQMEmnkSYKKSMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQDSEKQELMEQL 194
Cdd:TIGR02168 848 EELSEDIESLAAEIE---ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 195 DIEKKKWQEASQQIQTLQasQSLLAEYEqkikdleqkLSQQEHDALIVKNMKAELarfpKMERELRQLKEENAY------ 268
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQ--ERLSEEYS---------LTLEEAEALENKIEDDEE----EARRRLKRLENKIKElgpvnl 989
|
250 260 270
....*....|....*....|....*....|...
gi 525013811 269 -----FREMKENNGLLKEEVEGLQRKLERYEKV 296
Cdd:TIGR02168 990 aaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-529 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 347 ALKEQNSTFMNSARMLEKARQQLQ--EEILSVQSQLLDEKKKREHQEALVRRL-----QKRVVLLTKERDGMRAILESYD 419
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 420 SELSpaehspQLSRRMREAEDMVQKLHAHNA--------ELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQST 491
Cdd:COG4913 309 AELE------RLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190
....*....|....*....|....*....|....*...
gi 525013811 492 VVTKEEVDTLRlkiEELEAERSKLAEENRSLEMKLEKL 529
Cdd:COG4913 383 AALRAEAAALL---EALEEELEALEEALAEAEAALRDL 417
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
104-369 |
2.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 104 QELLTRIKQYQERE-------AEAENKLKEQMEMNKSYKK-------------SMETMSKKIQEKESKLAEANETITVLK 163
Cdd:PRK11281 69 LALLDKIDRQKEETeqlkqqlAQAPAKLRQAQAELEALKDdndeetretlstlSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 164 GKISELQWNIMNQEMQMTSQDSEKQELMEQLDIEK--KKWQEASQQIQtLQASQSLL-AEYEQKIKDLE-----QKLSQQ 235
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKvgGKALRPSQRVL-LQAEQALLnAQNDLQRKSLEgntqlQDLLQK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 236 EHDALIvknmkaelARFPKMERELRQLKEE-NAYFREMKEnngllkEEVEGLQRKLERYEKVQAQLVTVELENEKLLGK- 313
Cdd:PRK11281 228 QRDYLT--------ARIQRLEHQLQLLQEAiNSKRLTLSE------KTVQEAQSQDEAARIQANPLVAQELEINLQLSQr 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 314 -LQSWEKLDQSTGLNIRTPDDLSRqivaLQQRELALKEQNSTFMNS---ARMLEKARQQL 369
Cdd:PRK11281 294 lLKATEKLNTLTQQNLRVKNWLDR----LTQSERNIKEQISVLKGSlllSRILYQQQQAL 349
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
40-554 |
3.45e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 40 SLQMQYQQRMQLEEQAGQIHSKSQLLQVEREKMQmelshkrarielekaantnarNYEREADRNQELLTRIKQYQEREAE 119
Cdd:pfam15921 97 SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMA---------------------DIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 120 AENKLKEQMEMNKS-----YKKSM------------------ETMSKKIQEKES-------KLAEA-NETITVLKGKISE 168
Cdd:pfam15921 156 AAKCLKEDMLEDSNtqieqLRKMMlshegvlqeirsilvdfeEASGKKIYEHDSmstmhfrSLGSAiSKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 169 LQWNIMNQEMQMTSQDSEKQELMEQLdiekkkWQEASQQIqtlqasQSLLAEYEQKIKDLEQKLSQQEHDALIVKNmkae 248
Cdd:pfam15921 236 LKGRIFPVEDQLEALKSESQNKIELL------LQQHQDRI------EQLISEHEVEITGLTEKASSARSQANSIQS---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 249 larfpKMERELRQLKEENAYF----REMKENNGLLKEEVEGLQRKLE-RYEKVQAQLVtveLENEKLLGKLQSWEKLDQS 323
Cdd:pfam15921 300 -----QLEIIQEQARNQNSMYmrqlSDLESTVSQLRSELREAKRMYEdKIEELEKQLV---LANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 324 TGlniRTPDDLSRQIVALQQRELAL---KEQNSTF----MNSARMLEKARQQLQEEILSVQS-QLLDEKKKREHQEALVR 395
Cdd:pfam15921 372 SG---NLDDQLQKLLADLHKREKELsleKEQNKRLwdrdTGNSITIDHLRRELDDRNMEVQRlEALLKAMKSECQGQMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 396 RLQ---------KRVVLLTKERDGMRAILESYDSELSPAEHSPQLSRR--------MREAEDMVQKLHAHNAELEAQLSQ 458
Cdd:pfam15921 449 QMAaiqgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltasLQEKERAIEATNAEITKLRSRVDL 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 459 VLEEVGSHKQRAEML---EVEMKVLKSQQCTAEQSTVVTKEEVDTLRLKIEE-------LEAERSKLAEENRSLEMKLEK 528
Cdd:pfam15921 529 KLQELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQE 608
|
570 580
....*....|....*....|....*.
gi 525013811 529 LTLQGDYDPSRTKVLHLSMNPMSLAK 554
Cdd:pfam15921 609 FKILKDKKDAKIRELEARVSDLELEK 634
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
172-300 |
3.48e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 172 NIMNQEMQMTSQDSEKQELM----EQLDIE-KKKWQEAsqqiqtlqasQSLLAEYEQKIKDLEQKLS--QQEHDAL---- 240
Cdd:PRK00409 502 NIIEEAKKLIGEDKEKLNELiaslEELERElEQKAEEA----------EALLKEAEKLKEELEEKKEklQEEEDKLleea 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525013811 241 ------IVKNMKAELARFPKMERELRQLKEENAYFREMKENNGLLKEEVEGLQRKLERYEKVQAQL 300
Cdd:PRK00409 572 ekeaqqAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
85-330 |
3.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 85 LEKAANTNARNYEREADRnqelltrIKQYQEREAEAENKLKEqMEMNKSYKKSMETMSKKIQEKESKLAEANETItvlkg 164
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKR-------ILEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 165 kiselqwnimnqeMQMTSQDSEKQELMEQLDIE-KKKWQEASQQIQTLqasqsllaeyEQKIKDLEQKLSQQEHDALIVK 243
Cdd:PRK12704 92 -------------LQKEENLDRKLELLEKREEElEKKEKELEQKQQEL----------EKKEEELEELIEEQLQELERIS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 244 NMKAELAR---FPKMERELRQlkEENAYFREMKENnglLKEEVEGLQRKL-----ERY--EKVQAQLVT-VELENEKLLG 312
Cdd:PRK12704 149 GLTAEEAKeilLEKVEEEARH--EAAVLIKEIEEE---AKEEADKKAKEIlaqaiQRCaaDHVAETTVSvVNLPNDEMKG 223
|
250
....*....|....*...
gi 525013811 313 KLQSWEkldqstGLNIRT 330
Cdd:PRK12704 224 RIIGRE------GRNIRA 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-293 |
4.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 124 LKEQMEMNKSYKKSMETMSKKIQEKESKLAEAN--------ETITVLKGKISELQwNIMNQEMQMTSQDSEKQELMEQLD 195
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELK 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 196 IEKKKWQEASQQIQTLQASqslLAEYEQKIKDLEQKLSQQEHDALIVKNMK--AELARFPK-----------MERELRQL 262
Cdd:PRK03918 623 KLEEELDKAFEELAETEKR---LEELRKELEELEKKYSEEEYEELREEYLElsRELAGLRAeleelekrreeIKKTLEKL 699
|
170 180 190
....*....|....*....|....*....|....
gi 525013811 263 KEENAYFREMKENNGLLK---EEVEGLQRKLERY 293
Cdd:PRK03918 700 KEELEEREKAKKELEKLEkalERVEELREKVKKY 733
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
50-534 |
4.69e-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: 40.54 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 50 QLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAA---------NTNARNYERE------ADRNQELLTRIKQYQ 114
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAArqklqlekvTTEAKIKKLEedilllEDQNSKLSKERKLLE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 115 EREAEAENKLKEQMEMNKSYKKSMETMSKKIQEKESKLAEANET--------------ITVLKGKISELQWNIMNQEMQM 180
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqelekakrklegeSTDLQEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 181 TSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEyeqkikDLEQKLSQQEHDALIVKNMKAELArfpKMERELR 260
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE------DLESERAARNKAEKQRRDLGEELE---ALKTELE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 261 QLKEENAYFREMKENNgllKEEVEGLQRKLERYEKV-QAQLVTVELENEKLLGKLQswEKLDQStglnirtpddlSRQIV 339
Cdd:pfam01576 310 DTLDTTAAQQELRSKR---EQEVTELKKALEEETRShEAQLQEMRQKHTQALEELT--EQLEQA-----------KRNKA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 340 ALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALVRRLQKRVVLLTKERDGMRAILESYD 419
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 420 SELSP-AEHSPQLSRRMREAEDMVQKLHAHNAELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQSTVVTKEEV 498
Cdd:pfam01576 454 GKNIKlSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL 533
|
490 500 510
....*....|....*....|....*....|....*.
gi 525013811 499 DTLRLKIEELEAERSKLAEENRSLEMKLEKLTLQGD 534
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
31-236 |
5.43e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 31 LATPGSSQSSLQMQYQQRM-QLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIeleKAANTNARNYEREADRNQElltR 109
Cdd:COG4942 11 LALAAAAQADAAAEAEAELeQLQQEIAELEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAALEA---E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 110 IKQYQEREAEAENKLKEQME-----MNKSYK--------------------KSMETMSKKIQEKESKLAEANETITVLKG 164
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEelaelLRALYRlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525013811 165 KISELQWNIMNQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQIQTLQASQSLLAEYEQKIKDLEQKLSQQE 236
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-304 |
6.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 65 LQVEREKMQMELSHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQMEMNKSYKKSMETMSKK 144
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 145 IQEKESKLAEANETITVLKGKISELQWNIMNQEMQMTSQD--SEKQELMEQLDIEKKKWQEASQQiqtlqaSQSLLAEYE 222
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiADAEDEIERLREKREALAELNDE------RRERLAEKR 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 223 QKIKDLEQKLSQQEHDALIVKNMKAELArFPKMERELRQLKEENAyfrEMKENNGLLKEEVEGLQRKLERYEKVQAQLVT 302
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKERAEEY-LEQVEEKLDELREERD---DLQAEIGAVENELEELEELRERREALENRVEA 709
|
..
gi 525013811 303 VE 304
Cdd:PRK02224 710 LE 711
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-529 |
7.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 255 MERELRQL----KEENAYfREMKENNGLLKEEVEGLQRKLERYEKVQAQLVTVELENEKLLGKLQSWEKLDQSTGLNIRT 330
Cdd:PRK03918 147 REKVVRQIlgldDYENAY-KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 331 PDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQLLDEKKKREHQEALvRRLQKRVVLLTKERDG 410
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 411 MRAILESYDSELSPAEHSPQ-LSRRMREAEDMVQKLHahnaELEAQLSQVLEEVGSHKQRAEMLEVEMKVLKSQQCTAEQ 489
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINgIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 525013811 490 STVVTKEEV----DTLRLKIEELEAERSKLAEENRSLEMKLEKL 529
Cdd:PRK03918 381 LTGLTPEKLekelEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
98-423 |
8.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 98 READRNQElltRIKQYQEREAEAENKLKEQMEMnksykksMETMSKKIQEKESKLAEANETITVLKGKISELQWNIMNQE 177
Cdd:PRK04863 341 QTALRQQE---KIERYQADLEELEERLEEQNEV-------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 178 mQMTSQDSEKQELMEQ---------LDIEK-KKWQEASQQiQTLQASQSLLaEYEQKIKDLEQKLSQQEHDALIVKNMKA 247
Cdd:PRK04863 411 -TRAIQYQQAVQALERakqlcglpdLTADNaEDWLEEFQA-KEQEATEELL-SLEQKLSVAQAAHSQFEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 248 ELAR------FPKMERELRQLKEENAYFREMKENNGLLKEEVE---GLQRKLERYEKVQAQLVTVELENEKLLGKL-QSW 317
Cdd:PRK04863 488 EVSRseawdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKNLDDEDELEQLQEELeARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 318 EKLDQSTGLNIRTPDDLSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSvqSQLLDEkkkrehqeaLVRRL 397
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED--SQDVTE---------YMQQL 636
|
330 340
....*....|....*....|....*.
gi 525013811 398 QKRVVLLTKERDGMRAILESYDSELS 423
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIE 662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
256-422 |
9.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 256 ERELRQLKEEnayFREMKENNGLLKEEVEGLQRKLERYEKVQaQLVTVELENEKLLGKLQSWE-KLDQstglnIRTPDD- 333
Cdd:COG4913 616 EAELAELEEE---LAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEaELER-----LDASSDd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 334 ---LSRQIVALQQRELALKEQNSTFMNSARMLEKARQQLQEEILSVQSQL--------------LDEKKKREHQEALVRR 396
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaedlarlelralLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*.
gi 525013811 397 LQKRvvlLTKERDGMRAILESYDSEL 422
Cdd:COG4913 767 LREN---LEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
49-227 |
9.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 49 MQLEEQAGQIHSKSQLLQVEREKMQMELSHKRARIELEKAANTNARNYEREADRNQELLTRIKQYQEREAEAENKLKEQM 128
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525013811 129 EMNKSYKKsmETMSKKIQEKESKLAEANETITVLKGKISELQwnimnQEMQMTSQDSEKQELMEQLDIEKKKWQEASQQI 208
Cdd:COG4717 420 ELLEALDE--EELEEELEELEEELEELEEELEELREELAELE-----AELEQLEEDGELAELLQELEELKAELRELAEEW 492
|
170
....*....|....*....
gi 525013811 209 QTLQASQSLLAEYEQKIKD 227
Cdd:COG4717 493 AALKLALELLEEAREEYRE 511
|
|
| |
