|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1236-1756 |
1.85e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1236 IRAEQQTALQRLREEAETLQKAERASLEQKSRRA------LEQLREQL-----EAEERSAQAALRAEKEAEKEATLLQLR 1304
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAellllkLRELEAELeeleaELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1305 EQLE--GERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1382
Cdd:COG1196 274 LELEelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1383 ELSSLLRDKRQEVEREHErkmDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELEsvRQEQDQQL 1462
Cdd:COG1196 352 ELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--LEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1463 EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEH--- 1539
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegf 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1540 ------THLLESKQQLRRAIDDLRVRRVELESQ---------VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1604
Cdd:COG1196 507 legvkaALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1605 PPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVR-------QTRSMRRRQT 1677
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtlegeggSAGGSLTGGS 666
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1678 ALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDED 1756
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1243-1597 |
4.79e-18 |
|
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: 91.27 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1243 ALQRLREEAETLQKAERA---------SLEQKSRRAlEQLREqLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERRE 1313
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIlnelerqlkSLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1314 avaglEKKHSTELEQLCSSLEAkHREVISNLQKKIEGAQQKeeaqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRD-KR 1392
Cdd:TIGR02168 255 -----LEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE--------LYALANEISRLEQQKQILRERLANLERQlEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1393 QEVEREH-ERKMDKMKEEhwqemaeareryEAEERKQRADLLGHLTGELERLRRAHE--RELESVRQEQDQQLEDLRRRH 1469
Cdd:TIGR02168 321 LEAQLEElESKLDELAEE------------LAELEEKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1470 RDQERKLQDLEAELSSrtkdVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK--EEATATRRHLEEAKKEHTHLLESKQ 1547
Cdd:TIGR02168 389 AQLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1548 QLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1597
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1239-1609 |
5.18e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1239 EQQTALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEAtLLQLREQLEGERREAvagl 1318
Cdd:COG4913 285 FAQRRLELLEAELEELR-AELARLEAE-LERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEER---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1319 eKKHSTELEQLCSSLEAK---HREVISNLQKKIEGAQQK---EEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR--- 1389
Cdd:COG4913 358 -ERRRARLEALLAALGLPlpaSAEEFAALRAEAAALLEAleeELEALEEALAEAEAALRDLRRELRELEAEIASLERrks 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1390 --DKRQ-------------------------EVEREHE----------------------------RKMDKMKEEH---W 1411
Cdd:COG4913 437 niPARLlalrdalaealgldeaelpfvgeliEVRPEEErwrgaiervlggfaltllvppehyaaalRWVNRLHLRGrlvY 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1412 QEMAEARERYEAEERKQRA-----------------DLLGHL--------TGELERLRRA--------HERELesvRQEQ 1458
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSlagkldfkphpfrawleAELGRRfdyvcvdsPEELRRHPRAitragqvkGNGTR---HEKD 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1459 DQQleDLRRRH---RDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeATATRRHL 1532
Cdd:COG4913 594 DRR--RIRSRYvlgFDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1533 EEAKKEHTHLLESK---QQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1609
Cdd:COG4913 671 AELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1181-1765 |
2.14e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1181 YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLR--------AQVQSSTEA--FENQIRAEQQTALQRLR-- 1248
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaedarkaEEARKAEDArkAEEARKAEDAKRVEIARka 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1249 EEA---ETLQKAERASLEQKSRRALEQLR--EQLEAEE-RSAQAALRAEKEAEKEatllQLREQLEGERREAVAGLEKKH 1322
Cdd:PTZ00121 1161 EDArkaEEARKAEDAKKAEAARKAEEVRKaeELRKAEDaRKAEAARKAEEERKAE----EARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1323 STEleqlcssLEAKHREVISNLQ--KKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--- 1397
Cdd:PTZ00121 1237 KDA-------EEAKKAEEERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEakk 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1398 --EHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGE--LERLRRAHER-ELESVRQEQDQQLEDLRRRHRDQ 1472
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1473 ERKLQDLEA---ELSSRTKDVKARLAQLNVQEENMRK-EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHThlLESKQQ 1548
Cdd:PTZ00121 1390 KKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE--AKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1549 LRRAIDDLRvRRVELESQVDQLQTQSQRLQKHVSSLE--AEVQRKQNILK--EMAAETNAPPHPEPGLHIEDLRKSLGTN 1624
Cdd:PTZ00121 1468 EAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1625 ENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTK 1704
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798729 1705 VLENVRKNLDEETKHLDEMKsamRKGHDLlkKKEEKLNQLESSLLEEVSDEDTLKGSSIKK 1765
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEK---KKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1248-1604 |
8.43e-15 |
|
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: 80.17 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1248 REEAETLQKAERASLEQKSRRALEQL--REQLEAEERSAQAALraekeaEKEATLLQLREQLEGERREavaglekkhstE 1325
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEM------DRQAAIYAEQERMAMERER-----------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1326 LEQLcsSLEAKHREVISNLQKKIegAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQEVEREHERKMDK 1405
Cdd:pfam17380 350 LERI--RQEERKRELERIRQEEI--AMEISRMRELERLQMERQQKNERVRQELEAARKVK-ILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1406 MKEEhwQEmaeareryeaeERKQRadllghltgELERLRRAHERELESVRQEQ---DQQLEDLRRRHRDQERKLQDLEAE 1482
Cdd:pfam17380 425 IRAE--QE-----------EARQR---------EVRRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1483 lssrtkdvkarlaqlnvqeenmrKEKQLLLDAQRQAALEKEEATATRRHLEEAKK--------EHTHLLESKQQLRRAID 1554
Cdd:pfam17380 483 -----------------------KRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllekemEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1555 DLRVRRVELESQvDQLQTQSQRLQKHVSSLEAeVQRKQNILKEMAAETNA 1604
Cdd:pfam17380 540 EERRKQQEMEER-RRIQEQMRKATEERSRLEA-MEREREMMRQIVESEKA 587
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1182-1647 |
2.22e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLLKT--QLQKAAEEEEKEEETQIREEESQRLAC-------LRAQVQSSTEAFENQIRAEQQTALQRLREEAE 1252
Cdd:PTZ00121 1375 EAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKAAAakkkadeAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1253 TLQKAERASLEQKSRRALEQLREQLEaEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQlcsS 1332
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---A 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1333 LEAKHREVIsnlqKKIEGAQQKEEAQLQESLGRAEQRthQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQ 1412
Cdd:PTZ00121 1531 EEAKKADEA----KKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1413 EMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQ-EQDQQLEDLRRRHRDQERKLQDLEA----ELSSRT 1487
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaEELKKAEEENKIKAAEEAKKAEEDKkkaeEAKKAE 1684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1488 KDVKARLAQLNVQEENMRKEKQLlldaQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVElESQV 1567
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEEL----KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKI 1759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1568 DQLQTQSQRlqkhvsSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSL-----GTNENQEVsssLSLSKEGIDL 1642
Cdd:PTZ00121 1760 AHLKKEEEK------KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFaniieGGKEGNLV---INDSKEMEDS 1830
|
....*
gi 1958798729 1643 SMDSV 1647
Cdd:PTZ00121 1831 AIKEV 1835
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1169-1621 |
3.28e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1169 EEKEEKEEEHWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLR 1248
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1249 EEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQ 1328
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1329 LCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVI----EYEQELSSLLRDKRQEVEREHERKMD 1404
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDEVAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1405 KMKEEHWQEMAEARERYEAEERKQRADL-LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAEL 1483
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALaAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1484 SSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIddlrvrrvEL 1563
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA--------EA 712
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1564 ESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPgLHIEDLRKSL 1621
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELEREL 769
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1221-1584 |
6.58e-14 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 77.69 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAfenqiRAEQQTALQRLREEAETLqKAERASLEQksrrALEQLREQLEaeerSAQAALR-AEKEAEKEAT 1299
Cdd:PRK04863 291 LRRELYTSRRQ-----LAAEQYRLVEMARELAEL-NEAESDLEQ----DYQAASDHLN----LVQTALRqQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1300 LLQLREQLEgERREAVAGL--------EKKHSTELEQLCSsleakhREVISNLQKKIEgAQQKEEAQLQES---LGRAEQ 1368
Cdd:PRK04863 357 LEELEERLE-EQNEVVEEAdeqqeeneARAEAAEEEVDEL------KSQLADYQQALD-VQQTRAIQYQQAvqaLERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1369 RTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER 1442
Cdd:PRK04863 429 LCGLpdlTADNAEDWLEEF----QAKEQEATeelLSLEQKLSVAQAAHSQ-------------FEQAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1443 ----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQER--------------------KLQDLEAELSSRTKDVK 1491
Cdd:PRK04863 492 seawdvarelLRRLREQRHLAEQLQQlRMRLSELEQRLRQQQRaerllaefckrlgknlddedELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1492 ARLAQLNVQEENMR-KEKQLLLDAQRQAALEKE--EATATRRHLEEAKKEHthlLESKQQLRRAIDDLRVRRVELESQVD 1568
Cdd:PRK04863 572 ESVSEARERRMALRqQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEE---FEDSQDVTEYMQQLLERERELTVERD 648
|
410
....*....|....*.
gi 1958798729 1569 QLQTQSQRLQKHVSSL 1584
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1339-1751 |
1.40e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1339 EVISNLQKKIEGAQQ--KEEAQLQESLGRAEQRTHQKVHQVieyeQELSSLLRDKRQEVE--REHERKMDKMKEEhwqem 1414
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEklEKEVKELEELKEE----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1415 aeareryEAEERKQRADLLGHLTGELERLR---------RAHERELESVRQEQDQ---------QLEDLRRRHRDQERKL 1476
Cdd:PRK03918 240 -------IEELEKELESLEGSKRKLEEKIReleerieelKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1477 QDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR------------------QAALEKEEATATRRHLEEAKKE 1538
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhelyeeakakKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1539 HTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH-----VSSLEAEVQRKQNILKEMAAEtnapphpepglh 1613
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAE------------ 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1614 IEDLRKSLGTNENQEvsSSLSLSKEGIDLSMDSVRHFLSAEGVA--VRSAKEFLvrqtrsmrrRQTALKAAQQHWRhela 1691
Cdd:PRK03918 461 LKRIEKELKEIEEKE--RKLRKELRELEKVLKKESELIKLKELAeqLKELEEKL---------KKYNLEELEKKAE---- 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1692 SAQEVDEDLPGtkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1751
Cdd:PRK03918 526 EYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1305-1818 |
1.53e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.70 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1305 EQLEGERREAVAGLEKKHSTELEQLCSsleaKHREVISNLQKKIEGAQQKE---EAQLQESLGRAEQRTHQKVHQVIEYE 1381
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1382 QELSSLlRDKRQEVEREHERKMDKMKEEhwQEMAEARERYEAEERKQRADLLGHLTGELERL-RRAHERELE-SVRQEQD 1459
Cdd:pfam15921 324 STVSQL-RSELREAKRMYEDKIEELEKQ--LVLANSELTEARTERDQFSQESGNLDDQLQKLlADLHKREKElSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1460 QQLED-----------LRRRHRDQERKLQDLEAELSSRTKDVKARLAQ--LNVQEENMRKEKQLLLDAQRQAALEK---- 1522
Cdd:pfam15921 401 KRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1523 -EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaEVQRKQNILKEMAAE 1601
Cdd:pfam15921 481 vEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1602 TNAPphpepglhIEDLRKSLG-----TNENQEVSSSLSLSKEGIDLSMDSVRHFLSaEGVAVRSAKEFLVRQTRSM---- 1672
Cdd:pfam15921 560 KDKV--------IEILRQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRELEARvsdl 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1673 -RRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHL--------DEMKSAMRKGHDLLKKKEEKLNQ 1743
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrnksEEMETTTNKLKMQLKSAQSELEQ 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1744 LESSLLE-EVSDEDTLKGS--SIKKVTFDLSDMDDLSSEsfescpLLHITPTPNSADPNKiHYLSSSLQRISSELNGV 1818
Cdd:pfam15921 711 TRNTLKSmEGSDGHAMKVAmgMQKQITAKRGQIDALQSK------IQFLEEAMTNANKEK-HFLKEEKNKLSQELSTV 781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1367-1606 |
1.88e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1367 EQRTHQKVHQVIEYEQELSSLlrdkRQEVEREhERKMDKMK--EEHWQEMAEARERYEAEerKQRADLLGHLTGELE-RL 1443
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERA----HEALEDA-REQIELLEpiRELAERYAAARERLAEL--EYLRAALRLWFAQRRlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE-K 1522
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1523 EEATATRRHLEEAKKEHTHLLES----KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqnILKEM 1598
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDAL 449
|
....*...
gi 1958798729 1599 AAETNAPP 1606
Cdd:COG4913 450 AEALGLDE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1260-1602 |
2.40e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1260 ASLEQKSRRALEQLREqleAEERSAQAALraekeaeKEATLLQLREQLEGERREAV---AGLEKKHSTELEQLCSSLEAk 1336
Cdd:TIGR02169 166 AEFDRKKEKALEELEE---VEENIERLDL-------IIDEKRQQLERLRREREKAEryqALLKEKREYEGYELLKEKEA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1337 HREVISNLQKKIEGaQQKEEAQLQESLGRAEQRTHqkvhqvieyeqELSSLLRDKRQEVEREHERKMDKMKEEhwqemae 1416
Cdd:TIGR02169 235 LERQKEAIERQLAS-LEEELEKLTEEISELEKRLE-----------EIEQLLEELNKKIKDLGEEEQLRVKEK------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1417 areryeaeerkqradlLGHLTGELERLRRAherelesvrqeqdqqLEDLRRRHRDQERKLQDLEAELSSrtkdVKARLAQ 1496
Cdd:TIGR02169 296 ----------------IGELEAEIASLERS---------------IAEKERELEDAEERLAKLEAEIDK----LLAEIEE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1497 LNVQEENMRKEKQLLLDaqRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQR 1576
Cdd:TIGR02169 341 LEREIEEERKRRDKLTE--EYAELKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340
....*....|....*....|....*.
gi 1958798729 1577 LQKHVSSLEAEVQRKQNILKEMAAET 1602
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEK 443
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1439-1702 |
1.56e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV----------KARLAQLN-----VQEEN 1503
Cdd:TIGR02168 250 EAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqilRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1504 MRKEKQLLLDAQRQAALEKEEATATRRH------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1577
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1578 QKHVSSLEAEVQRKQNIlkemaaetnapphpepglhIEDLRKSLGTNENQEVSSSLSLSKEGIdlsmdsvrHFLSAEGVA 1657
Cdd:TIGR02168 406 EARLERLEDRRERLQQE-------------------IEELLKKLEEAELKELQAELEELEEEL--------EELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798729 1658 VRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPG 1702
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1182-1780 |
1.59e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEqqtALQRLREEAETLQKAERAS 1261
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1262 lEQKSRRALEQLREQLEAEERSAQAALR----AEKEAEKEATLLQLREQLEGERREA----VAGLEKKHSTELEQlcssl 1333
Cdd:PTZ00121 1352 -AEAAADEAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKAdelkKAAAAKKKADEAKK----- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1334 EAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEqELSSLLRDKRQEVE-----REHERKMDKMKE 1408
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEakkkaEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1409 EhwQEMAEARERYEAEERKQRADLL--GHLTGELERLRRAHE-------RELESVRQ-EQDQQLEDLRRRHRDQERKLQD 1478
Cdd:PTZ00121 1505 A--AEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEkkkadelKKAEELKKaEEKKKAEEAKKAEEDKNMALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1479 LEaELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRV 1558
Cdd:PTZ00121 1583 AE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1559 RRVELESQVDQLQTQSQRLQKHvsslEAEVQRKQNILKEMAAETNapphpepglHIEDLRKSlgtnENQEVSSSLSLSKE 1638
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAK---------KAEELKKK----EAEEKKKAEELKKA 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1639 gidlsmDSVRHFLSAEgvAVRSAKEfLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGT------KVLENVRKN 1712
Cdd:PTZ00121 1725 ------EEENKIKAEE--AKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieeeldEEDEKRRME 1795
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1713 LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKVTFDLSDMDDLSSES 1780
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1161-1748 |
6.49e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1161 EEEEEEEEEEKEEKEEEHWLYQQKEKSLS-LLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAE 1239
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1240 QQTALQRLREEAETLQKAERAsleqkSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQ-LREQLEGERREAVAGL 1318
Cdd:TIGR02168 438 LQAELEELEEELEELQEELER-----LEEALEELREELEEAEQALDAAERELAQLQARLDSLErLQENLEGFSEGVKALL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1319 EKKhsteleqlcsSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEY-EQ---------ELSSLL 1388
Cdd:TIGR02168 513 KNQ----------SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFlKQnelgrvtflPLDSIK 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1389 RDKRQEVEREHerkmdKMKEEHWQEMAEARERYEAEERKQRADLLGH------LTGELERLRRAHEREL----------- 1451
Cdd:TIGR02168 583 GTEIQGNDREI-----LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRivtldgdlvrp 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1452 -----------ESVRQEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLLLDAQRQAAL 1520
Cdd:TIGR02168 658 ggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELEELSRQISALRK 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1521 EKEEATATRRHLEE----AKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILK 1596
Cdd:TIGR02168 734 DLARLEAEVEQLEEriaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1597 EM---------AAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDL--------SMDSVRHFLSAEGVAVR 1659
Cdd:TIGR02168 814 LLneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleALLNERASLEEALALLR 893
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1660 SAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQevdEDLPGTKV-LENVRKNLDEETK-HLDEMKSAMRKGHDLLKKK 1737
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVrIDNLQERLSEEYSlTLEEAEALENKIEDDEEEA 970
|
650
....*....|.
gi 1958798729 1738 EEKLNQLESSL 1748
Cdd:TIGR02168 971 RRRLKRLENKI 981
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1427-1766 |
8.79e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 69.16 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1427 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1506
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1586
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1587 EVQR-----KQNILKEMAAETN-APPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRS 1660
Cdd:COG4372 172 ELQAlseaeAEQALDELLKEANrNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1661 AKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1740
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340
....*....|....*....|....*.
gi 1958798729 1741 LNQLESSLLEEVSDEDTLKGSSIKKV 1766
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1221-1637 |
9.80e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.64 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEE------RSAQAALRAEKE 1293
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLENFDerieraREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1294 AEKEAtLLQLR----EQLEGERREAVAGLEKKhsTELEQLCSSLEAKHREVISNLQKkiegaqqkEEAQLQESLGR---A 1366
Cdd:pfam12128 489 RLQSE-LRQARkrrdQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRK--------EAPDWEQSIGKvisP 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1367 EQRTHQKVHQVIEYEQELSSL------LRDKRQEV------EREHERKMDKMKEehwqemaeaRERYEAEERKQRADLLG 1434
Cdd:pfam12128 558 ELLHRTDLDPEVWDGSVGGELnlygvkLDLKRIDVpewaasEEELRERLDKAEE---------ALQSAREKQAAAEEQLV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1435 HLTGELERLRRAHERELESV--------------RQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQ 1500
Cdd:pfam12128 629 QANGELEKASREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1501 EENMRKEKQLLLD----------AQRQAALEKEEaTATRRHLEEAKKEHTHLLESK--------------QQLRRAIDDL 1556
Cdd:pfam12128 709 KREARTEKQAYWQvvegaldaqlALLKAAIAARR-SGAKAELKALETWYKRDLASLgvdpdviaklkreiRTLERKIERI 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1557 RVRRVELESQVDQLQT----QSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphpepgLHIEDLRKSLGTNENQEVSSS 1632
Cdd:pfam12128 788 AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTK--------LRRAKLEMERKASEKQQVRLS 859
|
....*
gi 1958798729 1633 LSLSK 1637
Cdd:pfam12128 860 ENLRG 864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1439-1601 |
1.10e-11 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 66.87 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELESVRQEQD---QQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLlldaq 1515
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAaleARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRNNKEY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1516 rqAALEKEEATATRRhLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQtqsQRLQKHVSSLEAEVQRKQNIL 1595
Cdd:COG1579 92 --EALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAER 165
|
....*.
gi 1958798729 1596 KEMAAE 1601
Cdd:COG1579 166 EELAAK 171
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1178-1751 |
1.24e-11 |
|
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: 70.38 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1178 HWLYQQKEKSLsllktqlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFENQIR--AEQQTALQRLREEAETLQ 1255
Cdd:TIGR00618 242 HAYLTQKREAQ------------------------EEQLKKQQLLKQLRARIEELRAQEAvlEETQERINRARKAAPLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1256 KAER-ASLEQKSRRALEQLREQ---LEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAvaglEKKHSTELEQLCS 1331
Cdd:TIGR00618 298 HIKAvTQIEQQAQRIHTELQSKmrsRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA----HEVATSIREISCQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1332 SLEAKHRevISNLQKKIEGAQQKEEAQLQESLG-RAEQrtHQKVHQVIEYEQELSSLLRDKRQEverEHERKMDKMKEEH 1410
Cdd:TIGR00618 374 QHTLTQH--IHTLQQQKTTLTQKLQSLCKELDIlQREQ--ATIDTRTSAFRDLQGQLAHAKKQQ---ELQQRYAELCAAA 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1411 WQEmaeareryeaeerkqradllghlTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKlqdleaelssrtKDV 1490
Cdd:TIGR00618 447 ITC-----------------------TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK------------KAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1491 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeatATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL 1570
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDNPG---PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1571 QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE---------------PGLHIEDLRKSLGTNENQEVSSSLSL 1635
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlaceqhallrklqPEQDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1636 SKEGIDLSMDSVRHflsaegvAVRSAKEFlvrQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDe 1715
Cdd:TIGR00618 649 HALQLTLTQERVRE-------HALSIRVL---PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD- 717
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958798729 1716 etKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1751
Cdd:TIGR00618 718 --REFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1430-1769 |
1.24e-11 |
|
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: 70.48 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1430 ADLLGHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRK 1506
Cdd:TIGR02169 680 RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLD--AQRQAALEKEEAtatrrhlEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSL 1584
Cdd:TIGR02169 759 ELKELEAriEELEEDLHKLEE-------ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1585 EAEVQRKQNILKEMAAETNapphpEPGLHIEDLRKSLGTNENQEVSSSLS---LSKEGIDLSMDsvRHFLSAEGVAVRSA 1661
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIK-----SIEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKE--RDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1662 KEFLVRQTRSMRRRQTALKAAQQHWRHELAS----AQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSA-MR-------- 1728
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEiedpKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnMLaiqeyeev 984
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958798729 1729 -KGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKvTFD 1769
Cdd:TIGR02169 985 lKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME-AFE 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1318-1766 |
1.50e-11 |
|
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: 69.66 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1318 LEKKHsTELEQLCSSLEAKHREVISNLQKKiegaqQKEEAQLQESLgraeQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1397
Cdd:TIGR04523 209 KIQKN-KSLESQISELKKQNNQLKDNIEKK-----QQEINEKTTEI----SNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1398 eHERKMDkmkeehwqemaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQL-EDLRRRHRDQERKL 1476
Cdd:TIGR04523 279 -NNKKIK----------------------------------ELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1477 QDLEAELSSRTKdvkaRLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDL 1556
Cdd:TIGR04523 324 EEIQNQISQNNK----IISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1557 RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqniLKEMAAETNApphpepglHIEDLrkslgTNENqevsSSLSLS 1636
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNS--------EIKDL-----TNQD----SVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1637 KEGIDLSMDSVRHFLSAegvavrsakeflvrQTRSMRRRQTALKAAQqhwrhelasaQEVDEDLPGTKVLENVRKNLDEE 1716
Cdd:TIGR04523 456 IKNLDNTRESLETQLKV--------------LSRSINKIKQNLEQKQ----------KELKSKEKELKKLNEEKKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958798729 1717 TKHL----DEMKSAMRKGHDLLKKKEEKLNQLESSLLEevsDEDTLKGSSIKKV 1766
Cdd:TIGR04523 512 VKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDELNK---DDFELKKENLEKE 562
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1216-1601 |
1.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEafENQIRAEQQTALQRLREEAETLQkAERASLEQKSRR------ALEQLREQLEAEERSAQAALR 1289
Cdd:COG4717 71 KELKELEEELKEAEE--KEEEYAELQEELEELEEELEELE-AELEELREELEKlekllqLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1290 AEKEAEKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQkEEAQLQESLGRAEQR 1369
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAEL-----AELQEELEELLEQLSLATEEELQDLAEELEELQQ-RLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1370 THQKVHQVIEYEQELSSLlrDKRQEVEREH----------------------------------------ERKMDKMKEE 1409
Cdd:COG4717 222 LEELEEELEQLENELEAA--ALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1410 HWQEMAEARERYEAEERKQRAdllghLTGELERLRRAHERELESVRqEQDQQLEDLRRRHRDQERklQDLEAELSSRTKD 1489
Cdd:COG4717 300 LGKEAEELQALPALEELEEEE-----LEELLAALGLPPDLSPEELL-ELLDRIEELQELLREAEE--LEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1490 VKARLAQLNVQEENMRKEKqlLLDAQRQAALEKEEATATRRhLEEAKKEHTHLLE--SKQQLRRAIDDLRVRRVELESQV 1567
Cdd:COG4717 372 IAALLAEAGVEDEEELRAA--LEQAEEYQELKEELEELEEQ-LEELLGELEELLEalDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958798729 1568 DQLQTQSQRLQKHVSSLE---------AEVQRKQNILKEMAAE 1601
Cdd:COG4717 449 EELREELAELEAELEQLEedgelaellQELEELKAELRELAEE 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1235-1775 |
2.15e-11 |
|
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: 69.43 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1235 QIRAEQQTALQRLREEAETLQKAERASleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegERREA 1314
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQL--STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE---EKAAA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1315 VAGLEKKHS---TELEQLCSSLEaKHREVISNLQKKIEGAQQ--KEE----AQLQESLGRAEQRTHQKVHQVIEYEQELS 1385
Cdd:pfam01576 568 YDKLEKTKNrlqQELDDLLVDLD-HQRQLVSNLEKKQKKFDQmlAEEkaisARYAEERDRAEAEAREKETRALSLARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1386 SLLrDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERELESVRqEQDQQLED- 1464
Cdd:pfam01576 647 EAL-EAKEELERTNKQLRAEMED-----------------LVSSKDDVGKNVHELERSKRALEQQVEEMK-TQLEELEDe 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1465 --------LRRRHRDQ------ERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEA----T 1526
Cdd:pfam01576 708 lqatedakLRLEVNMQalkaqfERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELeaqiD 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1527 ATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRvelesqvDQLQTQSQRLQKHVSSLEAEVQRKQNILK---------- 1596
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELEEARASR-------DEILAQSKESEKKLKNLEAELLQLQEDLAaserarrqaq 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1597 ----EMAAETNAPPHPEPGLHIE----DLRKSLGTNENQEVSSSLSLSKE---GIDLSMDSVRHFLSAEGVA---VRSAK 1662
Cdd:pfam01576 861 qerdELADEIASGASGKSALQDEkrrlEARIAQLEEELEEEQSNTELLNDrlrKSTLQVEQLTTELAAERSTsqkSESAR 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1663 EFLVRQTRSMRRR--------QTALKAAQQHWRHELASA-----QEVDEDLPGTKVLENVRKNL-------DEETKHLDE 1722
Cdd:pfam01576 941 QQLERQNKELKAKlqemegtvKSKFKSSIAALEAKIAQLeeqleQESRERQAANKLVRRTEKKLkevllqvEDERRHADQ 1020
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958798729 1723 MKSAMRKGHDLLKkkeeklnQLESSlLEEVSDEDTLKGSSIKKVTFDLSDMDD 1775
Cdd:pfam01576 1021 YKDQAEKGNSRMK-------QLKRQ-LEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1242-1754 |
2.16e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1242 TALQRLREEAETLQKAERASLE-QKSRRALEQLREQLE-----AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAV 1315
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDaREQIELLEPIRELAEryaaaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1316 AGLEKKHStELEQLCSSLEAKHREvisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrdkrqEV 1395
Cdd:COG4913 305 ARLEAELE-RLEARLDALREELDE----LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------GL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1396 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgELERLRRAHERELESVRQEqdqqLEDLRRRH----RD 1471
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALA--------EAEAALRDLRRELRELEAE----IASLERRKsnipAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1472 QERKLQDLEAELSSRTKDVK--ARLAQLNVQEENMRK--EKQL------LL--DAQRQAALEKEEATATRRHL--EEAK- 1536
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEEERWRGaiERVLggfaltLLvpPEHYAAALRWVNRLHLRGRLvyERVRt 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1537 ---------------------KEHT------HLL---------ESKQQLR---RAI----------------DDLRVRRV 1561
Cdd:COG4913 522 glpdperprldpdslagkldfKPHPfrawleAELgrrfdyvcvDSPEELRrhpRAItragqvkgngtrhekdDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1562 ------------ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILkemAAETNAPPHPEPGLHIEDLRKSLGTNENQev 1629
Cdd:COG4913 602 yvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERR---EALQRLAEYSWDEIDVASAEREIAELEAE-- 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1630 ssslslsKEGIDLSMDSVRHfLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLEnV 1709
Cdd:COG4913 677 -------LERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-L 747
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958798729 1710 RKNLDE--ETKHLDEMKSAMRKG-HDLLKKKEEKLNQLESSLLEEVSD 1754
Cdd:COG4913 748 RALLEErfAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1270-1779 |
2.60e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1270 LEQLREQLEAEERSAQAALRAEK-EAEKEATLLQLREQLEGerreavaglekKHSTELEQLCSSLEAKHREV---ISNLQ 1345
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERvLSDQRGSLDQLKAQIEE-----------KEEKDLHERLNGLESELAELdeeIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1346 KKIEGAQQKEEAqLQESLGRAEQRthqkvhqvieyEQELSSLLR--DKRQEVEREHERKMDKMKEEhwqemaearERYEA 1423
Cdd:PRK02224 227 EQREQARETRDE-ADEVLEEHEER-----------REELETLEAeiEDLRETIAETEREREELAEE---------VRDLR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1424 EERKQRADLLGHLTGELErLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlaqlnvQEEN 1503
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL------EERA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1504 MrkekqlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1583
Cdd:PRK02224 359 E--------ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1584 LEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKE 1663
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1664 FlvrqTRSMRRRQTALKAAQQHwrhelasAQEVDEDlpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQ 1743
Cdd:PRK02224 511 I----ERLEERREDLEELIAER-------RETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958798729 1744 LESSLLEEVSDEDTLkgssiKKVTFDLSDMDDLSSE 1779
Cdd:PRK02224 577 LNSKLAELKERIESL-----ERIRTLLAAIADAEDE 607
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1237-1566 |
5.82e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.10 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1237 RAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAAlRAEKEAEKEATLLQLREQLEGERREAVA 1316
Cdd:pfam13868 44 RLDEMMEEERERALEEEEEKEEE--RKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1317 GLEKKHSTELE-QLCSSLEAKHREvisnlQKKIEgaQQKEEAQLQESLG----RAEQRTHQKVHQVIEYEQELSSLLrdK 1391
Cdd:pfam13868 121 KLEKQRQLREEiDEFNEEQAEWKE-----LEKEE--EREEDERILEYLKekaeREEEREAEREEIEEEKEREIARLR--A 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1392 RQEVEREHERKMDKMKEEHWQEmaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRD 1471
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQE-------------------------EQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1472 QERKLQDLEAElssrtKDVKARLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRR 1551
Cdd:pfam13868 247 LKERRLAEEAE-----REEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGE 318
|
330
....*....|....*...
gi 1958798729 1552 AIDDL---RVRRVELESQ 1566
Cdd:pfam13868 319 RLREEeaeRRERIEEERQ 336
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1227-1754 |
1.01e-10 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 67.08 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1227 SSTEAFENQIRAEQQTALQRLREEAETLQKAeraSLEQKSRraleqlreqLEAEERSAQAALRAEKEAEKEATLLQ---- 1302
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRET---SLQQKMR---------LEAQAMELDALAVAEKAGQAEAEGLRaala 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1303 ----LREQL-EGERREavagLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQK----------EEAQLQESLGRAE 1367
Cdd:pfam07111 126 gaemVRKNLeEGSQRE----LEEIQRLHQEQL-SSLTQAHEEALSSLTSKAEGLEKSlnsletkragEAKQLAEAQKEAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1368 QRTHQ--KVHQVIEYEQELSSLLRD----------KRQEVEREHERKMDKMKeeHWQEMAEARERYEAEERKQRADLLGH 1435
Cdd:pfam07111 201 LLRKQlsKTQEELEAQVTLVESLRKyvgeqvppevHSQTWELERQELLDTMQ--HLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1436 LTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQ------ERKLQDLEAelSSRTKDVKARLAQLNVQEENMRKEKQ 1509
Cdd:pfam07111 279 LALQEEELTRKIQ-PSDSLEPEFPKKCRSLLNRWREKvfalmvQLKAQDLEH--RDSVKQLRGQVAELQEQVTSQSQEQA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1510 LLLDA--QRQAALEKEEATATRRHLE-----EAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV 1581
Cdd:pfam07111 356 ILQRAlqDKAAEVEVERMSAKGLQMElsraqEARRRQQQQTASaEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1582 SSLEAEVQRKQNI---------LKEMAAETNAPPHPEP------GLHIEDLRKslgtnENQEVSSSLSLSKEGIDLSMDS 1646
Cdd:pfam07111 436 NRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAPpvdadlSLELEQLRE-----ERNRLDAELQLSAHLIQQEVGR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1647 VRHFLSAEgvavrsakeflvrqtrsmrrRQTALKAAQQhWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSA 1726
Cdd:pfam07111 511 AREQGEAE--------------------RQQLSEVAQQ-LEQELQRAQESLASV--GQQLEVARQGQQESTEEAASLRQE 567
|
570 580
....*....|....*....|....*....
gi 1958798729 1727 MRKGHDLLKKK-EEKLNQLESSLLEEVSD 1754
Cdd:pfam07111 568 LTQQQEIYGQAlQEKVAEVETRLREQLSD 596
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1138-1591 |
1.48e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1138 EKEEEEEEEKEEEGEEEEKEEKEEEEEEEEEEEkeekeeehwlyQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQR 1217
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1218 LACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKS--RRALEQLREQLEAEERSAQAALRAEKEAE 1295
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAllELLAELLEEAALLEAALAELLEELAEAAA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1296 KEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSL---EAKHREVI---------SNLQKKIEGAQQKEEAQLQESL 1363
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKA 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1364 GRAE---------QRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLG 1434
Cdd:COG1196 572 GRATflpldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1435 HLT-----GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQ 1509
Cdd:COG1196 652 EGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1510 LLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESK-QQLRRAIDDL-RV-------------RRVELESQVDQLQTQS 1574
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERElERLEREIEALgPVnllaieeyeeleeRYDFLSEQREDLEEAR 811
|
490
....*....|....*..
gi 1958798729 1575 QRLQKHVSSLEAEVQRK 1591
Cdd:COG1196 812 ETLEEAIEEIDRETRER 828
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1215-1581 |
4.12e-10 |
|
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: 65.36 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1215 SQRLACLRAQVQSSTEafenqIRAEQQTALQRLREEAETLQKAERAsLEQKSRRALEQLREqleaeersAQAALR-AEKE 1293
Cdd:COG3096 284 SERALELRRELFGARR-----QLAEEQYRLVEMARELEELSARESD-LEQDYQAASDHLNL--------VQTALRqQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1294 AEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAE 1367
Cdd:COG3096 350 ERYQEDLEELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1368 QRTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELE 1441
Cdd:COG3096 427 ALCGLpdlTPENAEDYLAAF----RAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1442 RLRrAHERELESVR-----QEQDQQLEDLRRRHRDQERKLQdleaelssRTKDVKARLAQLNVQEenmrkekQLLLDAQR 1516
Cdd:COG3096 490 RSQ-AWQTARELLRryrsqQALAQRLQQLRAQLAELEQRLR--------QQQNAERLLEEFCQRI-------GQQLDAAE 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1517 QAALEKEEATATRRHLEEAKKEHThllESKQQLRRAIDDLRVRRVELESQVD---QLQTQSQRLQKHV 1581
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLEQLRARIKELAARAPawlAAQDALERLREQS 618
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1182-1489 |
4.62e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLqKAERAS 1261
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1262 LEQKSRRALEQLrEQLEAEERSAQAALRAEKE--AEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLE-AKHR 1338
Cdd:TIGR02168 787 LEAQIEQLKEEL-KALREALDELRAELTLLNEeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEiEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1339 EVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMD----KMKEEHWQEM 1414
Cdd:TIGR02168 866 ELIEELESELEALL-NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRleglEVRIDNLQER 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1415 AEARERYEAEERKQ----RADLLGHLTGELERLRRAHER----------ELESVRQEQD---QQLEDLRRRHRDQERKLQ 1477
Cdd:TIGR02168 945 LSEEYSLTLEEAEAlenkIEDDEEEARRRLKRLENKIKElgpvnlaaieEYEELKERYDfltAQKEDLTEAKETLEEAIE 1024
|
330
....*....|..
gi 1958798729 1478 DLEAELSSRTKD 1489
Cdd:TIGR02168 1025 EIDREARERFKD 1036
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1601 |
7.31e-10 |
|
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: 63.24 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAhERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK------------ 1506
Cdd:COG4942 42 ELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLL------DAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH 1580
Cdd:COG4942 121 PLALLLspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180
....*....|....*....|.
gi 1958798729 1581 VSSLEAEVQRKQNILKEMAAE 1601
Cdd:COG4942 201 LARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1185-1556 |
9.12e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1185 EKSLSLLKTQLqkaaeeeekeeetqireeesQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkaeRASLEQ 1264
Cdd:TIGR02169 687 KRELSSLQSEL--------------------RRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKL----KERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1265 kSRRALEQLREQLEAEERSaQAALRAEKEaEKEATLLQLREQLEG-ERREAVAGLEK--KHSTELEQLCSSLEAKHREVI 1341
Cdd:TIGR02169 742 -LEEDLSSLEQEIENVKSE-LKELEARIE-ELEEDLHKLEEALNDlEARLSHSRIPEiqAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1342 SNLQKKiegaqQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKR--QEVEREHERKMDKMKEEhwqemaeare 1419
Cdd:TIGR02169 819 QKLNRL-----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEelEEELEELEAALRDLESR---------- 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1420 ryeaeerkqradlLGHLTGELERLrRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------- 1492
Cdd:TIGR02169 884 -------------LGDLKKERDEL-EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipee 949
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1493 RLAQLNVQEENMRKEKQLL-LDAQRQAALEKEEATATRrhLEEAKKEHTHLLESKQQLRRAIDDL 1556
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRaLEPVNMLAIQEYEEVLKR--LDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1238-1744 |
1.11e-09 |
|
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: 63.98 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1238 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleAEERSAQAALRAEKEAEKEatllQLREQLEGERREAVAG 1317
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM--QMERDAMADIRRRESQSQE----DLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1318 ------LEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQKEEAQLQE----------SLGRAEQRTHQKVHQVIEY- 1380
Cdd:pfam15921 158 kclkedMLEDSNTQIEQL-RKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmstmhfrSLGSAISKILRELDTEISYl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1381 -------EQELSSLLRDKRQEVE---REHERKMDKMKEEHWQEmaeareryeaeerkqradllghLTGELERLRRAhere 1450
Cdd:pfam15921 237 kgrifpvEDQLEALKSESQNKIElllQQHQDRIEQLISEHEVE----------------------ITGLTEKASSA---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1451 lESVRQEQDQQLEDLRRRHRDQE----RKLQDLEAELSSRTKDVKarlaqlnvqeENMRKEKQLLLDAQRQAALEKEEAT 1526
Cdd:pfam15921 291 -RSQANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELR----------EAKRMYEDKIEELEKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1527 ATRRHLEEAKKEHTHLlesKQQLRRAIDDLRVRRVELESQVDQLQTQSQR----------LQKHVSSLEAEVQRKQNILK 1596
Cdd:pfam15921 360 EARTERDQFSQESGNL---DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhLRRELDDRNMEVQRLEALLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1597 EMAAETNapphpepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQ 1676
Cdd:pfam15921 437 AMKSECQ-------GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1677 TALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQL 1744
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1149-1765 |
1.44e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1149 EEGEEEEKEEKEEEEEEEEEEEKEekeeehwlyqQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLaclrAQVQSS 1228
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKA----------EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA----EEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1229 TEA--FENQIRAEQQTALQRLREEAETLQKAEraslEQKSRRALEQLREQLEAEERSAQAALRAEkEAEKEATLLQLREQ 1306
Cdd:PTZ00121 1215 EEArkAEDAKKAEAVKKAEEAKKDAEEAKKAE----EERNNEEIRKFEEARMAHFARRQAAIKAE-EARKADELKKAEEK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1307 LEGErrEAVAGLEKKHSTELEQlcsslEAKHREVISNLQKKIEGAQQK--------EEAQLQESLGRAEQRTHQKVHQVI 1378
Cdd:PTZ00121 1290 KKAD--EAKKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKKadaakkkaEEAKKAAEAAKAEAEAAADEAEAA 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1379 EYEQELSSL----LRDKRQEVER--EHERKMDKMKEEHWQEMAEARERYEAEERKQRADllgHLTGELERLRRAHERELE 1452
Cdd:PTZ00121 1363 EEKAEAAEKkkeeAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD---EAKKKAEEKKKADEAKKK 1439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1453 SvrqEQDQQLEDLRRRhRDQERKLQDL--EAELSSRTKDVKARLAQLNVQEENMRK--EKQLLLDAQRQAALEKEEATAT 1528
Cdd:PTZ00121 1440 A---EEAKKADEAKKK-AEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEA 1515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1529 RRHLEEAKKEHTHLLESKQ---QLRRA-----IDDLR----VRRVELESQVDQLQTQSQRlqKHVSSLEAEVQRKqnILK 1596
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKkadEAKKAeekkkADELKkaeeLKKAEEKKKAEEAKKAEED--KNMALRKAEEAKK--AEE 1591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1597 EMAAETNAPPHPEPGLHIEDLRKslgtnENQEVSSSLSLSKEgiDLSMDSVRHFLSAEGVAVRSAKEFL-VRQTRSMRRR 1675
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAA 1664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1676 QTALKAAQQHWRHELASAQEVDEdlpgtKVLENVRKNLDEETKHLDEMKSA----MRKGHDLlkKKEEKLNQLESSLLEE 1751
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDE-----KKAAEALKKEAEEAKKAEELKKKeaeeKKKAEEL--KKAEEENKIKAEEAKK 1737
|
650
....*....|....
gi 1958798729 1752 VSDEDTLKGSSIKK 1765
Cdd:PTZ00121 1738 EAEEDKKKAEEAKK 1751
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1227-1670 |
1.94e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.82 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1227 SSTEAFENQIRAEQQTALQrLREEAETlQKAEraslEQKSRRALEQLREQLEAEERSAQAALRAEKEA----EKEATLLQ 1302
Cdd:pfam05483 310 STQKALEEDLQIATKTICQ-LTEEKEA-QMEE----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRleknEDQLKIIT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1303 LREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQ-KKIEGAQQKEEAQLQESLGRAEQRTHQ---KVHQVI 1378
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDleiQLTAIK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1379 EYEQELSSLLRDKRQEVEREHERKM------DKMKEEHwQEMAEARERYEAEERKQRADLLGHLTGElERLRRAHER--- 1449
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIeltahcDKLLLEN-KELTQEASDMTLELKKHQEDIINCKKQE-ERMLKQIENlee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1450 -------ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK 1522
Cdd:pfam05483 542 kemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1523 EEATATRRHLE----EAKKEHTHLLESKQQLRRAID----DLRVRRVELESQVDQLQtQSQRLQKHVSSLEAEV-QRKQN 1593
Cdd:pfam05483 622 KKGSAENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIdKRCQH 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1594 ILKEMAAETNAPPHPEPGLhIEDLRKSLG--TNENQEVSS---SLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQ 1668
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKI-IEERDSELGlyKNKEQEQSSakaALEIELSNIKAELLSLKKQLEIE----KEEKEKLKME 775
|
..
gi 1958798729 1669 TR 1670
Cdd:pfam05483 776 AK 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1222-1539 |
2.30e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1222 RAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLE--QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAT 1299
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1300 LLQL----------------------------------------REQLEGERREAVAGLEKKHSTELEQLCSSLEAKHre 1339
Cdd:COG4717 252 LLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1340 VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQkvHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehWQEMAEARE 1419
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEQAEE--YQELKEELE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1420 RYeaeerkqRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDvkARLAQLNV 1499
Cdd:COG4717 406 EL-------EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798729 1500 QEENMRKEKQLLldAQRQAALEKEEATAtRRHLEEAKKEH 1539
Cdd:COG4717 477 ELEELKAELREL--AEEWAALKLALELL-EEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1429-1758 |
4.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1429 RADLLGHLTGELERLRRAHERELESV---RQEQDQQLEDLRRRHRDQERKLQDLEaELSSRTKDVKARLAQLNVQEENMR 1505
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNlkeLKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1506 KEKQLLLDAQRQAALEKEEATATRR--HLEEAKKEHTHLLESKQQLRRAIDDLRVRRVE------------LESQVDQLQ 1571
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEElleqlslateeeLQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1572 TQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTnenqeVSSSLSLSKEGIDLSMDSVRHF- 1650
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI-----AAALLALLGLGGSLLSLILTIAg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1651 -------LSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRknldeetkHLDEM 1723
Cdd:COG4717 278 vlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD--------RIEEL 349
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798729 1724 KSAMRKGHDLLKKKEEKLNQLE-SSLLEE--VSDEDTL 1758
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEiAALLAEagVEDEEEL 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1222-1390 |
6.77e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1222 RAQVQSSTEAFENQIR------AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAE 1295
Cdd:COG3206 170 REEARKALEFLEEQLPelrkelEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1296 KE-----------ATLLQLREQ---LEGERREAVAGLEKKHST------ELEQLCSSLEAKHREVISNLQKKIEGAQQkE 1355
Cdd:COG3206 250 GSgpdalpellqsPVIQQLRAQlaeLEAELAELSARYTPNHPDvialraQIAALRAQLQQEAQRILASLEAELEALQA-R 328
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798729 1356 EAQLQESLGRAEQRthqkVHQVIEYEQELSSLLRD 1390
Cdd:COG3206 329 EASLQAQLAQLEAR----LAELPELEAELRRLERE 359
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1234-1588 |
6.90e-09 |
|
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: 61.34 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1234 NQIRAEQQTALQRLREEAEtlqKAERASLEQKSR-----RALEQLREQLEAEERsAQAALRAEKEA---EKEATLLQLRE 1305
Cdd:pfam01576 607 DQMLAEEKAISARYAEERD---RAEAEAREKETRalslaRALEEALEAKEELER-TNKQLRAEMEDlvsSKDDVGKNVHE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1306 qLEGERREAVAGLE--KKHSTELE-QLCSSLEAKHRevisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 1382
Cdd:pfam01576 683 -LERSKRALEQQVEemKTQLEELEdELQATEDAKLR-----LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1383 ELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLR----------RAHERELE 1452
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilaqsKESEKKLK 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1453 SVRQEQDQQLEDL-----RRRHRDQERklQDLEAELSSRTKD----------VKARLAQLNVQEENMRKEKQLLLDAQRQ 1517
Cdd:pfam01576 837 NLEAELLQLQEDLaaserARRQAQQER--DELADEIASGASGksalqdekrrLEARIAQLEEELEEEQSNTELLNDRLRK 914
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1518 AALEKE----EATATRRHLEEAKKehthlleSKQQLRRAIDDLRVRRVELESQVDQLQTQSqrlqkhVSSLEAEV 1588
Cdd:pfam01576 915 STLQVEqlttELAAERSTSQKSES-------ARQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAKI 976
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1283-1528 |
7.70e-09 |
|
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: 59.78 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1283 SAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQES 1362
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-AALERR----IAALARRIR-ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1363 LGRAEQRTHQKVHQVIEYEQELSSLLRdkRQEVEREHERKMDKMKEEHWQEMAEARE--RYEAEERKQRADLLGHLTGEL 1440
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1441 ERLRRAHERE---LESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRtkdvKARLAQLNVQEENMRKekqlLLDAQRQ 1517
Cdd:COG4942 163 AALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEA----LIARLEA 234
|
250
....*....|.
gi 1958798729 1518 AALEKEEATAT 1528
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1239-1528 |
9.89e-09 |
|
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: 60.52 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1239 EQQTALQRLREEAETLQKAERASlEQKSRRALEQLREQLEAEeRSAQAALRAEKE---AEKEATLLQLREQ-----LEGE 1310
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAR-EVERRRKLEEAEKARQAE-MDRQAAIYAEQErmaMERERELERIRQEerkreLERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1311 RREAVAgLEKKHSTELEQLCSSLEAKHREVISNL-------------QKKIEGAQ--------QKEEAQlQESLGRAEQR 1369
Cdd:pfam17380 366 RQEEIA-MEISRMRELERLQMERQQKNERVRQELeaarkvkileeerQRKIQQQKvemeqiraEQEEAR-QREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1370 THQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQ---EMAEARERYEAEERKQRADLlghltgELERLRRA 1446
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraEEQRRKILEKELEERKQAMI------EEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1447 HERELEsvrQEQDQQLEDLRRRHRDQERKLQdLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEAT 1526
Cdd:pfam17380 518 LEKEME---ERQKAIYEEERRREAEEERRKQ-QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
..
gi 1958798729 1527 AT 1528
Cdd:pfam17380 594 TT 595
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1215-1755 |
1.78e-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: 60.08 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1215 SQRLACLRAQVQSSTEAFENQIRAeqqtalqrlreeaetlQKAERASLE---QKSRRALEQLREQLEAEERSAQAALRAE 1291
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEE----------------ERKRRDKLTeeyAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1292 KEAEKEATLLQ-LREQLEGERREAVAGLEKKHS--TELEQLCSSLEAKHREVIS---NLQKKIEGAQQKEEaQLQESLGR 1365
Cdd:TIGR02169 388 KDYREKLEKLKrEINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1366 AEQRTHQKVHQVIEYEQELSSLlrdKRQEVEREHERKMdkmkeehWQEMAEARERYEAEERKQRADLLGhLTGELERLRR 1445
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKL---QRELAEAEAQARA-------SEERVRGGRAVEEVLKASIQGVHG-TVAQLGSVGE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1446 AHERELES---------------------------------------VRQEQ---------------------DQQLE-- 1463
Cdd:TIGR02169 536 RYATAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnkMRDERrdlsilsedgvigfavdlvefDPKYEpa 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1464 --------------DLRRRHRDQERkLQDLEAEL-----------------SSRTKDVKARLAQLNVQEENMRKEKQLLL 1512
Cdd:TIGR02169 616 fkyvfgdtlvvediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1513 DAQRQAaleKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQ 1592
Cdd:TIGR02169 695 SELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1593 NILKEMAAETNAPPHPEPGLHIEDLRKSLgtNENQEVSSSLSLSKEGIDLSMDSvrhfLSAEGVAVRSAKEFLVRQTRSM 1672
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAEL--SKLEEEVSRIEARLREIEQKLNR----LTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1673 RRRQTALKAAQQHWRHELASAQEVDEDLPG-TKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL--- 1748
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAaLRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkak 925
|
....*..
gi 1958798729 1749 LEEVSDE 1755
Cdd:TIGR02169 926 LEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1314-1593 |
1.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1314 AVAGLEKKHSTELEQLcssleakhREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQ 1393
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1394 EVEREhERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAheRELESVRQEQDQQLEDLRRRhrdqe 1473
Cdd:COG4942 87 ELEKE-IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRAD----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1474 rklqdleaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAalekeeatatRRHLEEAKKEHTHLLESkqqlrrai 1553
Cdd:COG4942 159 -----------------LAELAALRAELEAERAELEALLAELEEE----------RAALEALKAERQKLLAR-------- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798729 1554 ddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1593
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1239-1599 |
1.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1239 EQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE-ATLLQLREQLE---GERREA 1314
Cdd:PRK03918 349 ELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiSKITARIGELKkeiKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1315 VAGLEKKHST------EL-EQLCSSLEAKHREVISNLQKKIEGAQQKEEaQLQESLGRAEQ---------RTHQKVHQVI 1378
Cdd:PRK03918 428 IEELKKAKGKcpvcgrELtEEHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKvlkkeseliKLKELAEQLK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1379 EYEQELSSLLRDKRQEVEREHE---RKMDKMKEEhwQEMAEARERYEAEERKQRADL----------LGHLTGELERLRR 1445
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEklkEKLIKLKGE--IKSLKKELEKLEELKKKLAELekkldeleeeLAELLKELEELGF 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1446 AHERELESVRQEqdqqLEDLRRRH---RDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE- 1521
Cdd:PRK03918 585 ESVEELEERLKE----LEPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEe 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1522 ----KEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKhVSSLEAEVQRKQNILKE 1597
Cdd:PRK03918 661 yeelREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKALLKE 739
|
..
gi 1958798729 1598 MA 1599
Cdd:PRK03918 740 RA 741
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1237-1578 |
1.98e-08 |
|
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: 59.80 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1237 RAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE--------ATLLQLREQLE 1308
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEnaelqaelRTLQQAKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1309 GERREAVAGLEK--------------------KHSTELEQLCSSLEAKHREVIsNLQKKIEGAqqkeEAQLQESLGRAEQ 1368
Cdd:pfam01576 405 HKRKKLEGQLQElqarlseserqraelaeklsKLQSELESVSSLLNEAEGKNI-KLSKDVSSL----ESQLQDTQELLQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1369 RTHQKV---HQVIEYEQELSSLLrdKRQEVEREHERKMDKMKEEHWQEMaeareryeAEERKQRADLLGHLTGeLERLRR 1445
Cdd:pfam01576 480 ETRQKLnlsTRLRQLEDERNSLQ--EQLEEEEEAKRNVERQLSTLQAQL--------SDMKKKLEEDAGTLEA-LEEGKK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1446 AHERELESVRQ---EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------RLAQLNVQEENMRKEKQLLLDAQR 1516
Cdd:pfam01576 549 RLQRELEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNlekkqkKFDQMLAEEKAISARYAEERDRAE 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1517 QAALEKE-EATATRRHLEEAKKEHTHLLESKQQLRRAIDDL---------------RVRRVeLESQVDQLQTQSQRLQ 1578
Cdd:pfam01576 629 AEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvgknvheleRSKRA-LEQQVEEMKTQLEELE 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1216-1498 |
2.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFE--NQIRAEQQTALQRLREEAETLQKAERASLEQKS----RRALEQLREQLEAEERSAQAALR 1289
Cdd:COG4913 610 AKLAALEAELAELEEELAeaEERLEALEAELDALQERREALQRLAEYSWDEIDvasaEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1290 AEKEAEK-EATLLQLREQLEgERREAVAGLEKKHsTELEQLCSSLEAKhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ 1368
Cdd:COG4913 690 LEEQLEElEAELEELEEELD-ELKGEIGRLEKEL-EQAEEELDELQDR-------LEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1369 RTHQKvhqviEYEQELSSLLRDKRQEVEREHERKMDKMKE--EHWQemaeareryeaeerkqraDLLGHLTGELERLrRA 1446
Cdd:COG4913 761 DAVER-----ELRENLEERIDALRARLNRAEEELERAMRAfnREWP------------------AETADLDADLESL-PE 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798729 1447 HERELESVRQEQDQQLED--LRRRHRDQERKLQDLEAELSSRTKDVKARLAQLN 1498
Cdd:COG4913 817 YLALLDRLEEDGLPEYEErfKELLNENSIEFVADLLSKLRRAIREIKERIDPLN 870
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1178-1524 |
2.94e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1178 HWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQqtalqRLREEAETLQKA 1257
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE-----RMLKQIENLEEK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1258 ErasleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegerreavaglekKHSTELEQLCSSLeakh 1337
Cdd:pfam05483 543 E-----MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE--------------KQMKILENKCNNL---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1338 REVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVhQVIEYEQELSSLlRDKRQEVEREHERKMD--KMKEEHWQEMA 1415
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASA-KQKFEEIIDNYQKEIEdkKISEEKLLEEV 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1416 EARERYEAEERKQRADL---LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1492
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIdkrCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
330 340 350
....*....|....*....|....*....|..
gi 1958798729 1493 RLAQLNVQEEnmRKEKqLLLDAQRQAALEKEE 1524
Cdd:pfam05483 758 LKKQLEIEKE--EKEK-LKMEAKENTAILKDK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1456-1604 |
3.59e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1456 QEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKqllldAQRQAALEKEEATATR--RHLE 1533
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEI-----KRLELEIEEVEARIKKyeEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798729 1534 EAK--KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1604
Cdd:COG1579 84 NVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1245-1586 |
4.20e-08 |
|
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: 58.81 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1245 QRLREEAETLQKAERASLEQksrRALEQLR---------------EQLEAEERSA-------QAALR-AEKEAEKEATLL 1301
Cdd:COG3096 281 RELSERALELRRELFGARRQ---LAEEQYRlvemareleelsareSDLEQDYQAAsdhlnlvQTALRqQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1302 QLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAEQRTHQ--- 1372
Cdd:COG3096 358 ELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKARALCGLpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1373 KVHQVIEYEQElsslLRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER------- 1442
Cdd:COG3096 435 TPENAEDYLAA----FRAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVERsqawqta 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1443 ---LRRAHERELESVRQEQ-DQQLEDLRRRHRDQERkLQDLEAELSSRTKDVKARLAQLnvqEENMRKEKQLLLDAQRQA 1518
Cdd:COG3096 498 relLRRYRSQQALAQRLQQlRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1519 ALEKEEATATRRHLEEAKKEHTHL------------------------LESKQQLRRAIDDLRVRRVELESQVDQLQTQS 1574
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELaarapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVERDELAARK 653
|
410
....*....|..
gi 1958798729 1575 QRLQKHVSSLEA 1586
Cdd:COG3096 654 QALESQIERLSQ 665
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1234-1601 |
5.10e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1234 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaeersaqaalraEKEAEKEATLLQLREQLEgERre 1313
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEE------------ERKEERKRYRQELEEQIE-ER-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1314 avaglEKKHSTELEQlcsslEAKHREVISNLQKKIegaqQKEEAQLQESLGRAEQRTHQKVHQVIEyeqelsslLRDKRQ 1393
Cdd:pfam13868 86 -----EQKRQEEYEE-----KLQEREQMDEIVERI----QEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1394 EVEREHERKMDKMKEEHWQEMAeareryeaeerKQRADLlghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQe 1473
Cdd:pfam13868 144 ELEKEEEREEDERILEYLKEKA-----------EREEER------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1474 rklqdleaelssrtkdvkarLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEhthlLESKQQLRRAI 1553
Cdd:pfam13868 206 --------------------LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER----RLAEEAEREEE 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1554 DDLRVRRVELES-QVDQLQTQSQRL--QKHVSSLEAEVQ-RKQNILKEMAAE 1601
Cdd:pfam13868 262 EFERMLRKQAEDeEIEQEEAEKRRMkrLEHRRELEKQIEeREEQRAAEREEE 313
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1224-1638 |
5.40e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1224 QVQSSTEAFENQiraEQQTALQRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAeersaqaaLRAEKEaEKEATLL 1301
Cdd:TIGR04523 292 QLKSEISDLNNQ---KEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQ--------LKKELT-NSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1302 QLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQESLgraeqRTHQKVHQVIEYE 1381
Cdd:TIGR04523 360 EKQRELE-EKQNEIEKLKKENQSYKQEI-KNLESQ----INDLESKIQ-NQEKLNQQKDEQI-----KKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1382 QE-LSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghltgelerlrraheRELESVRQEQDQ 1460
Cdd:TIGR04523 428 IErLKETIIKNNSEIKDLTNQDSVKELII---------------------------------------KNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1461 QLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMrKEKQLLLDAQRQAALEKEEAtatrrhLEEAKKEht 1540
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELK----KLNEEKKEL-EEKVKDLTKKISSLKEKIEK------LESEKKE-- 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1541 hlLESK-QQLRRAI--DDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDL 1617
Cdd:TIGR04523 536 --KESKiSDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE------------KKDL 601
|
410 420
....*....|....*....|.
gi 1958798729 1618 RKSLGTNEnqevSSSLSLSKE 1638
Cdd:TIGR04523 602 IKEIEEKE----KKISSLEKE 618
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1205-1589 |
6.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1205 EEETQIREEESQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkAERASLEQKSRRALEQLREQLEAEERSA 1284
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVR-DLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1285 QAALR----AEKEAEKEATLL-----QLREQLEgERREAVAGLEkkhsTELEQLCSSLEaKHREVISNLQKKIEGAqQKE 1355
Cdd:PRK02224 327 RDRLEecrvAAQAHNEEAESLredadDLEERAE-ELREEAAELE----SELEEAREAVE-DRREEIEELEEEIEEL-RER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1356 EAQLQESLGRAEQR------THQKVHqviEYEQELSSLLRDKRQEVErEHERKMDKMK-EEHWQEMAEARERYEAEERKQ 1428
Cdd:PRK02224 400 FGDAPVDLGNAEDFleelreERDELR---EREAELEATLRTARERVE-EAEALLEAGKcPECGQPVEGSPHVETIEEDRE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1429 RADllghltgELERLRRAHERELESVRQEQDqQLEDLRRRHRDQERKLQDLEAeLSSRTKDVKARLAQLNVQEENMRKEK 1508
Cdd:PRK02224 476 RVE-------ELEAELEDLEEEVEEVEERLE-RAEDLVEAEDRIERLEERRED-LEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1509 QLL---LDAQRQAALEK-EEATATRRHLEEAKKEHTHLLESKQQLRR-------------AIDDLRVRRVELESQVDQLQ 1571
Cdd:PRK02224 547 AELeaeAEEKREAAAEAeEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKREALAELNDERR 626
|
410
....*....|....*...
gi 1958798729 1572 TQSQRLQKHVSSLEAEVQ 1589
Cdd:PRK02224 627 ERLAEKRERKRELEAEFD 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1448-1601 |
8.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1448 ERELESVRQEQDQ---QLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEkQLLLDAQ-------RQ 1517
Cdd:COG3883 43 QAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-DVLLGSEsfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1518 AALEKEeATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1597
Cdd:COG3883 122 SALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
....
gi 1958798729 1598 MAAE 1601
Cdd:COG3883 201 LEAE 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1221-1599 |
1.28e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAFENqIRAEQQTALQRLREeAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRA-------EK 1292
Cdd:PRK01156 303 YKNDIENKKQILSN-IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDdLNNQILELEGYEMDYNSYLKSieslkkkIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1293 EAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQR--- 1369
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK----VSSLNQRIRALRENLD-ELSRNMEMLNGQsvc 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1370 ----TH---QKVHQVIEYEQELSSLLRDKRQEVERE------HERKMDKMKEEHWQEMAEARERYEAEERKQRADLlGHL 1436
Cdd:PRK01156 456 pvcgTTlgeEKSNHIINHYNEKKSRLEEKIREIEIEvkdideKIVDLKKRKEYLESEEINKSINEYNKIESARADL-EDI 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1437 TGELERLRRAHERELESVRQEQDQQLEDLRRRHRD-----QERKLQDLEA------ELSSRTKDVKARLAQLNVQEE--- 1502
Cdd:PRK01156 535 KIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalAVISLIDIETnrsrsnEIKKQLNDLESRLQEIEIGFPddk 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1503 ---------------------NMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHT-HLLESK---QQLRRAIDDLR 1557
Cdd:PRK01156 615 syidksireieneannlnnkyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITsRINDIEdnlKKSRKALDDAK 694
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798729 1558 VRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1599
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1224-1590 |
2.02e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.60 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1224 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAerasleQKSRRALE-------QLREQLEAEERSAQAALRAEKEAEK 1296
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERA------KQYQQVIDnfpklsaELRQQLNNERDEPRSVPPNMSTDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1297 EATLLQLREQLEGERREAVAGLEKKH--STELEQLCSSLEAKHR---EVISNLQKKIEGAQQKEEAQLqeSLGRAEQRTH 1371
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDRAReiSDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQL--TALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1372 Q-KVHqvieyEQELSSLLRDKRQEVEReherkmdkMKEEHWQEmaeareryeaeeRKQRADL-LGHLTGELERLR-RAHE 1448
Cdd:PRK10929 186 KaLVD-----ELELAQLSANNRQELAR--------LRSELAKK------------RSQQLDAyLQALRNQLNSQRqREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1449 RELESVRQEQDQQlEDLRRRHRDQERKLQDLEAElssrtkdvkarlaqLNVQEENMrkekQLLLDAQRQAA---LEKEEA 1525
Cdd:PRK10929 241 RALESTELLAEQS-GDLPKSIVAQFKINRELSQA--------------LNQQAQRM----DLIASQQRQAAsqtLQVRQA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1526 TATRRHLEEAKKEHTHLLES-------------KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1590
Cdd:PRK10929 302 LNTLREQSQWLGVSNALGEAlraqvarlpempkPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNR 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1440-1601 |
2.05e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1440 LERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE-----LSSRTKDVKARLAQLNVQeenmrkekqlLLDA 1514
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQ----------LAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1515 QRQAALEKEEATATRRHLEEAKKEHTHLLESK--QQLRRAIDDLRVRR--------------VELESQVDQLQTQ-SQRL 1577
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQlQQEA 311
|
170 180
....*....|....*....|....
gi 1958798729 1578 QKHVSSLEAEVQRKQNILKEMAAE 1601
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQ 335
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1223-1535 |
3.05e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.53 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1223 AQVQSSTEAFENQIRAEQ---QTALQRLREEAETLQK---AERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK 1296
Cdd:pfam09731 161 AHTDSLKEASDTAEISREkatDSALQKAEALAEKLKEvinLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1297 EATLL-QLREQLEGERREAVAGLEKKH---STELEQLCSSLEAK--------HREvISNLQKKIEGAQQKEEAQLQESL- 1363
Cdd:pfam09731 241 LAKLVdQYKELVASERIVFQQELVSIFpdiIPVLKEDNLLSNDDlnsliahaHRE-IDQLSKKLAELKKREEKHIERALe 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1364 GRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghLTGELERL 1443
Cdd:pfam09731 320 KQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--------------------------LRTELERQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEdlRRRHRD------QERKLQDLE-AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR 1516
Cdd:pfam09731 374 AEAHEEHLKDVLVEQEIELQ--REFLQDikekveEERAGRLLKlNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVEA 451
|
330 340
....*....|....*....|
gi 1958798729 1517 -QAALEKEEATATRRHLEEA 1535
Cdd:pfam09731 452 lRSTLEDGSADSRPRPLVRE 471
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1514-1762 |
3.62e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1514 AQRQAALE--KEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1591
Cdd:COG4942 23 AEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1592 QNILKEMAAE---TNAPPHPEPGLHIEDLrkslgtnenQEVSSSLSLskegidlsMDSVRHFLSAEGVAVRSAKEFLVRQ 1668
Cdd:COG4942 103 KEELAELLRAlyrLGRQPPLALLLSPEDF---------LDAVRRLQY--------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1669 TRS---MRRRQTALKAAQQHWRHELASAQEVDEDLpgtkvLENVRKNLDEETKHLDEmksamrkghdlLKKKEEKLNQLE 1745
Cdd:COG4942 166 RAEleaERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAE-----------LQQEAEELEALI 229
|
250
....*....|....*..
gi 1958798729 1746 SSLLEEVSDEDTLKGSS 1762
Cdd:COG4942 230 ARLEAEAAAAAERTPAA 246
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1214-1579 |
3.96e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.86 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1214 ESQRLACLRAQVQSSTEAFEN--QIRAEQQTALQRLREEAETLQK---AERASLEQksrrALEQLREQL-EAEERSAQAA 1287
Cdd:pfam06160 91 IEELLDDIEEDIKQILEELDEllESEEKNREEVEELKDKYRELRKtllANRFSYGP----AIDELEKQLaEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1288 LRAEK----EAEKEatLLQLREQLE--GERREAVAGLEKKHSTEL-EQLcSSLEAKHREVI--------SNLQKKIEGAq 1352
Cdd:pfam06160 167 ELTESgdylEAREV--LEKLEEETDalEELMEDIPPLYEELKTELpDQL-EELKEGYREMEeegyalehLNVDKEIQQL- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1353 qkeEAQLQESLGRAEQRTHQKVHQVIE-YEQELSSLLRDKRQEVEREH--ERKMDKMKE--EHWQEMAEareryeaeerk 1427
Cdd:pfam06160 243 ---EEQLEENLALLENLELDEAEEALEeIEERIDQLYDLLEKEVDAKKyvEKNLPEIEDylEHAEEQNK----------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1428 qradllgHLTGELERLRRA---HERELESVRQEQDqQLEDLRRRHRDQERKLQDLEA---ELSSRTKDVKARLAQLNVQE 1501
Cdd:pfam06160 309 -------ELKEELERVQQSytlNENELERVRGLEK-QLEELEKRYDEIVERLEEKEVaysELQEELEEILEQLEEIEEEQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1502 ENMRKEKQLL----LDAQRQAALEKEEATATRRHLEeakKEH---------THLLESKQQLRRAIDDLRVRRV---ELES 1565
Cdd:pfam06160 381 EEFKESLQSLrkdeLEAREKLDEFKLELREIKRLVE---KSNlpglpesylDYFFDVSDEIEDLADELNEVPLnmdEVNR 457
|
410
....*....|....
gi 1958798729 1566 QVDQLQTQSQRLQK 1579
Cdd:pfam06160 458 LLDEAQDDVDTLYE 471
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1241-1628 |
4.29e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.96 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1241 QTALQRLREEAETLQKAERASleqKSRRALEQLREQLEAEERSAQAALRAEKEAEKEatlLQLREQLEGERREAVAGLEK 1320
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTV---NSIKESETGNLGSESTLLEKAKEIINIEEALKG---FQDPESELEDLAQTSDKLEK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1321 --KHSTELEQ--LCSSLEAKHR--EVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsllrdkrqE 1394
Cdd:COG5185 258 lvEQNTDLRLekLGENAESSKRlnENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELE--------E 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1395 VEREHERKMDKMKEEHWQEmaeaRERYEAEERKQRADLlGHLTGElERLRRAhERELESVRQEQDQQLEDLRRRHRDQER 1474
Cdd:COG5185 330 SKRETETGIQNLTAEIEQG----QESLTENLEAIKEEI-ENIVGE-VELSKS-SEELDSFKDTIESTKESLDEIPQNQRG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1475 KLQDLEAELSSRTKDVKARLAQLNVQ--------EENMRKEKQLLLDAQRQAALEKEEATAtrrHLEEAKKEHthllesK 1546
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQieqatssnEEVSKLLNELISELNKVMREADEESQS---RLEEAYDEI------N 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1547 QQLRRAIDDLRVRRVELESQVDQLQTQsqrLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI---EDLRKSLGT 1623
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIlalENLIPASEL 550
|
....*
gi 1958798729 1624 NENQE 1628
Cdd:COG5185 551 IQASN 555
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1234-1671 |
4.72e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.91 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1234 NQIRAEQQTALQRLRE--EAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATLLQLREQLEGE 1310
Cdd:COG5278 82 EEARAEIDELLAELRSltADNPEQQARLDELEALIDQWLAELEQVIALrRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1311 RREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD 1390
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1391 KRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHR 1470
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1471 DQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLR 1550
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1551 RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVS 1630
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958798729 1631 SSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRS 1671
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1432-1604 |
5.30e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.30 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1432 LLGHLTGELERLRRAHER--ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK-----------------DVKA 1492
Cdd:pfam19220 32 LIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVArlakleaalreaeaakeELRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1493 RLAQLNVQEENMrkEKQLLLDAQRQAALEKE------EATATRRHLEEAKKEhthLLESKQQLRRAIDDLRVRRVELESQ 1566
Cdd:pfam19220 112 ELRDKTAQAEAL--ERQLAAETEQNRALEEEnkalreEAQAAEKALQRAEGE---LATARERLALLEQENRRLQALSEEQ 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798729 1567 VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1604
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1441-1604 |
6.42e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 52.37 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1441 ERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvKARLAqLNVQEENMRKEKqllldAQRQAAL 1520
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE--KAQAA-LTKGNEELAREA-----LAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1521 EKeeatatrrHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL--QTQSQRLQKHV---------SSLEAEVQ 1589
Cdd:pfam04012 96 EK--------QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVqtslgslstSSATDSFE 167
|
170
....*....|....*
gi 1958798729 1590 RKQNILKEMAAETNA 1604
Cdd:pfam04012 168 RIEEKIEEREARADA 182
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1439-1541 |
6.50e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDL---EAELSSRTKDVKARLAQLNVQEENM-RKEKQLLLDA 1514
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEELeELIEEQLQEL 144
|
90 100
....*....|....*....|....*..
gi 1958798729 1515 QRQAALEKEEATAtrRHLEEAKKEHTH 1541
Cdd:PRK12704 145 ERISGLTAEEAKE--ILLEKVEEEARH 169
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1218-1600 |
1.15e-06 |
|
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: 54.19 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1218 LACLRAQVQSSTEAFENQIraEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQA-------AL 1288
Cdd:COG3096 559 LAELEAQLEELEEQAAEAV--EQRSELRQQLEQLRARIKelAARAPAWLAAQDALERLREQSGEALADSQEvtaamqqLL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1289 RAEKEAEKEATLLQLR-EQLEGERRE--AVAGLEkkhSTELEQLCSSL-------------------------EAKHREV 1340
Cdd:COG3096 637 EREREATVERDELAARkQALESQIERlsQPGGAE---DPRLLALAERLggvllseiyddvtledapyfsalygPARHAIV 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1341 ISNLQ--KK--------------IEG-----------AQQKEEA--------QLQES-------LGRAE----------- 1367
Cdd:COG3096 714 VPDLSavKEqlagledcpedlylIEGdpdsfddsvfdAEELEDAvvvklsdrQWRYSrfpevplFGRAArekrleelrae 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1368 ------------------QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERKMDKMKeeHWQEmaeare 1419
Cdd:COG3096 794 rdelaeqyakasfdvqklQRLHQAFSQFVgghlavafapDPEAELA-ALRQRRSELERELAQHRAQEQ--QLRQ------ 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1420 ryEAEERKQRADLLGHLTGELERLRRA-HERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKAR 1493
Cdd:COG3096 865 --QLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDPEQfeqLQAD 942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1494 LAQLNVQEENMRKEKQLLLD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQ 1571
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEvVQRRPHFSYEDA-------VGLLGENSDLNEKlRARLEQAEEARREAREQLRQAQAQYS 1015
|
490 500
....*....|....*....|....*....
gi 1958798729 1572 TQSQRLQKHVSSLEAEVQRKQNILKEMAA 1600
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1114-1556 |
1.50e-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: 53.52 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1114 RLCREEEEEEkeeeeeekeeeeeeekeeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwLYQQKEKSLSLLKt 1193
Cdd:TIGR02168 672 ILERRREIEE--------------------------------------------------------LEEKIEELEEKIA- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1194 qlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASlEQKSRRALEQL 1273
Cdd:TIGR02168 695 -------------------ELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLS 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1274 REQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGErreaVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQ- 1352
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKALREAL-DELRAELTLLNEEAANLRERLEs 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1353 -QKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSlLRDKRQEVEREHERKmDKMKEEHWQEMAEARERYEAEERKQRAD 1431
Cdd:TIGR02168 829 lERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEAL-LNERASLEEALALLRSELEELSEELREL 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1432 L--LGHLTGELERLRR---AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqeENMRK 1506
Cdd:TIGR02168 907 EskRSELRRELEELREklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKIK 982
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EkqllLDAQRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIDDL 1556
Cdd:TIGR02168 983 E----LGPVNLAAIEEYEELKERY--DFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1216-1761 |
1.51e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFEnQIRAEQ---QTALQRLREEAETLQKAERASLEQKSRR--ALEQLREQLEAEErSAQAALRA 1290
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFA-ETRDELkdyREKLEKLKREINELKRELDRLQEELQRLseELADLNAAIAGIE-AKINELEE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1291 EKEA------EKEATLLQLREQLEGERREavagLEKKhSTELEQLCSSLEAKHREVISNL-QKKIEGAQQKEEAQLQESL 1363
Cdd:TIGR02169 442 EKEDkaleikKQEWKLEQLAADLSKYEQE----LYDL-KEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1364 GRAEQRTHQKVHQVIEYEQELSSLLR----------------DKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERK 1427
Cdd:TIGR02169 517 KASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSED 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1428 QRADLLGHL-----------------TGELERLRRAHE----------------------------RELESVRQEQDQQL 1462
Cdd:TIGR02169 597 GVIGFAVDLvefdpkyepafkyvfgdTLVVEDIEAARRlmgkyrmvtlegelfeksgamtggsrapRGGILFSRSEPAEL 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1463 EDLRRRhrdqerkLQDLEAELSS----------RTKDVKARLAQLNVQEENMRKEKQLLldaQRQAALEKEEATATRRHL 1532
Cdd:TIGR02169 677 QRLRER-------LEGLKRELSSlqselrrienRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLKERLEELEEDL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1533 EEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL-----QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNApph 1607
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--- 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1608 pepglhiEDLRKSLGTNENQEVSSSLSLSKEGIDlsmdsvrhflsaegvavrsakeflvrqtrSMRRRQTALKAAQQHWR 1687
Cdd:TIGR02169 824 -------LTLEKEYLEKEIQELQEQRIDLKEQIK-----------------------------SIEKEIENLNGKKEELE 867
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798729 1688 HELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLE---SSLLEEVSDEDTLKGS 1761
Cdd:TIGR02169 868 EELEELEAALRDL--ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1601 |
1.91e-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: 53.14 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1146 EkeeegeeeekeekeeeeeeeeeeekeekeeehwlyqQKEKSLSLLKTQLqkaaeeeekeeetqirEEESQRLACLRAQV 1225
Cdd:TIGR02168 450 E------------------------------------ELQEELERLEEAL----------------EELREELEEAEQAL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1226 QsSTEAFENQIRAEqQTALQRLREEAETLQKAERASLEQKSRRA--LEQLREQLEAEE-------------------RSA 1284
Cdd:TIGR02168 478 D-AAERELAQLQAR-LDSLERLQENLEGFSEGVKALLKNQSGLSgiLGVLSELISVDEgyeaaieaalggrlqavvvENL 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1285 QAALRA----EKEAEKEATLLQLRE----QLEGERREAVAGLEKKHSTELEqlCSSLEAKHREVIS-------------- 1342
Cdd:TIGR02168 556 NAAKKAiaflKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKD--LVKFDPKLRKALSyllggvlvvddldn 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1343 --NLQKKIEG------------------------------AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL--- 1387
Cdd:TIGR02168 634 alELAKKLRPgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELeee 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1388 LRDKRQEVERE----HERKMDKMKEEHWQEmaeARERYEAEERKQRADLLGHLTGELERLR--RAHERELESVRQEQDQQ 1461
Cdd:TIGR02168 714 LEQLRKELEELsrqiSALRKDLARLEAEVE---QLEERIAQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQ 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1462 LEDLRRRHRDQERKLQDLEAELSsrtkDVKARLAQLNVQEENMRKE----KQLLLDAQRQAALEKEEATA-------TRR 1530
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELT----LLNEEAANLRERLESLERRiaatERRLEDLEEQIEELSEDIESlaaeieeLEE 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1531 HLEEAKKEHTHLLESKQQLRRAIDDLRVRRV-------ELESQVDQLQTQSQRLQKHVSSLEAEVQR-KQNI--LKEMAA 1600
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEelseelrELESKRSELRRELEELREKLAQLELRLEGlEVRIdnLQERLS 946
|
.
gi 1958798729 1601 E 1601
Cdd:TIGR02168 947 E 947
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1182-1481 |
1.93e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLL--KTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAER 1259
Cdd:pfam17380 303 QEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1260 ASLEQKSRRalEQLREQLEAEER-SAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLcsSLEAKHR 1338
Cdd:pfam17380 383 LQMERQQKN--ERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV--RLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1339 evisnlQKKIEGAQQKEEAQLQESLG-----RAEQRTHQKVHQVIEYEQElssllRDKRQEVEREHERKMDKMKEEHWQE 1413
Cdd:pfam17380 459 ------QQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKILEKELE-----ERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1414 MAEARERYEAEERKQRADLlghltgELERLRRAHEREL----ESVRQEQDQQLEDLRRRHRDQERKLQDLEA 1481
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQ------EMEERRRIQEQMRkateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1437-1764 |
2.35e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1437 TGELERLRRAHERELESVRQEqdqqLEDLRRRHRDQERKLQDLEAELSsRTKDVKARLAQLNVQEENMRKEKQLLLDAQR 1516
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1517 Q-----AALEK-----EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLE- 1585
Cdd:PRK03918 263 EleeriEELKKeieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEe 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1586 -----AEVQRKQNILKE--------MAAETNAPPHPEP--GLHIEDLRKSLGTNEN--QEVSSSL--------SLSKEGI 1640
Cdd:PRK03918 343 lkkklKELEKRLEELEErhelyeeaKAKKEELERLKKRltGLTPEKLEKELEELEKakEEIEEEIskitarigELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1641 DLsMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTA-LKAAqqhwRHELASAQEVDEDLpgTKVLENVRKNLDEETKH 1719
Cdd:PRK03918 423 EL-KKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRI----EKELKEIEEKERKL--RKELRELEKVLKKESEL 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958798729 1720 LdemksAMRKGHDLLKKKEEKLNQLESSLLEEVSDE-DTLKGSSIK 1764
Cdd:PRK03918 496 I-----KLKELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIK 536
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1264-1530 |
3.41e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1264 QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQlreqlegERREAVAGLEKKHSTELEqlcssLEAKHREvISN 1343
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEID-----VASAERE-IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1344 LQKKIEGAQQ--KEEAQLQESLGRAEQRthqkvhqvieyEQELSSLLRDKRQEvEREHERKMDKMKEEHWQEMAEARERY 1421
Cdd:COG4913 673 LEAELERLDAssDDLAALEEQLEELEAE-----------LEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1422 EAEERKQRADLlghltgeLERLRRAHERELES-VRQEQDQQLEDLRRRHRDQERKL---------------QDLEAELSS 1485
Cdd:COG4913 741 DLARLELRALL-------EERFAAALGDAVEReLRENLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958798729 1486 RTkDVKARLAQLnVQEENMRKE---KQLLLDAQRQ------AALEKEEATATRR 1530
Cdd:COG4913 814 LP-EYLALLDRL-EEDGLPEYEerfKELLNENSIEfvadllSKLRRAIREIKER 865
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1177-1787 |
3.70e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1177 EHWLYQQKEK-SLSLLKTQlqkaaeeeekeEETQIREEESQRLACLRAQVQSSTEAFEnQIRAEQQTA-LQ---RLREEA 1251
Cdd:pfam05483 154 RHLCNLLKETcARSAEKTK-----------KYEYEREETRQVYMDLNNNIEKMILAFE-ELRVQAENArLEmhfKLKEDH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1252 ETLQKaerasLEQKSRRaleqlreqlEAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCS 1331
Cdd:pfam05483 222 EKIQH-----LEEEYKK---------EINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQDENLKE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1332 SLEAKH------REVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQ--------------VIEYEQ---ELSSLL 1388
Cdd:pfam05483 287 LIEKKDhltkelEDIKMSLQRSMS-TQKALEEDLQIATKTICQLTEEKEAQmeelnkakaahsfvVTEFEAttcSLEELL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1389 RDKRQEVER-EHERKMDKM----KEEHWQEMAEARERYEAEERKqradlLGHLTGELERLRRaHERELESVRQEQDQQLE 1463
Cdd:pfam05483 366 RTEQQRLEKnEDQLKIITMelqkKSSELEEMTKFKNNKEVELEE-----LKKILAEDEKLLD-EKKQFEKIAEELKGKEQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1464 DLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEK-----------QLLLDAQR------QAALE----K 1522
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknieltahcdKLLLENKEltqeasDMTLElkkhQ 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1523 EEATATRRHLEEAKKEHTHLLESKQQLRraiDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAET 1602
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1603 NapphpepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAA 1682
Cdd:pfam05483 597 N-------NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1683 QQHWRHELASAQE-VDEDLpgtkvleNVRKNLDEETKH-LDEMKSAMRKGHD--------------LLKKKEEKLNQLES 1746
Cdd:pfam05483 670 EEKLLEEVEKAKAiADEAV-------KLQKEIDKRCQHkIAEMVALMEKHKHqydkiieerdselgLYKNKEQEQSSAKA 742
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958798729 1747 SLLEEVSDEDTLKGSSIKKVTFDLSDMDDLSSESFESCPLL 1787
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1216-1609 |
4.15e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTE---AFENQIRAEQQTALQRL----REEAETLQKAERASLEqksrRALEQLREQLEAEERSAQAA- 1287
Cdd:NF041483 134 QELAERRQTVESHVNenvAWAEQLRARTESQARRLldesRAEAEQALAAARAEAE----RLAEEARQRLGSEAESARAEa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1288 ----LRAEKEAEK----------EAT--LLQLREQLEGERREAvagleKKHSTEL----EQLCSSLEAKHREVISNLQKK 1347
Cdd:NF041483 210 eailRRARKDAERllnaastqaqEATdhAEQLRSSTAAESDQA-----RRQAAELsraaEQRMQEAEEALREARAEAEKV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1348 IEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER-------EHERKMDKMKEEHWQEMAEARER 1420
Cdd:NF041483 285 VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQaladaraEAEKLVAEAAEKARTVAAEDTAA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1421 YEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKARLAQLNVQ 1500
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQA---EQLKGAAKDDTKEYRAKTVELQEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1501 EENMRKEKQLLL------------DAQRQAALEKEEATATRRHL----------------EEAKKEHTHLLESKQQLRRA 1552
Cdd:NF041483 442 ARRLRGEAEQLRaeavaegerirgEARREAVQQIEEAARTAEELltkakadadelrstatAESERVRTEAIERATTLRRQ 521
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1553 IDDL--RVR------RVELESQVDQLQTQSQRlqkHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1609
Cdd:NF041483 522 AEETleRTRaeaerlRAEAEEQAEEVRAAAER---AARELREETERAIAARQAEAAEELTRLHTE 583
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1255-1492 |
4.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1255 QKAERASLEQK---SRRALEQLREQLEAEERSAQAALRAEKEAEKE-ATLLQLREQLEGERREAVAGLEKKhSTELEQLC 1330
Cdd:COG4942 18 QADAAAEAEAEleqLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAEL-EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1331 SSLEAKhREVISNLQKKIEGAQQKEEAQL---QESLGRAEQRThQKVHQVIEYEQELSSLLRDKRQEVEReherkmdkmK 1407
Cdd:COG4942 97 AELEAQ-KEELAELLRALYRLGRQPPLALllsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAA---------L 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1408 EEHWQEMAEARERYEAEERKQRADLLghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRT 1487
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALE-----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*
gi 1958798729 1488 KDVKA 1492
Cdd:COG4942 241 ERTPA 245
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1437-1597 |
4.64e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 49.38 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1437 TGELERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQeenMRKEKQLLldaQR 1516
Cdd:pfam14988 49 TAELQTQLLQKEKEQASLKKEL-QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALL---EK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1517 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaevQRKQNILK 1596
Cdd:pfam14988 122 QLQELRILELGERATRELKRKAQALKLAAKQALSEFCRSIKRENRQLQKELLQLIQETQALEAIKSKLE---NRKQRLKE 198
|
.
gi 1958798729 1597 E 1597
Cdd:pfam14988 199 E 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1216-1597 |
6.06e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSStEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSrraLEQLREQLEaEERSAQAALraekeAE 1295
Cdd:TIGR00606 591 DRLAKLNKELASL-EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD---LERLKEEIE-KSSKQRAML-----AG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1296 KEATLLQLREQLEGERREAVAGLEKKHST--ELEQLCSSLEAKHReVISNLQKKIEGAQQKEEAQLQESLGRAEQRthQK 1373
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTeaELQEFISDLQSKLR-LAPDKLKSTESELKKKEKRRDEMLGLAPGR--QS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1374 VHQVIEyeQELSSLlRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHEReles 1453
Cdd:TIGR00606 738 IIDLKE--KEIPEL-RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ---- 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1454 vrQEQDQQLEDLRRRHRDQERKLQDLEAELssRTKDVKARLAQLNVQEENMRKEK-QLLLDAQRQAALEKEEATATRRHL 1532
Cdd:TIGR00606 811 --QAAKLQGSDLDRTVQQVNQEKQEKQHEL--DTVVSKIELNRKLIQDQQEQIQHlKSKTNELKSEKLQIGTNLQRRQQF 886
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1533 EEAKKEhthLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1597
Cdd:TIGR00606 887 EEQLVE---LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1438-1602 |
6.64e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1438 GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV---KARLAQLNVQEENMRKEKQLLLDA 1514
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeelEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1515 -----QRQAALEKEEATATRRHLEeakkEHTHLLESKQQLRRAIDDLRvrrvELESQVDQLQTQSQRLQKHVSSLEAEVQ 1589
Cdd:pfam07888 124 raaheARIRELEEDIKTLTQRVLE----RETELERMKERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|...
gi 1958798729 1590 RKQNILKEMAAET 1602
Cdd:pfam07888 196 ELRNSLAQRDTQV 208
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1267-1597 |
8.91e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1267 RRALEQLREQLEAE-----ERSAQAALRAEK--------------------EAEKEATLLQLREQLeGERREAVAGLEKK 1321
Cdd:PRK04863 781 RAAREKRIEQLRAEreelaERYATLSFDVQKlqrlhqafsrfigshlavafEADPEAELRQLNRRR-VELERALADHESQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1322 HSTELEQLCSSleakhREVISNLQKKI-------EGAQQKEEAQLQESLGRAEQ-----RTHQKvhQVIEYEQELSSLlr 1389
Cdd:PRK04863 860 EQQQRSQLEQA-----KEGLSALNRLLprlnllaDETLADRVEEIREQLDEAEEakrfvQQHGN--ALAQLEPIVSVL-- 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1390 dkrqeveREHERKMDKMKEEHWQemaearERYEAEERKQRADLLGHLtgeleRLRRAHERELESVR-QEQDQQL-EDLRR 1467
Cdd:PRK04863 931 -------QSDPEQFEQLKQDYQQ------AQQTQRDAKQQAFALTEV-----VQRRAHFSYEDAAEmLAKNSDLnEKLRQ 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1468 RHRDQERKLQDLEAELssrtKDVKARLAQLNvqeenmrkekqllldaQRQAALeKEEATATRRHLEEAKKEHTHL----- 1542
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYN----------------QVLASL-KSSYDAKRQMLQELKQELQDLgvpad 1051
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798729 1543 --LESKqqlrraiddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1597
Cdd:PRK04863 1052 sgAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1182-1401 |
1.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEesQRLACLRAQVQSSTE---AFENQIrAEQQTALQRLREEAETLQKae 1258
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARrirALEQEL-AALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1259 raSLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSLEAKHR 1338
Cdd:COG4942 98 --ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1339 EVISNLQKKIE-----GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHER 1401
Cdd:COG4942 175 ELEALLAELEEeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1238-1517 |
1.16e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1238 AEQQTALQRLREEAETLQKAERASLEQkSRRALEQLREQLEAeersaqaaLRAEKeAEKEATLLQLREQLEGERREAVAG 1317
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELES-LKKENKDLKEKVSA--------LQPEL-TEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1318 LEKKHSTELE-----QLCSSLEAKHREV----------------ISNLQKkiEGAQQKEEA--------QLQESLGRAEQ 1368
Cdd:pfam10174 516 DSKLKSLEIAveqkkEECSKLENQLKKAhnaeeavrtnpeindrIRLLEQ--EVARYKEESgkaqaeveRLLGILREVEN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1369 RTHQKVHQVIEYEQELSSLLRDKRQEVeREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRR--- 1445
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeld 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1446 AHERELESVRQ---EQDQQLEDLRRRHRDQ-----ERKLQDLEAELSSrtKDVKARLAQLN------VQEENM--RKEKQ 1509
Cdd:pfam10174 673 ATKARLSSTQQslaEKDGHLTNLRAERRKQleeilEMKQEALLAAISE--KDANIALLELSsskkkkTQEEVMalKREKD 750
|
....*...
gi 1958798729 1510 LLLDAQRQ 1517
Cdd:pfam10174 751 RLVHQLKQ 758
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.49e-05 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 43.26 E-value: 1.49e-05
10 20 30
....*....|....*....|....*....|
gi 1958798729 58 LPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1440-1594 |
1.53e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.25 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1440 LERLRRAHERELESVRQEqDQQLedlrrrhRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRqAA 1519
Cdd:smart00787 142 LEGLKEGLDENLEGLKED-YKLL-------MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK-EK 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1520 LEKEEatatrRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH----VSSLEAEVQRKQNI 1594
Cdd:smart00787 213 LKKLL-----QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKLLQSL 286
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1221-1377 |
1.54e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAFENQIRAEQQTalqrLREEAETLQKAERASLEQK-SRRALEQLREQLEAE----ERSAQAALRAEKE-- 1293
Cdd:COG1842 10 IRANINALLDKAEDPEKMLDQA----IRDMEEDLVEARQALAQVIaNQKRLERQLEELEAEaekwEEKARLALEKGREdl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1294 ----AEKEATLLQLREQLEgerreavaglekkhsTELEQLcSSLEAKHREVISNLQKKIEGA-QQKEEAQLQESLGRAEQ 1368
Cdd:COG1842 86 areaLERKAELEAQAEALE---------------AQLAQL-EEQVEKLKEALRQLESKLEELkAKKDTLKARAKAAKAQE 149
|
....*....
gi 1958798729 1369 RTHQKVHQV 1377
Cdd:COG1842 150 KVNEALSGI 158
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1367-1594 |
1.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1367 EQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW----QEMAEARERYEAEERKQRADLLGHLTgELER 1442
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELA-EAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1443 LRRAHERELESVRQE-----QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKE-KQLLLDAQR 1516
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1517 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRraiddlRVRRvELESQVDQLQTQSQRLQkhvsslEAEVQRKQNI 1594
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELR------RLER-EVEVARELYESLLQRLE------EARLAEALTV 385
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1169-1759 |
1.62e-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: 50.36 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1169 EEKEekeeehwLYQQKEKSLSLLKTQLQkaaeeEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLR 1248
Cdd:pfam02463 208 KALE-------YYQLKEKLELEEEYLLY-----LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1249 EEAETLQKAERASLEQKSRraLEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKH--STEL 1326
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELeiKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1327 EQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQrTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKM 1406
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1407 KE-EHWQEMAEARERYEAEERKQRADLLGHLTGELER--LRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAEL 1483
Cdd:pfam02463 433 EEeEESIELKQGKLTEEKEELEKQELKLLKDELELKKseDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1484 SSRTKDVKARLAQlnvQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEhtHLLESKQQLRRAIDDLRVRRVEL 1563
Cdd:pfam02463 513 LALIKDGVGGRII---SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1564 ESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLS 1643
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKAS 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1644 MDSVRHFLSAEgvAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKN----LDEETKH 1719
Cdd:pfam02463 668 LSELTKELLEI--QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIneelKLLKQKI 745
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1958798729 1720 LDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLK 1759
Cdd:pfam02463 746 DEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1334-1591 |
1.95e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1334 EAKHREV--ISNLQKKIEGA---QQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE 1408
Cdd:pfam15558 14 LARHKEEqrMRELQQQAALAweeLRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1409 EHWQEmaearerYEAEERKQRadllghltgeLERLRRAHERElESVRQEQDQQL---EDLRRRHRDQERKLQDLEAELSS 1485
Cdd:pfam15558 94 SRWRE-------QAEDQENQR----------QEKLERARQEA-EQRKQCQEQRLkekEEELQALREQNSLQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1486 RTKDVKARLAQLNVQEENMRKE-----KQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRaiddlRVRR 1560
Cdd:pfam15558 156 HKRQLKEREEQKKVQENNLSELlnhqaRKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELRE-----KAQK 230
|
250 260 270
....*....|....*....|....*....|...
gi 1958798729 1561 VELESQVDQLQT--QSQRLQKHVSSLEAEVQRK 1591
Cdd:pfam15558 231 EEEQFQRAKWRAeeKEEERQEHKEALAELADRK 263
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1234-1522 |
2.02e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1234 NQIRAEQQTALQRLREEAETLQKAERASLEQKSR------------RALEQLREQ--LEAEERSAQAA---LRAEKEAEK 1296
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLERARQEAEQRkqcqeqrlkekeEELQALREQnsLQLQERLEEAChkrQLKEREEQK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1297 EATLLQLREQLEGERREAvaGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE-------GAQQKEEAQLQESLGRAEQR 1369
Cdd:pfam15558 168 KVQENNLSELLNHQARKV--LVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEerhrelrEKAQKEEEQFQRAKWRAEEK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1370 THQ-KVHQvieyeqELSSLLRDKRQEVEREHERKMDKMKEEHWQEmaeareryeAEERKQRADLLghLTGELERLRRAHE 1448
Cdd:pfam15558 246 EEErQEHK------EALAELADRKIQQARQVAHKTVQDKAQRARE---------LNLEREKNHHI--LKLKVEKEEKCHR 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798729 1449 RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaqlnvQEENMRKEKQLLLDAQRQAALEK 1522
Cdd:pfam15558 309 EGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVR--------EETNNRTFDKMALEAQLHASLQR 374
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1215-1359 |
2.51e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1215 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAE-----ERSAQAALR 1289
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEER-LVQKEEQLDARaekldNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1290 AEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELeqLCSSLEAKhreviSNLQKKIEGAQQKEEAQL 1359
Cdd:PRK12705 111 EKALSARELELEELEKQLD-NELYRVAGLTPEQARKL--LLKLLDAE-----LEEEKAQRVKKIEEEADL 172
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1240-1765 |
2.62e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1240 QQTALQRLREEAETLQKAErasleQKSRRALEQLREQLEAEERSAqAALRAEKEA------EKEATLLQLREQLE--GER 1311
Cdd:pfam10174 301 KESELLALQTKLETLTNQN-----SDCKQHIEVLKESLTAKEQRA-AILQTEVDAlrlrleEKESFLNKKTKQLQdlTEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1312 REAVAGlekkhstELEQLCSSLEAKHREvISNLQKKIEgaqqkeeaqlqeslgraeqrthqkvhqvieyeqELSSLLRDK 1391
Cdd:pfam10174 375 KSTLAG-------EIRDLKDMLDVKERK-INVLQKKIE---------------------------------NLQEQLRDK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1392 RQEVEREHERkMDKMKEEHWQEMAEARERYEAEERKQRAdllghltgeLERLRRAHERElesvRQEQDQQLEDLRRRHRD 1471
Cdd:pfam10174 414 DKQLAGLKER-VKSLQTDSSNTDTALTTLEEALSEKERI---------IERLKEQRERE----DRERLEELESLKKENKD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1472 QERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAkkehtHLLESKQQLRR 1551
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA-----HNAEEAVRTNP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1552 AIDDlRVRrvELESQVDQLQTQSQRLQkhvssleAEVQRKQNILKEMAAETNapphpepglhieDLRKSLGTNENQEVSS 1631
Cdd:pfam10174 555 EIND-RIR--LLEQEVARYKEESGKAQ-------AEVERLLGILREVENEKN------------DKDKKIAELESLTLRQ 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1632 SLSLSKEGIDLSmdsvrhflSAEGVAVRSAKEFLVRQtrsmRRRQTALKAAQQHWRHE--LASAQEVDEDLPGTKV-LEN 1708
Cdd:pfam10174 613 MKEQNKKVANIK--------HGQQEMKKKGAQLLEEA----RRREDNLADNSQQLQLEelMGALEKTRQELDATKArLSS 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798729 1709 VRKNLDEETKHLDEMKSAMRkghdllKKKEEKLNQLESSLLEEVSDEDT----LKGSSIKK 1765
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERR------KQLEEILEMKQEALLAAISEKDAnialLELSSSKK 735
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1126-1779 |
2.68e-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: 49.58 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1126 EEEEEKEEEEEEEKEEEEEEEKEEEGEEEEKEEKEEEEEEEEEEEKEEKEEEHWLYQQKEKS-----LSLLKTQLQKAAE 1200
Cdd:pfam02463 344 LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKeaqllLELARQLEDLLKE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1201 EEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQK-AERASLEQKSRRALEQLREQLEA 1279
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvKLQEQLELLLSRQKLEERSQKES 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1280 EERSAQAALRAEKEaEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQL 1359
Cdd:pfam02463 504 KARSGLKVLLALIK-DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1360 QESLGRAEQRTHQKVHQVI------EYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLL 1433
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPilnlaqLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1434 GHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLD 1513
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1514 AQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1593
Cdd:pfam02463 743 QKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1594 ILKEMAAETNAPPHPEPGLHIEDLR---------KSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEF 1664
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKleklaeeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1665 LVRQTRSMRRRQTALKAAQqhWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRkghdLLKKKEEKLNQL 1744
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEE--RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR----LLLAKEELGKVN 976
|
650 660 670
....*....|....*....|....*....|....*
gi 1958798729 1745 ESSLLEEVSDEdtlkgssiKKVTFDLSDMDDLSSE 1779
Cdd:pfam02463 977 LMAIEEFEEKE--------ERYNKDELEKERLEEE 1003
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1216-1593 |
2.83e-05 |
|
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: 49.57 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFEnQIRaEQQTALQRLREEA-----ETLQ------KAERASLEQKSR------RALEQLREQLE 1278
Cdd:COG3096 850 RELAQHRAQEQQLRQQLD-QLK-EQLQLLNKLLPQAnlladETLAdrleelREELDAAQEAQAfiqqhgKALAQLEPLVA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1279 AEERSAQ--AALRAEKEAEKEaTLLQLREQLEG-----ERREAVAglekkHSTELEQLCSSleakhreviSNLQKKIEga 1351
Cdd:COG3096 928 VLQSDPEqfEQLQADYLQAKE-QQRRLKQQIFAlsevvQRRPHFS-----YEDAVGLLGEN---------SDLNEKLR-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1352 QQKEEAQLQESlgRAEQRTHQKVHQVIEYEQELSSLL--RDKRQEVEREHERKMdkmkeehwQEMAEARERYEAEERKQR 1429
Cdd:COG3096 991 ARLEQAEEARR--EAREQLRQAQAQYSQYNQVLASLKssRDAKQQTLQELEQEL--------EELGVQADAEAEERARIR 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1430 ADllgHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELS------------SRTKDVKARLA-- 1495
Cdd:COG3096 1061 RD---ELHEELSQNR-SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcavlrlARDNDVERRLHrr 1136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1496 QLNVQE-ENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHL---LESKQQLRRAI-------DD----LRVRR 1560
Cdd:COG3096 1137 ELAYLSaDELRSMSDKALGALRLAVADNEHLRDALRLSEDPRRPERKVqfyIAVYQHLRERIrqdiirtDDpveaIEQME 1216
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958798729 1561 VELESQVDQLQTQSQRLQkhVSS------LEAEVQRKQN 1593
Cdd:COG3096 1217 IELARLTEELTSREQKLA--ISSesvaniIRKTIQREQN 1253
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1430-1624 |
2.87e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.22 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1430 ADLLGHLTGELERLRRAHERELESVRQEQDQQ---LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqEENMRK 1506
Cdd:pfam09787 28 ASLKEGSGVEGLDSSTALTLELEELRQERDLLreeIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQEL---EEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLDAQRQAALEKEEataTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR----------RVELESQVDQL------ 1570
Cdd:pfam09787 105 ERSARREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQltsksqssssQSELENRLHQLtetliq 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1571 -QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphPEPGLHIEDLRKSLGTN 1624
Cdd:pfam09787 182 kQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS----NGTSINMEGISDGEGTR 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1389-1698 |
2.89e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1389 RDKRQEVE---REHERKMDKMKEEH----WQEmaeareryeaeERKQRADLLGHLTGeLERLRRAHERELESVRQEQDQQ 1461
Cdd:pfam12128 217 RLNRQQVEhwiRDIQAIAGIMKIRPeftkLQQ-----------EFNTLESAELRLSH-LHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1462 LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQ-RQAALEKEEATATRRHLEEAKKEHT 1540
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1541 HLLESKQQLRRAIDDLRVRRVE-----LESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIE 1615
Cdd:pfam12128 365 ALTGKHQDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1616 DLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLvRQTRSmrRRQTALKAAQQHWRHELASAQE 1695
Cdd:pfam12128 445 RLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSEL-RQARK--RRDQASEALRQASRRLEERQSA 521
|
...
gi 1958798729 1696 VDE 1698
Cdd:pfam12128 522 LDE 524
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1448-1602 |
3.54e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1448 ERELESVRQEQDQQLEDlrrrhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLlldaqrqaaLEKEEata 1527
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---------LEKRE--- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1528 trRHLEEAKKEHTHLLESKQQLRRAIDDLRvrrvelESQVDQLQtqsqrlqkHVSSLEAEvQRKQNILKEMAAET 1602
Cdd:PRK12704 110 --EELEKKEKELEQKQQELEKKEEELEELI------EEQLQELE--------RISGLTAE-EAKEILLEKVEEEA 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1162-1604 |
3.84e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1162 EEEEE---EEEEKEEKEEEHWLYQQKEKSlSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRA 1238
Cdd:TIGR00618 475 LQTKEqihLQETRKKAVVLARLLELQEEP-CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1239 EQQTaLQRLREEAETLQKAERAsLEQKSRRALEQLrEQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGL 1318
Cdd:TIGR00618 554 ERKQ-RASLKEQMQEIQQSFSI-LTQCDNRSKEDI-PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1319 EKKHSTELEQLCSSLEAKHREVISNLQKKIE---GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQev 1395
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALHALQLTLTQERVRehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE-- 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1396 EREHERKMDKMKEEhWQemaeARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLedLRRRHRDQErk 1475
Cdd:TIGR00618 709 LETHIEEYDREFNE-IE----NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV--TAALQTGAE-- 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1476 LQDLEAELSSRTKDVKAR---LAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRrhLEEakkEHTHLLESKQQLRRA 1552
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDthlLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR--LEE---KSATLGEITHQLLKY 854
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798729 1553 IDDLRvrrvelesQVDQLQTQSQRLQKHVSSLEA----EVQRKQNILKEMAAETNA 1604
Cdd:TIGR00618 855 EECSK--------QLAQLTQEQAKIIQLSDKLNGinqiKIQFDGDALIKFLHEITL 902
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1251-1535 |
4.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1251 AETLQKAERASLEQKSRRALEQLREQLEaeerSAQAALRaekeaEKEATLLQLREQlegerrEAVAGLEKKHSTELEQLc 1330
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLP----ELRKELE-----EAEAALEEFRQK------NGLVDLSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1331 SSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQRTHQKVhqvieyEQELSSLLRDKRQEVEREHERKMDKMKEEH 1410
Cdd:COG3206 222 SELESQ----LAEARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1411 wQEMAEareryeaeerkqradllghLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELsSRTKDV 1490
Cdd:COG3206 291 -PDVIA-------------------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPEL 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798729 1491 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEA 1535
Cdd:COG3206 350 EAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1230-1402 |
4.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1230 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEaeERSAQAALRAEKEAEKEATLLQLREQLEg 1309
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLD--RKLELLEKREEELEKKEKELEQKQQELE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1310 ERREAVAGLEKKHSTELEQlcssleakhrevISNLqkkiegaqQKEEAQlQESLGRAEQrthqkvhqviEYEQELSSLLR 1389
Cdd:PRK12704 128 KKEEELEELIEEQLQELER------------ISGL--------TAEEAK-EILLEKVEE----------EARHEAAVLIK 176
|
170
....*....|...
gi 1958798729 1390 DKRQEVEREHERK 1402
Cdd:PRK12704 177 EIEEEAKEEADKK 189
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1444-1750 |
5.11e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEEN-------MRKEKQLLLDAQR 1516
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasmQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1517 QAALEKEEATATRRhLEEakkehthLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILK 1596
Cdd:PLN02939 116 QTNSKDGEQLSDFQ-LED-------LVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1597 eMAAETNAppHPE-PGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVR-----HFLSAEGVAVRSAKEFLVRqtr 1670
Cdd:PLN02939 188 -LAAQEKI--HVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLlkddiQFLKAELIEVAETEERVFK--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1671 sMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKV------LENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEklnqL 1744
Cdd:PLN02939 262 -LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYdcwwekVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK----L 336
|
....*.
gi 1958798729 1745 ESSLLE 1750
Cdd:PLN02939 337 EASLKE 342
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
5.50e-05 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 41.74 E-value: 5.50e-05
10 20 30
....*....|....*....|....*....|.
gi 1958798729 59 PKGWKPCQNITGDLYYFNFDTGQSIWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1180-1521 |
6.74e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1180 LYQQKEKslsllktqlqkaaeeeekeeetqireeeSQRLACLRAQVQSSTEAFENQIRA--EQQTALQRLREEAETLQKA 1257
Cdd:COG5185 270 LGENAES----------------------------SKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1258 E-RASLEQKSRR---ALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSL 1333
Cdd:COG5185 322 EaEQELEESKREtetGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST-KESLDEIPQNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1334 EAKHREVISNLQKKIeGAQQKEEAQLQeslgRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQE 1413
Cdd:COG5185 401 RGYAQEILATLEDTL-KAADRQIEELQ----RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1414 mAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKAR 1493
Cdd:COG5185 476 -VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG---YAHILALENLIPASELI 551
|
330 340 350
....*....|....*....|....*....|
gi 1958798729 1494 LAQLNVQEENM--RKEKQLLLDAQRQAALE 1521
Cdd:COG5185 552 QASNAKTDGQAanLRTAVIDELTQYLSTIE 581
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1222-1360 |
8.38e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1222 RAQVQSSTEAFENQIRAE---QQTALQRLREEAETLQKAERASL---EQKSRRALEQLREQLEAEERSAQAAlrAEKEAE 1295
Cdd:COG2268 194 IAEIIRDARIAEAEAEREteiAIAQANREAEEAELEQEREIETAriaEAEAELAKKKAEERREAETARAEAE--AAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1296 KEATLLQLREQLEGERREAVAGLEKKhsteleqlcsSLEAKHREVISNLQKKIEG----AQQKEEAQLQ 1360
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEK----------EAEREEAELEADVRKPAEAekqaAEAEAEAEAE 330
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1351-1583 |
8.59e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1351 AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--EHERKMD---KMKEEHWQEMAEARERYEAEE 1425
Cdd:PRK10929 20 ATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERakQYQQVIDnfpKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1426 RKQRADllghltgELE-RLRRAHERELESVR---QEQD-------------QQLEDLRRRHRDQERKLQDL--------E 1480
Cdd:PRK10929 100 PNMSTD-------ALEqEILQVSSQLLEKSRqaqQEQDrareisdslsqlpQQQTEARRQLNEIERRLQTLgtpntplaQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1481 AELSSRTKDVKARLAQLNvqeenmrkekQLLLdAQRQAALEKEEAtatRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRR 1560
Cdd:PRK10929 173 AQLTALQAESAALKALVD----------ELEL-AQLSANNRQELA---RLRSELAKKRSQQLDAYLQALRNQLNSQRQRE 238
|
250 260
....*....|....*....|....*
gi 1958798729 1561 VE--LESqVDQLQTQSQRLQKHVSS 1583
Cdd:PRK10929 239 AEraLES-TELLAEQSGDLPKSIVA 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1504-1760 |
8.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1504 MRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1583
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1584 LEAEVQRKQNilkemaaetnapphpepglHIEDLRKSLGTNENQEVSSSLSLSKEGidlSMDSVRHFLSAEGV--AVRSA 1661
Cdd:COG4942 81 LEAELAELEK-------------------EIAELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFldAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1662 K------EFLVRQTRSMRRRQTALKAAQQhwrhELASAQevdedlpgtKVLENVRKNLDEETKHLDEMKSAMRKghdLLK 1735
Cdd:COG4942 139 QylkylaPARREQAEELRADLAELAALRA----ELEAER---------AELEALLAELEEERAALEALKAERQK---LLA 202
|
250 260
....*....|....*....|....*
gi 1958798729 1736 KKEEKLNQLESSLLEEVSDEDTLKG 1760
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEA 227
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1367-1756 |
1.29e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1367 EQRTHQKVHQVIEYEQELSSLLRDK--RQEVEREHERKMDKMKEEHWQEMAEARERYEAEERK--QRADLLGHLTG---E 1439
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimKLDNEIKALKSrkkQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1440 LERLRRAHERELESVRQEQDQQLEDLRRRH----RDQERKLQDLEAELSSRTKDVK-------------ARLA-QLNVQE 1501
Cdd:TIGR00606 281 MEKDNSELELKMEKVFQGTDEQLNDLYHNHqrtvREKERELVDCQRELEKLNKERRllnqektellveqGRLQlQADRHQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1502 ENMRKEKQLLLDAQRQAALEKEEATA-------------TRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1568
Cdd:TIGR00606 361 EHIRARDSLIQSLATRLELDGFERGPfserqiknfhtlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1569 QLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPphpepglhiEDLRKSLG------TNENQEVSSSLSLSKEGIDL 1642
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD---------QELRKAERelskaeKNSLTETLKKEVKSLQNEKA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1643 SMDSVRHFLSAEGVAVRSAKEFLvRQTRSMRRRQTalKAAQQ----HWRHELASAQEVDeDLPGTKVLENVRKNLDEETK 1718
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQLNHHTTTR-TQMEMLTKDKM--DKDEQirkiKSRHSDELTSLLG-YFPNKKQLEDWLHSKSKEIN 587
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958798729 1719 HLDE---------MKSAMRKGH--DLLKKKEEKLNQLESSLLEEVSDED 1756
Cdd:TIGR00606 588 QTRDrlaklnkelASLEQNKNHinNELESKEEQLSSYEDKLFDVCGSQD 636
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1230-1325 |
1.47e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1230 EAFENQIRAEQQTALQRLREEAETLQKAERASLE-----QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLR 1304
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREVQRQLEIAEREreielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK 335
|
90 100
....*....|....*....|.
gi 1958798729 1305 EQLEGERREAVAGLEKKHSTE 1325
Cdd:COG2268 336 GLAEAEGKRALAEAWNKLGDA 356
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1444-1740 |
1.83e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.18 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEDLRRRhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKE 1523
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRR--DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1524 EATAT---------RRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1594
Cdd:pfam15558 94 SRWREqaedqenqrQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1595 LKEMAaetnapphpepgLHieDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFL---SAEGVAVRSAKEflvrQTRS 1671
Cdd:pfam15558 174 LSELL------------NH--QARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLveeRHRELREKAQKE----EEQF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1672 MRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEK 1740
Cdd:pfam15558 236 QRAKWRAEEKEEERQEHKEALAELADRKI--QQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEK 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1183-1497 |
1.87e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1183 QKEKSLSLLKTQLQKAAeeeekeeetqireeesQRLACLRAQVQSSTEAfenqiRAEQQTALQRLREEAETLQKaERASL 1262
Cdd:COG4372 63 QLEEELEQARSELEQLE----------------EELEELNEQLQAAQAE-----LAQAQEELESLQEEAEELQE-ELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1263 eQKSRRALEQLREQLEAEERSAQAALraekeAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVIS 1342
Cdd:COG4372 121 -QKERQDLEQQRKQLEAQIAELQSEI-----AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1343 NLQKKIEGAQQkEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehwqemAEARERYE 1422
Cdd:COG4372 195 NAEKEEELAEA-EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE------IEELELAI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1423 AEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQL 1497
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1139-1586 |
1.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1139 KEeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwlYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRL 1218
Cdd:COG4717 109 AE----------------------------------------LEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1219 ACLRAQVQSsteafenqiRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK-E 1297
Cdd:COG4717 149 EELEERLEE---------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1298 ATLLQLREQLEGERREAVAGLEKKHSTELEQL------------CSSLEAKHREVISNLQKKIEGA-------QQKEEAQ 1358
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLlallfllLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1359 LQESLGRAEQRTHQKVHQvieyEQELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMaeareryeaeeRKQRADLlghlt 1437
Cdd:COG4717 300 LGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLDRiEELQEL-----------LREAEEL----- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1438 gELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLeaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQ 1517
Cdd:COG4717 360 -EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL-----------KEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798729 1518 AALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLR--VRRVELESQVDQLQTQSQRLQKHVSSLEA 1586
Cdd:COG4717 428 EELEEELEE-LEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1174-1501 |
1.98e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1174 KEEEHWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLAclRAQVQSSTEAFENQIrAEQQTALQRLREEAET 1253
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVE--GSPHVETIEEDRERV-EELEAELEDLEEEVEE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1254 L-QKAERASLEQKSRRALEQLREQLE-AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSteleqlcs 1331
Cdd:PRK02224 494 VeERLERAEDLVEAEDRIERLEERREdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE-------- 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1332 slEA-KHREVISNLQKKIegAQQKEEaqlQESLGRAEQRthqkVHQVIEYEQELSSlLRDKRQEV-EREHERKmDKMKE- 1408
Cdd:PRK02224 566 --EAeEAREEVAELNSKL--AELKER---IESLERIRTL----LAAIADAEDEIER-LREKREALaELNDERR-ERLAEk 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1409 -EHWQEMAEA---RERYEAEERKQRA-DLLGHLTGELERLRRAHER---ELESVRQEQDqQLEDLRRRHRDQERKLQDLE 1480
Cdd:PRK02224 633 rERKRELEAEfdeARIEEAREDKERAeEYLEQVEEKLDELREERDDlqaEIGAVENELE-ELEELRERREALENRVEALE 711
|
330 340
....*....|....*....|....*..
gi 1958798729 1481 A------ELSSRTKDVKARLAQLNVQE 1501
Cdd:PRK02224 712 AlydeaeELESMYGDLRAELRQRNVET 738
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1228-1349 |
2.50e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1228 STEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRaekeaekeatllQLREQ 1306
Cdd:cd16269 178 SKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEqQRELEQKLEDQERSYEEHLR------------QLKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798729 1307 LEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE 1349
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1332-1497 |
2.81e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.13 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1332 SLEAKHREVISNLQKKIEGAQQKEE--AQLQES---------------LGRAEQRTHQKVHQVIEYEQELSSLlRDKRQE 1394
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKliASLKEGsgvegldsstaltleLEELRQERDLLREEIQKLRGQIQQL-RTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1395 VEREHERKMDKMKEehwqemaeareryeaeerkQRADLLGHLTGElERLRRAHERELESVRQEQDQQLEDLRR------- 1467
Cdd:pfam09787 80 LEAQQQEEAESSRE-------------------QLQELEEQLATE-RSARREAEAELERLQEELRYLEEELRRskatlqs 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958798729 1468 RHRDQERKLQDLEAELSSRT------KDVKARLAQL 1497
Cdd:pfam09787 140 RIKDREAEIEKLRNQLTSKSqssssqSELENRLHQL 175
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1174-1750 |
3.05e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1174 KEEEHWL------------------YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFEN- 1234
Cdd:TIGR00606 306 LYHNHQRtvrekerelvdcqrelekLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERg 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1235 -----QIRAEQQTALQRLREEAETLQK--AERASLEQKSRRALEQLREQLEAEERSAQaaLRAEKEAEKEATLLQLREQL 1307
Cdd:TIGR00606 386 pfserQIKNFHTLVIERQEDEAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIE--LKKEILEKKQEELKFVIKEL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1308 EgerrEAVAGLEK--KHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELs 1385
Cdd:TIGR00606 464 Q----QLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME- 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1386 SLLRDKRQEVEReherkMDKMKEEHWQEMaeARERYEAEERKQRADLLGHLTGELERLRraheRELESVRQEQdQQLEDL 1465
Cdd:TIGR00606 539 MLTKDKMDKDEQ-----IRKIKSRHSDEL--TSLLGYFPNKKQLEDWLHSKSKEINQTR----DRLAKLNKEL-ASLEQN 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1466 RRRHRDQERKLQDLEAELSSRTKDVKARLAqLNVQEENMRKEkqlLLDAQRQAALEKEEATATRRHLEEAKKEHT----- 1540
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEE---IEKSSKQRAMLAGATAVYSQFITQLTDENQsccpv 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1541 --HLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLR 1618
Cdd:TIGR00606 683 cqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE------------IPELR 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1619 kslgtNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQTrSMRRRQTALKAAQQHWRHELASAQEVDE 1698
Cdd:TIGR00606 751 -----NKLQKVNRDIQRLKNDIEEQETLLGTIMPEE----ESAKVCLTDVT-IMERFQMELKDVERKIAQQAAKLQGSDL 820
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1699 DLPGTKvlenVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLE 1750
Cdd:TIGR00606 821 DRTVQQ----VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
3.08e-04 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 39.89 E-value: 3.08e-04
10 20 30
....*....|....*....|....*....|.
gi 1958798729 57 PLPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1233-1320 |
3.31e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1233 ENQIRAEQQTAlQRLREEAETLQK---AERASLEQKSRRALEQLREqlEAEERSAQAALRAEKEAEKEatLLQLREQLEG 1309
Cdd:cd06503 32 EEKIAESLEEA-EKAKEEAEELLAeyeEKLAEARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERI--LEQAKAEIEQ 106
|
90
....*....|.
gi 1958798729 1310 ERREAVAGLEK 1320
Cdd:cd06503 107 EKEKALAELRK 117
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1248-1321 |
3.62e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 42.84 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1248 REE--AETLQKAERASLEQKsrRALEQLREQL------------EAEERSAQ--AALRAEKEAEKEATLLQLREQLEGER 1311
Cdd:PRK05759 36 RQKkiADGLAAAERAKKELE--LAQAKYEAQLaearaeaaeiieQAKKRAAQiiEEAKAEAEAEAARIKAQAQAEIEQER 113
|
90
....*....|
gi 1958798729 1312 REAVAGLEKK 1321
Cdd:PRK05759 114 KRAREELRKQ 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1216-1357 |
4.04e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEErsaqaalRAEKEAE 1295
Cdd:COG1579 38 DELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLK-------RRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1296 KEatLLQLREQLEgERREAVAGLEKKHStELEQLCSSLEAKHREVISNLQKKIEGAQQKEEA 1357
Cdd:COG1579 110 DE--ILELMERIE-ELEEELAELEAELA-ELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1444-1601 |
4.11e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.42 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEDLRRRhrDQERK-LQDLEAELSSRTKDVKARlaqlnvQEENMRKEKQLLLDAQRQAAL-- 1520
Cdd:pfam10168 556 REEIQKRVKLLKLQKEQQLQELQSL--EEERKsLSERAEKLAEKYEEIKDK------QEKLMRRCKKVLQRLNSQLPVls 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1521 --EKEEatatrrhleeaKKEHTHLLESKQQLRRAIDDLRVRrveLESQVDQLQTQSQRLQKHVSSLEAEvQRK--QNILK 1596
Cdd:pfam10168 628 daEREM-----------KKELETINEQLKHLANAIKQAKKK---MNYQRYQIAKSQSIRKKSSLSLSEK-QRKtiKEILK 692
|
....*
gi 1958798729 1597 EMAAE 1601
Cdd:pfam10168 693 QLGSE 697
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1435-1569 |
4.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1435 HLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER--------KLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1506
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRqearrereELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLDA-------QRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIddlRVRRVELESQVDQ 1569
Cdd:PRK12705 110 REKALSAReleleelEKQLDNELYRVAGLTP--EQARKLLLKLLDAELEEEKAQ---RVKKIEEEADLEA 174
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1439-1566 |
4.71e-04 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 42.39 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSR--------------TKDVKARLAQLNVQEENM 1504
Cdd:pfam07321 3 RLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEeqrlyaeiqgklvlLKELEKVKQQVALLRENE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1505 RKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1566
Cdd:pfam07321 83 ADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELE 144
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1258-1566 |
5.09e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1258 ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKeatllqlreqLEGERREAVAglEKKHSTELEQLCSSLEAK- 1336
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHN----------SYEEDSELKP--SGQGGLDEEEAFLDRTAKr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1337 HREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHWQEMAE 1416
Cdd:pfam02029 72 EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1417 ARERYEAEERKQRADLlghlTGELERLRRAHERELESVRQEQDQQLED---LRRRHRDQERKLQDLEAELSSRTKDVKAR 1493
Cdd:pfam02029 151 QAEEEGEEEEDKSEEA----EEVPTENFAKEEVKDEKIKKEKKVKYESkvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1494 LAQLNV-----QEENMRKEKQLLLDAQRQ--AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1566
Cdd:pfam02029 227 QGGLSQsqereEEAEVFLEAEQKLEELRRrrQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE 306
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1368-1601 |
5.12e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1368 QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERkmdkmkeehwQEMAEARERYEAEERKQRADLLGHLT 1437
Cdd:PRK04863 813 QRLHQAFSRFIgshlavafeaDPEAELR-QLNRRRVELERALAD----------HESQEQQQRSQLEQAKEGLSALNRLL 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1438 GELERLRR-AHERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKARLAQLNVQEENMRKEKQLL 1511
Cdd:PRK04863 882 PRLNLLADeTLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFAL 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1512 LD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQkhvsSLEAEVQ 1589
Cdd:PRK04863 962 TEvVQRRAHFSYEDA-------AEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLA----SLKSSYD 1030
|
250
....*....|..
gi 1958798729 1590 RKQNILKEMAAE 1601
Cdd:PRK04863 1031 AKRQMLQELKQE 1042
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1242-1590 |
5.41e-04 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 45.18 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1242 TALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKK 1321
Cdd:COG2203 342 IAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1322 HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR------DKRQEV 1395
Cdd:COG2203 422 LLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLllllllALLALS 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1396 EREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERK 1475
Cdd:COG2203 502 ALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELAL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1476 LQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDD 1555
Cdd:COG2203 582 ALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLA 661
|
330 340 350
....*....|....*....|....*....|....*
gi 1958798729 1556 LRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1590
Cdd:COG2203 662 TELDLILDSSLLLGLLLLGALLLLGGGLALLLSIG 696
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1182-1564 |
5.71e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1182 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTAlQRLREEAETLQKAERAS 1261
Cdd:COG3064 8 KAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAA-ELAAEAAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1262 LEQKSRRALEQLREQLEAEERS----------AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCS 1331
Cdd:COG3064 87 AEAEKKAAAEKAKAAKEAEAAAaaekaaaaaeKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1332 SLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--------EHERKM 1403
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAalaaveatEEAALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1404 DKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAEl 1483
Cdd:COG3064 247 GAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1484 SSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVEL 1563
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
.
gi 1958798729 1564 E 1564
Cdd:COG3064 406 D 406
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1216-1361 |
5.93e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.64 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFENQIRAEqqtaLQRLREEAETLQKAERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAe 1295
Cdd:pfam01442 44 KDLEEVRAKLEPYLEELQAKLGQN----VEELRQRLEPYTEELRKRLNAD----AEELQEKLAPYGEELRERLEQNVDA- 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798729 1296 keatllqLREQLEGERREAVAGLEKKhsteLEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 1361
Cdd:pfam01442 115 -------LRARLAPYAEELRQKLAER----LEELKESLAPYAEEVQAQLSQRLQELREKLEPQAED 169
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1235-1348 |
6.10e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.08 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1235 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLegeRREA 1314
Cdd:COG0711 52 AALAEYEEKLAEARAEAAEI----IAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV---ADLA 124
|
90 100 110
....*....|....*....|....*....|....
gi 1958798729 1315 VAGLEKKHSTELEqlcsslEAKHREVISNLQKKI 1348
Cdd:COG0711 125 VAIAEKILGKELD------AAAQAALVDRFIAEL 152
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1412-1557 |
6.38e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1412 QEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER---KLQDLEAELSSRTK 1488
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1489 DVKARLAQLNVQEENMRKEkqllldAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLR 1557
Cdd:PRK12705 113 ALSARELELEELEKQLDNE------LYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1172-1590 |
6.57e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1172 EekeeehwlyqQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSsteafENQIRAEQQTAlqRLREEA 1251
Cdd:pfam15921 395 L----------EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS-----ECQGQMERQMA--AIQGKN 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1252 ETLQK-----AERASLEQKSRRALEQL---REQLEAEER-------SAQAALRAEKEAEKEATLLQLREQLEGERREAVA 1316
Cdd:pfam15921 458 ESLEKvssltAQLESTKEMLRKVVEELtakKMTLESSERtvsdltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1317 GlEKKHSTELEQLCSSLE---AKHREVISNLQKKIE-------------GAQQKEEAQLqeslgraEQRTHQKVHQVIEY 1380
Cdd:pfam15921 538 N-EGDHLRNVQTECEALKlqmAEKDKVIEILRQQIEnmtqlvgqhgrtaGAMQVEKAQL-------EKEINDRRLELQEF 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1381 EqelssLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEER-KQRADllgHLTGELERLRraheRELESVRQEQD 1459
Cdd:pfam15921 610 K-----ILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDiKQERD---QLLNEVKTSR----NELNSLSEDYE 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1460 QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATR---RHLEE-- 1534
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQskiQFLEEam 757
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1535 --AKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1590
Cdd:pfam15921 758 tnANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1235-1306 |
6.75e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.53 E-value: 6.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1235 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQ 1306
Cdd:pfam00430 51 AALAEAEQQLKEARAEAQEI----IENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQ 118
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1488-1588 |
7.57e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1488 KDVKARLAQLNVQEENMRKEKQLLlDAQRQAALEKEEATATRRH--LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELES 1565
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEA-SFERLAELRDELAELEEELeaLKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|...
gi 1958798729 1566 QVDQLQtqsQRLQKHVSSLEAEV 1588
Cdd:COG0542 493 ELAELE---EELAELAPLLREEV 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1140-1602 |
7.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1140 EEEEEEEKEEEGEEEEKEEKEEEEEEEEEEEkeekeeehwLYQQKEKSLSLLKtqlQKAAEEEEKEEETQIREEESQRLA 1219
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEE---------VRDLRERLEELEE---ERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1220 CLRA----------QVQSSTEAFENQIRAEQQTAL------QRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAEE 1281
Cdd:PRK02224 318 ELEDrdeelrdrleECRVAAQAHNEEAESLREDADdleeraEELREEAAELESELEEAREAveDRREEIEELEEEIEELR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1282 --------------------RSAQAALRaEKEAEKEATLLQLREQLE---------------------------GERREA 1314
Cdd:PRK02224 398 erfgdapvdlgnaedfleelREERDELR-EREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1315 VAGLEkkhsTELEQLcssleakhREVISNLQKKIEGAQQKEEAQ-----LQESLGRAEQRTHQKvHQVIEYEQELSSLLR 1389
Cdd:PRK02224 477 VEELE----AELEDL--------EEEVEEVEERLERAEDLVEAEdrierLEERREDLEELIAER-RETIEEKRERAEELR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1390 DKRQEVEREHERKMDKMKEEHwqEMAEARERYEAEERKQRADllghLTGELERLRRAheRELESVRQEQDQQLEDLRRRH 1469
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAE--EEAEEAREEVAELNSKLAE----LKERIESLERI--RTLLAAIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1470 RD-QERKLQDLE--AELSSRTKDVKARLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESk 1546
Cdd:PRK02224 616 EAlAELNDERRErlAEKRERKRELEAEFDEARIEE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE- 692
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798729 1547 qqlrraIDDLRVRRVELESQVDQLQT---QSQRLQKHVSSLEAEVqRKQNI--LKEMAAET 1602
Cdd:PRK02224 693 ------LEELRERREALENRVEALEAlydEAEELESMYGDLRAEL-RQRNVetLERMLNET 746
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1238-1364 |
7.92e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.13 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1238 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAG 1317
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEEL-AREALAEKKSLEKQAEALETQLAQQRSAVE-QLRKQLAA 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798729 1318 LEKKhsteLEQlcssLEAKHREVISNLQkkiegaQQKEEAQLQESLG 1364
Cdd:pfam04012 123 LETK----IQQ----LKAKKNLLKARLK------AAKAQEAVQTSLG 155
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1461-1606 |
8.08e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1461 QLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAqrqaaleKEEATATRRHLEEAKK 1537
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQEnkrLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-------KARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1538 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQ-LQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPP 1606
Cdd:pfam13851 107 EHEVLEQRFEKVERERDELYDKFEAAIQDVQQkTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLDP 176
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
1299-1404 |
8.38e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 41.81 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1299 TLLQLREQLEGERREAVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGA-------------QQKEEA--QLQESL 1363
Cdd:COG2882 9 TLLDLAEKEEDEAARELGQAQQALEQAEEQL-EQLEQYREEYEQRLQQKLQQGlsaaqlrnyqqfiARLDEAieQQQQQV 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798729 1364 GRAEQRTHQKVHQVIEYEQELSSL--LRDKRQEVEREHERKMD 1404
Cdd:COG2882 88 AQAEQQVEQARQAWLEARQERKALekLKERRREEERQEENRRE 130
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1224-1361 |
8.56e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1224 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQL 1303
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ--LEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1304 REQLEGERREAVAGL----EKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 1361
Cdd:PRK09510 148 KAEAEAKRAAAAAKKaaaeAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1238-1586 |
8.71e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1238 AEQQTALQRLREEAETLQKAERAslEQKSRRALEQLREQLEAEERSAQAALR---------AEKEAEKEATLLQLREqle 1308
Cdd:pfam07888 83 AELKEELRQSREKHEELEEKYKE--LSASSEELSEEKDALLAQRAAHEARIReleediktlTQRVLERETELERMKE--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1309 geRREAVAGLEKKHSTELEQLCSSLEAKHREV--ISNLQKKIEGAQQKEEAQLQEsLGRAEQRTHQKVHQVIEYEQELSS 1386
Cdd:pfam07888 158 --RAKKAGAQRKEEEAERKQLQAKLQQTEEELrsLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1387 LLRDKRQEVEREHerkmdkmkeehwqemaeareryeaeERKQRADLLGHLTGELERLRRAHERELESVRQEQDQ---QLE 1463
Cdd:pfam07888 235 LLEELRSLQERLN-------------------------ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlQLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1464 DLRRRHR-DQERKLQDLEAELSSRTKDvKARLAQLNvqEENMRKEKQLLLDAQRQAALEKE---EATATRRHLEEAKKEH 1539
Cdd:pfam07888 290 DASLALReGRARWAQERETLQQSAEAD-KDRIEKLS--AELQRLEERLQEERMEREKLEVElgrEKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958798729 1540 THLLESkqqlrraiddLRVRRVELEsqvdQLQTQSQRLQKHVSSLEA 1586
Cdd:pfam07888 367 QELKAS----------LRVAQKEKE----QLQAEKQELLEYIRQLEQ 399
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1439-1543 |
9.22e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.39 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELESVRQEQDQQLEDLRRRHR-DQERKLQDLEAELSSRTKDVKA---RLAQLNVQEE-NMRKEKQLLLD 1513
Cdd:pfam12474 26 ELEQLERQQKQQIEKLEQRQTQELRRLPKRIRaEQKKRLKMFRESLKQEKKELKQeveKLPKFQRKEAkRQRKEELELEQ 105
|
90 100 110
....*....|....*....|....*....|
gi 1958798729 1514 AQRQAALEKEEATATRRHLEEAKKEHTHLL 1543
Cdd:pfam12474 106 KHEELEFLQAQSEALERELQQLQNEKRKEL 135
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1295-1599 |
9.69e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1295 EKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEaqlqeslgraeqrthqKV 1374
Cdd:COG1340 8 SSLEELEEKIEELREEIEEL-----KEKRDELNEELKELAEKRDELNAQVKELREEAQELRE----------------KR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1375 HQVIEYEQELssllRDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERElesv 1454
Cdd:COG1340 67 DELNEKVKEL----KEERDELNEKLNELREELDE-----------------LRKELAELNKAGGSIDKLRKEIERL---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1455 rqEQDQQLEDLRRrhrDQERKLQDLEAELSSRTKDVKarlaQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRrhlEE 1534
Cdd:COG1340 122 --EWRQQTEVLSP---EEEKELVEKIKELEKELEKAK----KALEKNEKLKELRAELKELRKEAEEIHKKIKELA---EE 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798729 1535 AKKEHTHLLESKQQ---LRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMA 1599
Cdd:COG1340 190 AQELHEEMIELYKEadeLRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1427-1598 |
9.77e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1427 KQRADLLGHLtgelerlrraherelesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTkdvkARLAQLNVQeenmRK 1506
Cdd:PRK11637 68 QQRASLLAQL-------------------KKQEEAISQASRKLRETQNTLNQLNKQIDELN----ASIAKLEQQ----QA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLDAQRQAALEKEEATATRRHL--EEAKKEH------THLLESKQQlrrAIDDLRVRRVELESQVDQL---QTQSQ 1575
Cdd:PRK11637 121 AQERLLAAQLDAAFRQGEHTGLQLILsgEESQRGErilayfGYLNQARQE---TIAELKQTREELAAQKAELeekQSQQK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958798729 1576 RL------------------QKHVSSLEAEVQRKQNILKEM 1598
Cdd:PRK11637 198 TLlyeqqaqqqkleqarnerKKTLTGLESSLQKDQQQLSEL 238
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1216-1299 |
9.81e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1295
Cdd:COG0711 59 EKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV-----ADLAVAIAEKILG 133
|
....
gi 1958798729 1296 KEAT 1299
Cdd:COG0711 134 KELD 137
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1233-1401 |
9.89e-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: 44.56 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1233 ENQIRAEQQTALQRLRE--EAETLQK--AERASLEQKSRRALEQLREQLEA--EERSAQAALRAEKEAEKEATLLQLREQ 1306
Cdd:COG3096 514 LQQLRAQLAELEQRLRQqqNAERLLEefCQRIGQQLDAAEELEELLAELEAqlEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1307 LEGERREAVAGLekKHSTELEQLCssleakhrevisnlqkkiegaqqkeeAQLQESLGRAEQRTHQkVHQVIEYEQELS- 1385
Cdd:COG3096 594 IKELAARAPAWL--AAQDALERLR--------------------------EQSGEALADSQEVTAA-MQQLLEREREATv 644
|
170
....*....|....*...
gi 1958798729 1386 --SLLRDKRQEVEREHER 1401
Cdd:COG3096 645 erDELAARKQALESQIER 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1215-1522 |
1.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1215 SQRLACLRAQV---QSSTEAFENQIRAEQQTAL-----QRLREEAETLQKAERA-----SLEQKSRRALEQLREQLEAEE 1281
Cdd:PRK04863 799 AERYATLSFDVqklQRLHQAFSRFIGSHLAVAFeadpeAELRQLNRRRVELERAladheSQEQQQRSQLEQAKEGLSALN 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1282 RSA-QAALRAEKEAEKEATllQLREQLEgERREAVAGLEK--KHSTELEQLCSSLEAKHREvISNLQKKIEGAQQKEEAQ 1358
Cdd:PRK04863 879 RLLpRLNLLADETLADRVE--EIREQLD-EAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDA 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1359 ------LQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE---EHWQEMAEARERYEAEERKQr 1429
Cdd:PRK04863 955 kqqafaLTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQaqaQLAQYNQVLASLKSSYDAKR- 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1430 aDLLGHLTGELERLR-RAHERELESVRQEQDQQLEDLR--RRHRDQ-ERKLQDLEAELSSRTKDVKA---RLAQLNVQEE 1502
Cdd:PRK04863 1034 -QMLQELKQELQDLGvPADSGAEERARARRDELHARLSanRSRRNQlEKQLTFCEAEMDNLTKKLRKlerDYHEMREQVV 1112
|
330 340
....*....|....*....|
gi 1958798729 1503 NMRKEKQLLLDAQRQAALEK 1522
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDNGVER 1132
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1244-1397 |
1.32e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1244 LQRLREEAE-TLQKAER--ASLEQKSRRALEQLREQLEAEERSAQ--AALRAEKEAEKeatllqLREQLEGERreavagl 1318
Cdd:PRK00106 26 MKSAKEAAElTLLNAEQeaVNLRGKAERDAEHIKKTAKRESKALKkeLLLEAKEEARK------YREEIEQEF------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1319 eKKHSTELEQLcsslEAKHREVISNLQKKIEGAQQKEEAqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER 1397
Cdd:PRK00106 93 -KSERQELKQI----ESRLTERATSLDRKDENLSSKEKT-----LESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1444-1592 |
1.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1444 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlAQLNVQEENMRKEKQLLLDAQRQaalEKE 1523
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAE-AAYEIAEANAEREVQRQLEIAER---ERE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1524 EAtatrrhLEEAKKEhthllESKQQLRRAIddlrVRRVELESQVDQLQTQsqrlqkhvssLEAEVQRKQ 1592
Cdd:COG2268 292 IE------LQEKEAE-----REEAELEADV----RKPAEAEKQAAEAEAE----------AEAEAIRAK 335
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1465-1748 |
1.58e-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: 43.51 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1465 LRRRHRDQERKLQDLEAELSsRTKDVKARLaqlnvqeenmrkEKQL-LLDAQRQAALEKEEATATRRHLEEA--KKEHTH 1541
Cdd:TIGR02168 170 YKERRKETERKLERTRENLD-RLEDILNEL------------ERQLkSLERQAEKAERYKELKAELRELELAllVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1542 LLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLrksl 1621
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE------------ISRL---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1622 gtnENQevssslslskegidlsmdsVRHFlsaegvavRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLp 1701
Cdd:TIGR02168 301 ---EQQ-------------------KQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL- 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958798729 1702 gTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL 1748
Cdd:TIGR02168 350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1221-1361 |
1.60e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaleqLREQLEAEERSAQAALRAEKEAEKEATL 1300
Cdd:PRK00106 58 IKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESR----LTERATSLDRKDENLSSKEKTLESKEQS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798729 1301 LQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVI-----SNLQKKIEGAQQKEEAQLQE 1361
Cdd:PRK00106 134 LTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIIlaeteNKLTHEIATRIREAEREVKD 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1335-1511 |
1.73e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1335 AKHREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELssllRDKRQEVEREHERKMD--KMKEehwq 1412
Cdd:COG1579 20 DRLEHRLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvrNNKE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1413 emaeareryeaeerkqradlLGHLTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1492
Cdd:COG1579 91 --------------------YEALQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170
....*....|....*....
gi 1958798729 1493 RLAQLNVQEENMRKEKQLL 1511
Cdd:COG1579 150 ELAELEAELEELEAEREEL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1144-1598 |
1.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1144 EEEKEEEGEEEEKEEKEEEEEEEEEEEKEekeeehwlYQQKEKSLSLLKTQLqkaaeeeekeeetqireeeSQRLACLRA 1223
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEE--------YLDELREIEKRLSRL-------------------EEEINGIEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1224 QVQ--SSTEAFENQIR---AEQQTALQRLREEAETLQKAeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE- 1297
Cdd:PRK03918 329 RIKelEEKEERLEELKkklKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEi 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1298 ATLLQLREQLE---GERREAVAGLEKKHST------EL-EQLCSSLEAKHREVISNLQKKIEGAQQKEEaQLQESLGRAE 1367
Cdd:PRK03918 408 SKITARIGELKkeiKELKKAIEELKKAKGKcpvcgrELtEEHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1368 Q---------RTHQKVHQVIEYEQELSSLLRDKRQEVEREHErkmdKMKEEhwqemaeareryeaeerkqradlLGHLTG 1438
Cdd:PRK03918 487 KvlkkeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEYE----KLKEK-----------------------LIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLrrahERELESVrQEQDQQLEDLRRRHRDQERKLQDLEAELSSR----TKDVKARLAQLN------VQEENMRKEK 1508
Cdd:PRK03918 540 EIKSL----KKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneyLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1509 QLLLDAQrqaALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDD-----LRVRRVELESQVDQLQTQSQRLQKHVSS 1583
Cdd:PRK03918 615 EREEKEL---KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREE 691
|
490
....*....|....*
gi 1958798729 1584 LEAEVQRKQNILKEM 1598
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1224-1578 |
1.75e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1224 QVQSSTEAFENQIRAEQQTALQ-------RLREE--AETLQKAERASLEQKSRRAL------------EQLREQLE---- 1278
Cdd:NF041483 87 QLRADAERELRDARAQTQRILQehaehqaRLQAElhTEAVQRRQQLDQELAERRQTveshvnenvawaEQLRARTEsqar 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1279 -------AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLeKKHSTELEQLCSSLEAKHREVISNL-QKKIEG 1350
Cdd:NF041483 167 rlldesrAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAIL-RRARKDAERLLNAASTQAQEATDHAeQLRSST 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1351 AQQKEEAQLQES-LGR-AEQRThqkvhqvieyeQELSSLLRDKRQEVerehERKMDKMKEEHWQEMAEARERYEAEERKQ 1428
Cdd:NF041483 246 AAESDQARRQAAeLSRaAEQRM-----------QEAEEALREARAEA----EKVVAEAKEAAAKQLASAESANEQRTRTA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1429 RAdllghltgELERLRRAHERELESVRQEQDQQLEDLRrrhrdQERKLQDLEAELSSRTKDVKARLAQL----NVQEENM 1504
Cdd:NF041483 311 KE--------EIARLVGEATKEAEALKAEAEQALADAR-----AEAEKLVAEAAEKARTVAAEDTAAQLakaaRTAEEVL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798729 1505 RKEKQlllDAQRQAALEKEEATATRRHLE-EAKKEHTHLLESKQQLRRAIDD----LRVRRVELESQVDQLQTQSQRLQ 1578
Cdd:NF041483 378 TKASE---DAKATTRAAAEEAERIRREAEaEADRLRGEAADQAEQLKGAAKDdtkeYRAKTVELQEEARRLRGEAEQLR 453
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1367-1548 |
1.85e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1367 EQRTHQKVHQVIEYEQELSSLLRDKRQEVEREherkmDKMKEEhwQEMAEARERYEAEERKQRAdllghltgELERLRRA 1446
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERA-----EKMREE--LELEQQRRFEEIRLRKQRL--------EEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1447 HE-----RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSS----RTKDVKARLAQLNVQEENMRKEKQLLLDAQRQ 1517
Cdd:pfam15709 405 EEerkqrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|.
gi 1958798729 1518 AALEKEEATATRRHLEEAKKEHTHLLESKQQ 1548
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1223-1590 |
1.92e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 43.26 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1223 AQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQ 1302
Cdd:COG2203 338 DQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1303 LREQLEGERREAVAGLEKK-----HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQV 1377
Cdd:COG2203 418 LEGLLLLDLLLLLLLLRRIlllrvLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLAL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1378 IEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQE 1457
Cdd:COG2203 498 LALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLI 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1458 QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKK 1537
Cdd:COG2203 578 ELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLR 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958798729 1538 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1590
Cdd:COG2203 658 ALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVL 710
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1234-1306 |
2.21e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798729 1234 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRaekeAEKEATLLQLREQ 1306
Cdd:cd06503 50 EELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE----QEKEKALAELRKE 118
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1432-1638 |
2.33e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1432 LLGHLTGELErlrrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLL 1511
Cdd:PHA02562 189 KIDHIQQQIK----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1512 LDAQRQAALEKEEATATRRH---------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQ---- 1578
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLelkn 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798729 1579 ------KHVSSLEAEVQRKQNILKEMAAETnaPPHPEPglhIEDLRKSLgtnenQEVSSSLS-LSKE 1638
Cdd:PHA02562 345 kistnkQSLITLVDKAKKVKAAIEELQAEF--VDNAEE---LAKLQDEL-----DKIVKTKSeLVKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1562-1751 |
2.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1562 ELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAEtnapphpepglhIEDLRKSLGTNEN--QEVSSSLSLSKEG 1639
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE------------LEDLEKEIKRLELeiEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1640 IDlsmdsvrhflsaegvAVRSAKEF--LVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEET 1717
Cdd:COG1579 82 LG---------------NVRNNKEYeaLQKEIESLKRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798729 1718 KHLDEMKSAMRKGHDLLKKKEEKL-NQLESSLLEE 1751
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELaAKIPPELLAL 179
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1460-1601 |
2.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1460 QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLldaqrqaaleKEEATATRRHLEEAKKEH 1539
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSEL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798729 1540 THLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1601
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
1267-1590 |
2.51e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 42.87 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1267 RRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQK 1346
Cdd:COG2203 330 LELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1347 KIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEER 1426
Cdd:COG2203 410 ADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLL 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1427 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1506
Cdd:COG2203 490 LLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLL 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1507 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1586
Cdd:COG2203 570 LGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALA 649
|
....
gi 1958798729 1587 EVQR 1590
Cdd:COG2203 650 LASL 653
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1223-1340 |
3.39e-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: 42.47 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1223 AQVQSSTEAFENQIRaEQQTALQRLREEAETLQKAERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAEKEatLLQ 1302
Cdd:pfam01576 934 QKSESARQQLERQNK-ELKAKLQEMEGTVKSKFKSSIAALEAK----IAQLEEQLEQESRERQAANKLVRRTEKK--LKE 1006
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958798729 1303 LREQLEGERREAVAGLEK--KHSTELEQLCSSLEAKHREV 1340
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQaeKGNSRMKQLKRQLEEAEEEA 1046
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1538 |
3.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1335 AKHREVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD--KRQEVEREHERKMDKMKEEHWQ 1412
Cdd:COG3883 19 QAKQKELSELQAELEAAQ-AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1413 EMAEARERYEAEERKQRADLLGHLTGeLERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 1492
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958798729 1493 RLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKE 1538
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1242-1342 |
3.69e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1242 TALQRLREEAETLqKAERASLEQKSRRALEQLREQLEAEERSAQ---AALRAEKEAEKEAT--LLQLREQLEgERREAVA 1316
Cdd:COG0542 411 EELDELERRLEQL-EIEKEALKKEQDEASFERLAELRDELAELEeelEALKARWEAEKELIeeIQELKEELE-QRYGKIP 488
|
90 100
....*....|....*....|....*.
gi 1958798729 1317 GLEKKHsTELEQLCSSLEAKHREVIS 1342
Cdd:COG0542 489 ELEKEL-AELEEELAELAPLLREEVT 513
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1439-1534 |
3.72e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1439 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQA 1518
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*.
gi 1958798729 1519 ALEKEEATATRRHLEE 1534
Cdd:COG0542 495 AELEEELAELAPLLRE 510
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1454-1568 |
4.87e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1454 VRQEQDQQLEDLRrrhrDQERKLQDLEAELSSRTKD----VKARLAQLNVQEENMRKEKQLLLDAQRQaalEKEEATATR 1529
Cdd:COG0542 402 VRMEIDSKPEELD----ELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARWEA---EKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958798729 1530 RHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1568
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1230-1349 |
5.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1230 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAeersaqaaLRAEKE------AEKEATLLQL 1303
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEE-IRRLEEQVER--------LEAEVEeleaelEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958798729 1304 REQLEGERREAVAGLEK-----KHSTELEQLCSSLEAKhREVISNLQKKIE 1349
Cdd:COG2433 447 ERELSEARSEERREIRKdreisRLDREIERLERELEEE-RERIEELKRKLE 496
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1223-1604 |
5.06e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1223 AQVQSSTEAF------ENQIRAEQQTALQRL----REEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAA-LRA- 1290
Cdd:PRK10246 216 EQVQSLTASLqvltdeEKQLLTAQQQQQQSLnwltRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARqLRPh 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1291 -EKEAEKEATLLQLREQLEgerrEAVAGLEKKHSteleqlcssleakhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ- 1368
Cdd:PRK10246 296 wERIQEQSAALAHTRQQIE----EVNTRLQSTMA--------------------LRARIRHHAAKQSAELQAQQQSLNTw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1369 -RTHQKVHQvieYEQELSSLlrdkrqeveREH--ERKMDKMKEEHWQEmaeareryEAEERKQRADLLGHLTGELERLRR 1445
Cdd:PRK10246 352 lAEHDRFRQ---WNNELAGW---------RAQfsQQTSDREQLRQWQQ--------QLTHAEQKLNALPAITLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1446 AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQrqAALEKEEA 1525
Cdd:PRK10246 412 AAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK--TICEQEAR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1526 TAT----RRHLEEAK-------KEHThLLESKQQLRraIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1594
Cdd:PRK10246 490 IKDleaqRAQLQAGQpcplcgsTSHP-AVEAYQALE--PGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESE 566
|
410
....*....|
gi 1958798729 1595 LKEMAAETNA 1604
Cdd:PRK10246 567 AQSLRQEEQA 576
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1457-1601 |
5.12e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1457 EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQlNVQEENMRKEKQLLLDAQRQAalekeEATATRRHLEEAK 1536
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-EQLERAEKMREELELEQQRRF-----EEIRLRKQRLEEE 399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798729 1537 KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1601
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1216-1295 |
5.15e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 1295
Cdd:pfam00430 58 QQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQV-----VALAVQIAEKLLE 132
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1455-1601 |
5.40e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1455 RQEQDQQLEDLRRRHRDQERKLQDLEAEL----SSRTKDVKARLAQLNVQEENMRKEKQL--LLDAQRQAALEKEEATAT 1528
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQAQAELealkDDNDEETRETLSTLSLRQLESRLAQTLdqLQNAQNDLAEYNSQLVSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1529 RRHLEEAKKEHTHLLESKQQLRRAIDDLRV--------------------------RRVELE----------SQVDQLQT 1572
Cdd:PRK11281 155 QTQPERAQAALYANSQRLQQIRNLLKGGKVggkalrpsqrvllqaeqallnaqndlQRKSLEgntqlqdllqKQRDYLTA 234
|
170 180
....*....|....*....|....*....
gi 1958798729 1573 QSQRLQKHVSSLEAEVQRKQNILKEMAAE 1601
Cdd:PRK11281 235 RIQRLEHQLQLLQEAINSKRLTLSEKTVQ 263
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1295-1602 |
5.87e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.82 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1295 EKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLEA--KHRE--VISNLQKKIEGAQQKEeAQLQESLGRAEQRT 1370
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKErlKHKEslVAASTSSRVGGLCLKC-AQHEAVLAQTHTNV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1371 H-QKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKE-EHWQEMAEARERYEAEERKQradlLGHLTGELERLRRAHE 1448
Cdd:pfam15964 298 HmQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQvKQAVQMTEEANFEKTKALIQ----CEQLKSELERQKERLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1449 RELES-----------VRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKD-------VKARLAQLNVQEENMRKEKQL 1510
Cdd:pfam15964 374 KELASqqekraqekeaLRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREknslvsqLEEAQKQLASQEMDVTKVCGE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1511 LLDAQRQAALEKEEA--------TATRRHLE----EAKKEHTHLLESKQQLRRAIDDLRVRRVELeSQVDQLQTQSQRlQ 1578
Cdd:pfam15964 454 MRYQLNQTKMKKDEAekehreyrTKTGRQLEikdqEIEKLGLELSESKQRLEQAQQDAARAREEC-LKLTELLGESEH-Q 531
|
330 340
....*....|....*....|....
gi 1958798729 1579 KHVSSLEAEvQRKQNILKEMAAET 1602
Cdd:pfam15964 532 LHLTRLEKE-SIQQSFSNEAKAQA 554
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1138-1517 |
5.93e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1138 EKEEEEEEEKEEEGEEEEKeekeeeeeeeeeeekeekeeehwLYQQKEKSLSL--LKTQLQKAAEEEEKEEETQIREEES 1215
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLER-----------------------LRREREKAERYqaLLKEKREYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1216 Q---RLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREqLEAEERSAQaalRAEK 1292
Cdd:TIGR02169 241 AierQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKI----KDLGEEEQLRVKEKIGE-LEAEIASLE---RSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1293 EAEKEAtllqlrEQLEGERREAVAGLEKKHStELEQLCSSLEAKHREVISnLQKKIEGAQQKEEAQLQEsLGRAEQRTHQ 1372
Cdd:TIGR02169 312 EKEREL------EDAEERLAKLEAEIDKLLA-EIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAE-LEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1373 KVHQVIEYEQELSSLLRdKRQEVEREHERKMDKMKEEHwQEMAEARERYEAEERKQRAdllghLTGELERLR---RAHER 1449
Cdd:TIGR02169 383 TRDELKDYREKLEKLKR-EINELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINE-----LEEEKEDKAleiKKQEW 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1450 ELESVRqeqdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNV--QEENMRKEKQLLLDAQRQ 1517
Cdd:TIGR02169 456 KLEQLA----ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAseERVRGGRAVEEVLKASIQ 521
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1233-1349 |
6.04e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1233 ENQIRAEQQTA-LQRLREEAETLQKaeraSLEQKsrraLEQLREQLEAE----ERSAQAALRAEKEaEKEATLLQLREQL 1307
Cdd:PRK00409 527 ELERELEQKAEeAEALLKEAEKLKE----ELEEK----KEKLQEEEDKLleeaEKEAQQAIKEAKK-EADEIIKELRQLQ 597
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958798729 1308 EGERREAVAglekkhsTELEQLCSSLEAKHREVISNLQKKIE 1349
Cdd:PRK00409 598 KGGYASVKA-------HELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1215-1321 |
6.51e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.03 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1215 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQkaeraSLEQKSRRALEQLREQLEAEERSAqAALRAEKEA 1294
Cdd:pfam15665 95 RQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALE-----ELRAKHRQEIQELLTTQRAQSASS-LAEQEKLEE 168
|
90 100 110
....*....|....*....|....*....|
gi 1958798729 1295 EKEATLLQLREQLE---GERREAVAGLEKK 1321
Cdd:pfam15665 169 LHKAELESLRKEVEdlrKEKKKLAEEYEQK 198
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1252-1598 |
6.89e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1252 ETLQKAERasLEQK----SRRALEQLREQL-EAEERSAQAALRAEKEAEKEAT-LLQLREQLEGERREAVAGL---EKKH 1322
Cdd:PRK04778 61 QSEEKFEE--WRQKwdeiVTNSLPDIEEQLfEAEELNDKFRFRKAKHEINEIEsLLDLIEEDIEQILEELQELlesEEKN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1323 STELEQLcsslEAKHREV--------------ISNLQKKIEGAQQK-------------EEA-----QLQESLGRAEQrt 1370
Cdd:PRK04778 139 REEVEQL----KDLYRELrksllanrfsfgpaLDELEKQLENLEEEfsqfveltesgdyVEAreildQLEEELAALEQ-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1371 hqKVHQVIEYEQELSSLLRDKRQEVEREHerkmDKMKEEHWqemaeareryeaeerkqradLLGHLtgelerlrrAHERE 1450
Cdd:PRK04778 213 --IMEEIPELLKELQTELPDQLQELKAGY----RELVEEGY--------------------HLDHL---------DIEKE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1451 LESVRQEQDQQLEDLRRRHRDQ-ERKLQDLEAEL----SSRTKDVKARlaqlNVQEENMRKEKQLLLDAQRQAALEKEEA 1525
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEaEEKNEEIQERIdqlyDILEREVKAR----KYVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1526 TATRR--HLEEAKKEHTHLLESK-QQLRRAIDD--------------LRVRRVELESQVDQLQTQSQRLQKHVSSLEAEV 1588
Cdd:PRK04778 334 DRVKQsyTLNESELESVRQLEKQlESLEKQYDEiteriaeqeiayseLQEELEEILKQLEEIEKEQEKLSEMLQGLRKDE 413
|
410
....*....|
gi 1958798729 1589 QRKQNILKEM 1598
Cdd:PRK04778 414 LEAREKLERY 423
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1473-1601 |
7.41e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1473 ERKLQDLEAelssrtkdvkaRLAQLnvqEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRA 1552
Cdd:pfam20492 5 EREKQELEE-----------RLKQY---EEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958798729 1553 IDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1601
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1233-1314 |
7.46e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1233 ENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSA--QAALRAEKEAEKEATLLQLREQLEGE 1310
Cdd:pfam05672 30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAeeEAEEREQREQEEQERLQKQKEEAEAK 109
|
....
gi 1958798729 1311 RREA 1314
Cdd:pfam05672 110 AREE 113
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1427-1509 |
7.70e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1427 KQRADLLG-HLT-GELE-RLRRAHE--RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK---DVK----ARL 1494
Cdd:pfam08614 61 QLREELAElYRSrGELAqRLVDLNEelQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKlnqDLQdelvALQ 140
|
90
....*....|....*
gi 1958798729 1495 AQLNVQEENMRKEKQ 1509
Cdd:pfam08614 141 LQLNMAEEKLRKLEK 155
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1241-1598 |
7.77e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1241 QTALQRLREE---AETLQKAERASLEQKSRRALE-QLR-EQLEAEERSAQA------ALR--AEKEAEKEATLLQLREQL 1307
Cdd:pfam05622 65 QKQLEQLQEEnfrLETARDDYRIKCEELEKEVLElQHRnEELTSLAEEAQAlkdemdILResSDKVKKLEATVETYKKKL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1308 E--GERREAVAGLEKKHSTELEQLCSSLEAKHREviSNLQKKIEGAQQkeeaQLQESLGRAEQRTHQKVHQVIEY---EQ 1382
Cdd:pfam05622 145 EdlGDLRRQVKLLEERNAEYMQRTLQLEEELKKA--NALRGQLETYKR----QVQELHGKLSEESKKADKLEFEYkklEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1383 ELSSLLRDK-RQEVEREHERKMDKmkEEHWQEMAEARERYEAEERKQRADLLGHLTGEL------ERLRR-AHERELESV 1454
Cdd:pfam05622 219 KLEALQKEKeRLIIERDTLRETNE--ELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpaeirEKLIRlQHENKMLRL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1455 RQEQ--DQQLEDLRRRHRDQERKLQDLEAELssrtkdvkaRLAQLNVQEenMRKEKQLLLDAQRQAALEKEEATATRRHL 1532
Cdd:pfam05622 297 GQEGsyRERLTELQQLLEDANRRKNELETQN---------RLANQRILE--LQQQVEELQKALQEQGSKAEDSSLLKQKL 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798729 1533 EEAKKEHTHLLESKQQLRRAIDDLRvrrvelesqvdqlQTQSQRLQKHVSSLEAEVQRKQNILKEM 1598
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELE-------------PKQDSNLAQKIDELQEALRKKDEDMKAM 418
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1233-1321 |
7.90e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.83 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1233 ENQIRAEQQTALQRLrEEAETLQKAERASLEQkSRRALEQLREQLEAE-ERSAQAALrAEKEAEKEATLLQLREQLEGER 1311
Cdd:PRK07353 38 EDYIRTNRAEAKERL-AEAEKLEAQYEQQLAS-ARKQAQAVIAEAEAEaDKLAAEAL-AEAQAEAQASKEKARREIEQQK 114
|
90
....*....|
gi 1958798729 1312 REAVAGLEKK 1321
Cdd:PRK07353 115 QAALAQLEQQ 124
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1230-1369 |
8.51e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1230 EAFENQIRAEQQTAlQRLREEAETLQKaerasleqKSRRALEQLREqlEAEERSAQAalRAEKEAEKEATLLQLREQLEG 1309
Cdd:COG0711 30 DERQEKIADGLAEA-ERAKEEAEAALA--------EYEEKLAEARA--EAAEIIAEA--RKEAEAIAEEAKAEAEAEAER 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1310 ERREAVAGLEKKHSTELEQLcssleakhREVISNLqkkiegAQQKEEAQLQESLGRAEQR 1369
Cdd:COG0711 97 IIAQAEAEIEQERAKALAEL--------RAEVADL------AVAIAEKILGKELDAAAQA 142
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1470-1596 |
9.14e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1470 RDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKekqllLDAQRQAALEKEEatatrrhlEEAKKEhthLLESKQQL 1549
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-----WEEKARLALEKGR--------EDLARE---ALERKAEL 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958798729 1550 RRAIDDLRVRRVELESQVDQLQTQSQRLQKHVssleAEVQRKQNILK 1596
Cdd:COG1842 97 EAQAEALEAQLAQLEEQVEKLKEALRQLESKL----EELKAKKDTLK 139
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1221-1621 |
9.37e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1221 LRAQVQSSTEAFENQirAEQQTALQRLREEAETLQKAERASLE---------QKSRRALEQLREQLEAEER-------SA 1284
Cdd:pfam07111 336 LRGQVAELQEQVTSQ--SQEQAILQRALQDKAAEVEVERMSAKglqmelsraQEARRRQQQQTASAEEQLKfvvnamsST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1285 QAALRAE--KEAEKEATLLQLREQLEGERRE--AVAGL--EKKHSTELEQLCSSLEAKHREVISNLQKKIEgaqqkeeaQ 1358
Cdd:pfam07111 414 QIWLETTmtRVEQAVARIPSLSNRLSYAVRKvhTIKGLmaRKVALAQLRQESCPPPPPAPPVDADLSLELE--------Q 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1359 LQESLGRAEQRTHQKVHQVieyEQELSsllRDKRQ-EVEReheRKMDKMKEEHWQEMaeareryeaeerKQRADLLGHLT 1437
Cdd:pfam07111 486 LREERNRLDAELQLSAHLI---QQEVG---RAREQgEAER---QQLSEVAQQLEQEL------------QRAQESLASVG 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1438 GELERLRRAHERELE---SVRQEQDQQLEDLRRRHRDqerKLQDLEAELSSRTKDVKARLaqlNVQEENMRKEKQLLLDA 1514
Cdd:pfam07111 545 QQLEVARQGQQESTEeaaSLRQELTQQQEIYGQALQE---KVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQI 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1515 QRQAALEKEEATATRRHLEEAKKEhthllESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNI 1594
Cdd:pfam07111 619 QHRATQEKERNQELRRLQDEARKE-----EGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVV 693
|
410 420
....*....|....*....|....*..
gi 1958798729 1595 LKEMAAETNAPPHPEPGLHIEDLRKSL 1621
Cdd:pfam07111 694 SSPRPECSASAPIPAAVPTRESIKGSL 720
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1244-1409 |
9.59e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1244 LQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKeAEKEATLLQlrEQLEGERREAVAGLEKKHS 1323
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-AQQKADFAQ--DNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1324 TELEQLCSSLEAKHReVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQElsslLRDKRQEVEREHE--- 1400
Cdd:pfam05262 260 LPKPADTSSPKEDKQ-VAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKE----AEDKELEAQKKREpva 334
|
....*....
gi 1958798729 1401 RKMDKMKEE 1409
Cdd:pfam05262 335 EDLQKTKPQ 343
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1223-1295 |
9.69e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 40.21 E-value: 9.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798729 1223 AQVQsstEAFENQIRAeqqtalQRLREEAETLQKAERASLEQKSRRALEqlREQLEAEERSAQAALRAEKEAE 1295
Cdd:COG0330 167 EEVQ---DAMEDRMKA------EREREAAILEAEGYREAAIIRAEGEAQ--RAIIEAEAYREAQILRAEGEAE 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1132-1597 |
9.98e-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: 40.93 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1132 EEEEEEEKEEEEEEEKEEEGEEEEKEEKEEEEEEEEEEEKEEKEEEhwLYQQKEKSLSLLKTQLQKAAE-EEEKEEETQI 1210
Cdd:pfam01576 9 AKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE--LCAEAEEMRARLAARKQELEEiLHELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1211 REEESQRLACLRAQVQSSTEAFENQIrAEQQTALQRLREEAETLQKA-----ERASLEQKSRRALEQLREQLeaEERSAQ 1285
Cdd:pfam01576 87 EEERSQQLQNEKKKMQQHIQDLEEQL-DEEEAARQKLQLEKVTTEAKikkleEDILLLEDQNSKLSKERKLL--EERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1286 AALRAEKEAEKEATLLQLREQLEGERREAVAGL--EKKHSTELEQLCSSLEAKH---REVISNLQKKIE---GAQQKEEA 1357
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLkkEEKGRQELEKAKRKLEGEStdlQEQIAELQAQIAelrAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1358 QLQESLGRAEQRTHQK---VHQVIEYEQELSSLLRDkrQEVEREHERKMDKMKEEHWQEMAE---------ARERYEAEE 1425
Cdd:pfam01576 244 ELQAALARLEEETAQKnnaLKKIRELEAQISELQED--LESERAARNKAEKQRRDLGEELEAlkteledtlDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1426 RKQRADLLGHLTGELERLRRAHERELESVRQEQDQ-------QLEDLRRRHRDQERKLQDLEAELSSRTKDVKArLAQLN 1498
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaleelteQLEQAKRNKANLEKAKQALESENAELQAELRT-LQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798729 1499 VQEENMRKEkqllLDAQRQAALEKeeatatrrhLEEAKKEHTHLLESKQQLRRAIDDlrvrrveLESQVDQLQTQSQRLQ 1578
Cdd:pfam01576 401 QDSEHKRKK----LEGQLQELQAR---------LSESERQRAELAEKLSKLQSELES-------VSSLLNEAEGKNIKLS 460
|
490
....*....|....*....
gi 1958798729 1579 KHVSSLEAEVQRKQNILKE 1597
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQE 479
|
|
| |
