|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
730-1250 |
1.22e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 730 IRAEQQTALQRLREEAETLQKAERASLEQKSRRA------LEQLREQL-----EAEERSAQAALRAEKEAEKEATLLQLR 798
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELKEELKELEAellllkLRELEAELeeleaELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 799 EQLE--GERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEgaQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 876
Cdd:COG1196 274 LELEelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 877 ELSSLLRDKRQEVEREHErkmDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELEsvRQEQDQQL 956
Cdd:COG1196 352 ELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--LEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 957 EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEH--- 1033
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegf 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1034 ------THLLESKQQLRRAIDDLRVRRVELESQ---------VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1098
Cdd:COG1196 507 legvkaALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1099 PPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVR-------QTRSMRRRQT 1171
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtlegeggSAGGSLTGGS 666
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 1172 ALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDED 1250
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
737-1091 |
5.85e-16 |
|
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: 83.95 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 737 ALQRLREEAETLQKAERA---------SLEQKSRRAlEQLREqLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERRE 807
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIlnelerqlkSLERQAEKA-ERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 808 avaglEKKHSTELEQLCSSLEAkHREVISNLQKKIEGAQQKeeaqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRD--K 885
Cdd:TIGR02168 255 -----LEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE--------LYALANEISRLEQQKQILRERLANLERQleE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 886 RQEVEREHERKMDKMKEEhwqemaeareryEAEERKQRADLLGHLTGELERLRRAHE--RELESVRQEQDQQLEDLRRRH 963
Cdd:TIGR02168 321 LEAQLEELESKLDELAEE------------LAELEEKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 964 RDQERKLQDLEAELSSrtkdVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK--EEATATRRHLEEAKKEHTHLLESKQ 1041
Cdd:TIGR02168 389 AQLELQIASLNNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1042 QLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1091
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
676-1085 |
2.03e-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: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 676 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERAS 755
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 756 LEQKS--RRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSL---EAK 830
Cdd:COG1196 456 EEEEAllELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAA 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 831 HREVI---------SNLQKKIEGAQQKEEAQLQESLGRAE---------QRTHQKVHQVIEYEQELSSLLRDKRQEVERE 892
Cdd:COG1196 536 YEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLVASDLREADARY 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 893 HERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLT-----GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQE 967
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 968 RKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESK-QQLRRA 1046
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERElERLERE 775
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958798735 1047 IDDL--------------RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1085
Cdd:COG1196 776 IEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
733-1103 |
1.14e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 733 EQQTALQRLREEAETLQkAERASLEQKsRRALEQLREQLEAEERSAQAALRAEKEAEKEAtLLQLREQLEGERREAvagl 812
Cdd:COG4913 285 FAQRRLELLEAELEELR-AELARLEAE-LERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERELEER---- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 813 eKKHSTELEQLCSSLEAK---HREVISNLQKKIEGAQQK---EEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLR--- 883
Cdd:COG4913 358 -ERRRARLEALLAALGLPlpaSAEEFAALRAEAAALLEAleeELEALEEALAEAEAALRDLRRELRELEAEIASLERrks 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 884 --DKRQ-------------------------EVEREHE----------------------------RKMDKMKEEH---W 905
Cdd:COG4913 437 niPARLlalrdalaealgldeaelpfvgeliEVRPEEErwrgaiervlggfaltllvppehyaaalRWVNRLHLRGrlvY 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 906 QEMAEARERYEAEERKQRA-----------------DLLGHL--------TGELERLRRA--------HERELesvRQEQ 952
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSlagkldfkphpfrawleAELGRRfdyvcvdsPEELRRHPRAitragqvkGNGTR---HEKD 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 953 DQQleDLRRRH---RDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEeATATRRHL 1026
Cdd:COG4913 594 DRR--RIRSRYvlgFDNRAKLAALEAElaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1027 EEAKKEHTHLLESK---QQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE 1103
Cdd:COG4913 671 AELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1259 |
2.83e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 675 YQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLR--------AQVQSSTEA--FENQIRAEQQTALQRLR-- 742
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaedarkaEEARKAEDArkAEEARKAEDAKRVEIARka 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 743 EEA---ETLQKAERASLEQKSRRALEQLR--EQLEAEE-RSAQAALRAEKEAEKEatllQLREQLEGERREAVAGLEKKH 816
Cdd:PTZ00121 1161 EDArkaEEARKAEDAKKAEAARKAEEVRKaeELRKAEDaRKAEAARKAEEERKAE----EARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 817 STEleqlcssLEAKHREVISNLQ--KKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--- 891
Cdd:PTZ00121 1237 KDA-------EEAKKAEEERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEakk 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 892 --EHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGE--LERLRRAHER-ELESVRQEQDQQLEDLRRRHRDQ 966
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 967 ERKLQDLEA---ELSSRTKDVKARLAQLNVQEENMRK-EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHThlLESKQQ 1042
Cdd:PTZ00121 1390 KKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE--AKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1043 LRRAIDDLRvRRVELESQVDQLQTQSQRLQKHVSSLE--AEVQRKQNILK--EMAAETNAPPHPEPGLHIEDLRKSLGTN 1118
Cdd:PTZ00121 1468 EAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1119 ENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTK 1198
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798735 1199 VLENVRKNLDEETKHLDEMKsamRKGHDLlkKKEEKLNQLESSLLEEVSDEDTLKGSSIKK 1259
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEK---KKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
742-1098 |
4.95e-13 |
|
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: 74.00 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 742 REEAETLQKAERASLEQKSRRALEQL--REQLEAEERSAQAALraekeaEKEATLLQLREQLEGERREavaglekkhstE 819
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEM------DRQAAIYAEQERMAMERER-----------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 820 LEQLcsSLEAKHREVISNLQKKIegAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQEVEREHERKMDK 899
Cdd:pfam17380 350 LERI--RQEERKRELERIRQEEI--AMEISRMRELERLQMERQQKNERVRQELEAARKVK-ILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 900 MKEEHwqemaeareryeaEERKQRadllghltgELERLRRAHERELESVRQEQ---DQQLEDLRRRHRDQERKLQDLEAE 976
Cdd:pfam17380 425 IRAEQ-------------EEARQR---------EVRRLEEERAREMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 977 lssrtkdvkarlaqlnvqeenmrKEKQLLLDAQRQAALEKEEATATRRHLEEAKK--------EHTHLLESKQQLRRAID 1048
Cdd:pfam17380 483 -----------------------KRDRKRAEEQRRKILEKELEERKQAMIEEERKrkllekemEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1049 DLRVRRVELESQvDQLQTQSQRLQKHVSSLEAeVQRKQNILKEMAAETNA 1098
Cdd:pfam17380 540 EERRKQQEMEER-RRIQEQMRKATEERSRLEA-MEREREMMRQIVESEKA 587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1100 |
2.10e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 861 EQRTHQKVHQVIEYEQELSSLlrdkRQEVEREhERKMDKMK--EEHWQEMAEARERYEAEerKQRADLLGHLTGELE-RL 937
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERA----HEALEDA-REQIELLEpiRELAERYAAARERLAEL--EYLRAALRLWFAQRRlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 938 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALE-K 1016
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1017 EEATATRRHLEEAKKEHTHLLES----KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqnILKEM 1092
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEAleeeLEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDAL 449
|
....*...
gi 1958798735 1093 AAETNAPP 1100
Cdd:COG4913 450 AEALGLDE 457
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
715-1078 |
5.37e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 715 LRAQVQSSTEAfenqiRAEQQTALQRLREEAETLqKAERASLEQksrrALEQLREQLEaeerSAQAALR-AEKEAEKEAT 793
Cdd:PRK04863 291 LRRELYTSRRQ-----LAAEQYRLVEMARELAEL-NEAESDLEQ----DYQAASDHLN----LVQTALRqQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 794 LLQLREQLEgERREAVAGL--------EKKHSTELEQLCSsleakhREVISNLQKKIEgAQQKEEAQLQES---LGRAEQ 862
Cdd:PRK04863 357 LEELEERLE-EQNEVVEEAdeqqeeneARAEAAEEEVDEL------KSQLADYQQALD-VQQTRAIQYQQAvqaLERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 863 RTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELER 936
Cdd:PRK04863 429 LCGLpdlTADNAEDWLEEF----QAKEQEATeelLSLEQKLSVAQAAHSQ-------------FEQAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 937 ----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQER--------------------KLQDLEAELSSRTKDVK 985
Cdd:PRK04863 492 seawdvarelLRRLREQRHLAEQLQQlRMRLSELEQRLRQQQRaerllaefckrlgknlddedELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 986 ARLAQLNVQEENMR-KEKQLLLDAQRQAALEKE--EATATRRHLEEAKKEHthlLESKQQLRRAIDDLRVRRVELESQVD 1062
Cdd:PRK04863 572 ESVSEARERRMALRqQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEE---FEDSQDVTEYMQQLLERERELTVERD 648
|
410
....*....|....*.
gi 1958798735 1063 QLQTQSQRLQKHVSSL 1078
Cdd:PRK04863 649 ELAARKQALDEEIERL 664
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
754-1096 |
3.27e-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: 68.56 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 754 ASLEQKSRRALEQLREqleAEERSAQAALraekeaeKEATLLQLREQLEGERREAV---AGLEKKHSTELEQLCSSLEAk 830
Cdd:TIGR02169 166 AEFDRKKEKALEELEE---VEENIERLDL-------IIDEKRQQLERLRREREKAEryqALLKEKREYEGYELLKEKEA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 831 HREVISNLQKKIEGaQQKEEAQLQESLGRAEQRTHqkvhqvieyeqELSSLLRDKRQEVEREHERKMDKMKEEhwqemae 910
Cdd:TIGR02169 235 LERQKEAIERQLAS-LEEELEKLTEEISELEKRLE-----------EIEQLLEELNKKIKDLGEEEQLRVKEK------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 911 areryeaeerkqradlLGHLTGELERLRRAherelesvrqeqdqqLEDLRRRHRDQERKLQDLEAELSSrtkdVKARLAQ 990
Cdd:TIGR02169 296 ----------------IGELEAEIASLERS---------------IAEKERELEDAEERLAKLEAEIDK----LLAEIEE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 991 LNVQEENMRKEKQLLLDaqRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQR 1070
Cdd:TIGR02169 341 LEREIEEERKRRDKLTE--EYAELKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340
....*....|....*....|....*.
gi 1958798735 1071 LQKHVSSLEAEVQRKQNILKEMAAET 1096
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEK 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
799-1312 |
5.27e-11 |
|
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: 67.84 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 799 EQLEGERREAVAGLEKKHSTELEQLCSsleaKHREVISNLQKKIEGAQQKE---EAQLQESLGRAEQRTHQKVHQVIEYE 875
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLIS----EHEVEITGLTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 876 QELSSLlRDKRQEVEREHERKMDKMKEEhwQEMAEARERYEAEERKQRADLLGHLTGELERL-RRAHERELE-SVRQEQD 953
Cdd:pfam15921 324 STVSQL-RSELREAKRMYEDKIEELEKQ--LVLANSELTEARTERDQFSQESGNLDDQLQKLlADLHKREKElSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 954 QQLED-----------LRRRHRDQERKLQDLEAELSSRTKDVKARLAQ--LNVQEENMRKEKQLLLDAQRQAALEK---- 1016
Cdd:pfam15921 401 KRLWDrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1017 -EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEaEVQRKQNILKEMAAE 1095
Cdd:pfam15921 481 vEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1096 TNAPphpepglhIEDLRKSLG-----TNENQEVSSSLSLSKEGIDLSMDSVRHFLSaEGVAVRSAKEFLVRQTRSM---- 1166
Cdd:pfam15921 560 KDKV--------IEILRQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRELEARvsdl 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1167 -RRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDEETKHL--------DEMKSAMRKGHDLLKKKEEKLNQ 1237
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrnksEEMETTTNKLKMQLKSAQSELEQ 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 1238 LESSLLE-EVSDEDTLKGS--SIKKVTFDLSDMDDLSSEsfescpLLHITPTPNSADPNKiHYLSSSLQRISSELNGV 1312
Cdd:pfam15921 711 TRNTLKSmEGSDGHAMKVAmgMQKQITAKRGQIDALQSK------IQFLEEAMTNANKEK-HFLKEEKNKLSQELSTV 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1196 |
7.32e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHERELesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV----------KARLAQLN-----VQEEN 997
Cdd:TIGR02168 250 EAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqilRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 998 MRKEKQLLLDAQRQAALEKEEATATRRH------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRL 1071
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1072 QKHVSSLEAEVQRKQNIlkemaaetnapphpepglhIEDLRKSLGTNENQEVSSSLSLSKEGIdlsmdsvrHFLSAEGVA 1151
Cdd:TIGR02168 406 EARLERLEDRRERLQQE-------------------IEELLKKLEEAELKELQAELEELEEEL--------EELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798735 1152 VRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPG 1196
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
660-1115 |
7.65e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 660 EEEEEkeekeeehwlYQQKEKSLSLLKTQLQkaaeeeekeeetqirEEESQRLACLRAQVQSSTEAFENQIRAEQQTALQ 739
Cdd:COG1196 348 EAEEE----------LEEAEAELAEAEEALL---------------EAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 740 RLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTE 819
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 820 LEQLcssleAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVI----EYEQELSSLLRDKRQEVEREHER 895
Cdd:COG1196 483 LEEL-----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 896 KMDKMKEEHWQEMAEARERYEAEERKQRADL-LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLE 974
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALaAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 975 AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIddlrvrr 1054
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA------- 710
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798735 1055 vELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPgLHIEDLRKSL 1115
Cdd:COG1196 711 -EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELEREL 769
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
833-1245 |
1.04e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 833 EVISNLQKKIEGAQQ--KEEAQLQESLGRAEQRTHQKVHQVieyeQELSSLLRDKRQEVE--REHERKMDKMKEEhwqem 908
Cdd:PRK03918 169 EVIKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEklEKEVKELEELKEE----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 909 aeareryEAEERKQRADLLGHLTGELERLR---------RAHERELESVRQEQDQ---------QLEDLRRRHRDQERKL 970
Cdd:PRK03918 240 -------IEELEKELESLEGSKRKLEEKIReleerieelKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 971 QDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR------------------QAALEKEEATATRRHLEEAKKE 1032
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhelyeeakakKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1033 HTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH-----VSSLEAEVQRKQNILKEMAAEtnapphpepglh 1107
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAE------------ 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1108 IEDLRKSLGTNENQEvsSSLSLSKEGIDLSMDSVRHFLSAEGVA--VRSAKEFLvrqtrsmrrRQTALKAAQQHWRhela 1185
Cdd:PRK03918 461 LKRIEKELKEIEEKE--RKLRKELRELEKVLKKESELIKLKELAeqLKELEEKL---------KKYNLEELEKKAE---- 525
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1186 SAQEVDEDLPGtkvLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1245
Cdd:PRK03918 526 EYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1274 |
1.45e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 676 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEqqtALQRLREEAETLQKAERAS 755
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 756 lEQKSRRALEQLREQLEAEERSAQAALR----AEKEAEKEATLLQLREQLEGERREA----VAGLEKKHSTELEQlcssl 827
Cdd:PTZ00121 1352 -AEAAADEAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKAdelkKAAAAKKKADEAKK----- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 828 EAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEqELSSLLRDKRQEVE-----REHERKMDKMKE 902
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEakkkaEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 903 EhwQEMAEARERYEAEERKQRADLL--GHLTGELERLRRAHE-------RELESVRQ-EQDQQLEDLRRRHRDQERKLQD 972
Cdd:PTZ00121 1505 A--AEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEkkkadelKKAEELKKaEEKKKAEEAKKAEEDKNMALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 973 LEaELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRV 1052
Cdd:PTZ00121 1583 AE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1053 RRVELESQVDQLQTQSQRLQKHvsslEAEVQRKQNILKEMAAETNapphpepglHIEDLRKSlgtnENQEVSSSLSLSKE 1132
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAK---------KAEELKKK----EAEEKKKAEELKKA 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1133 gidlsmDSVRHFLSAEgvAVRSAKEfLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGT------KVLENVRKN 1206
Cdd:PTZ00121 1725 ------EEENKIKAEE--AKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieeeldEEDEKRRME 1795
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 1207 LDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSLLEEVSDEDTLKGSSIKKVTFDLSDMDDLSSES 1274
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1095 |
2.22e-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: 65.85 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 845 AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLL--RDKRQEVEREHERKMDKMKEEhwqemaearERYEAEERKQ 922
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKD---------LARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 923 RADLLGHLTGELErlrraherELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEK 1002
Cdd:TIGR02168 745 LEERIAQLSKELT--------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1003 QLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEV 1082
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250
....*....|...
gi 1958798735 1083 QRKQNILKEMAAE 1095
Cdd:TIGR02168 897 EELSEELRELESK 909
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
933-1195 |
5.28e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHErELESVRQEQD--QQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQE-ENMRKEKQLLLDAQ 1009
Cdd:COG4913 233 HFDDLERAHE-ALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1010 RQAALEKEEATATRRHLEEAKKEHThlLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNIL 1089
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1090 KEMAAETNApphpepglHIEDLRKSLGTNENQEVssslslskegidlsmdsvrhflsaegvAVRSAKEFLVRQTRSMRRR 1169
Cdd:COG4913 390 AALLEALEE--------ELEALEEALAEAEAALR---------------------------DLRRELRELEAEIASLERR 434
|
250 260
....*....|....*....|....*..
gi 1958798735 1170 QTALKAAQQHWRHELASAQEVDE-DLP 1195
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLDEaELP 461
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
933-1095 |
6.84e-10 |
|
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: 61.09 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHERELESVRQEQD---QQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKQLlldaq 1009
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAaleARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRNNKEY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1010 rqAALEKEEATATRRhLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQtqsQRLQKHVSSLEAEVQRKQNIL 1089
Cdd:COG1579 92 --EALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAER 165
|
....*.
gi 1958798735 1090 KEMAAE 1095
Cdd:COG1579 166 EELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1253 |
7.10e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 924 ADLLGHLTGELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRK 1000
Cdd:TIGR02169 680 RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLldaqrQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1080
Cdd:TIGR02169 759 ELKEL-----EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1081 EVQRKQNILKEMAAETNapphpEPGLHIEDLRKSLGTNENQEVSSSLS---LSKEGIDLSMDsvRHFLSAEGVAVRSAKE 1157
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIK-----SIEKEIENLNGKKEELEEELEELEAAlrdLESRLGDLKKE--RDELEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1158 FLVRQTRSMRRRQTALKAAQQHWRHELAS----AQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSA-MR---------K 1223
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEiedpKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnMLaiqeyeevlK 986
|
330 340 350
....*....|....*....|....*....|
gi 1958798735 1224 GHDLLKKKEEKLNQLESSLLEEVSDEDTLK 1253
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
715-1131 |
1.19e-09 |
|
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: 63.32 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 715 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQ-KAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAT 793
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 794 LLQLRE-QLEGERREAVAGLEKKHStELEQLCSSLEAKHREVISNLQKKIEgAQQKEEAQLQESLGR---AEQRTHQKVH 869
Cdd:pfam12128 489 RLQSELrQARKRRDQASEALRQASR-RLEERQSALDELELQLFPQAGTLLH-FLRKEAPDWEQSIGKvisPELLHRTDLD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 870 QVIEYEQELSSL------LRDKRQEV------EREHERKMDKMKEehwqemaeaRERYEAEERKQRADLLGHLTGELERL 937
Cdd:pfam12128 567 PEVWDGSVGGELnlygvkLDLKRIDVpewaasEEELRERLDKAEE---------ALQSAREKQAAAEEQLVQANGELEKA 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 938 RRAHERELESV--------------RQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQ 1003
Cdd:pfam12128 638 SREETFARTALknarldlrrlfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1004 LLLD----------AQRQAALEKEEaTATRRHLEEAKKEHTHLLESK--------------QQLRRAIDDLRVRRVELES 1059
Cdd:pfam12128 718 AYWQvvegaldaqlALLKAAIAARR-SGAKAELKALETWYKRDLASLgvdpdviaklkreiRTLERKIERIAVRRQEVLR 796
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798735 1060 QVDQLQT----QSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphpepgLHIEDLRKSLGTNENQEVSSSLSLSK 1131
Cdd:pfam12128 797 YFDWYQEtwlqRRPRLATQLSNIERAISELQQQLARLIADTK--------LRRAKLEMERKASEKQQVRLSENLRG 864
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
709-1080 |
1.44e-09 |
|
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: 63.05 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 709 SQRLACLRAQVQSSTEafenqIRAEQQTALQRLREEAETLQKAERAsLEQKSRRALEQLREqleaeersAQAALR-AEKE 787
Cdd:COG3096 284 SERALELRRELFGARR-----QLAEEQYRLVEMARELEELSARESD-LEQDYQAASDHLNL--------VQTALRqQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 788 AEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCSSlEAKHREVISNL---QKKIEgAQQKEEAQLQ---ESLGRAE 861
Cdd:COG3096 350 ERYQEDLEELTERLE-EQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLadyQQALD-VQQTRAIQYQqavQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 862 QRTHQ---KVHQVIEYEQELssllRDKRQEVE---REHERKMDKMKEEHWQemaeareryeaeeRKQRADLLGHLTGELE 935
Cdd:COG3096 427 ALCGLpdlTPENAEDYLAAF----RAKEQQATeevLELEQKLSVADAARRQ-------------FEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 936 R----------LRRAHERELESVRQEQ-DQQLEDLRRRHRDQERkLQDLEAELSSRTKDVKARLAQLnvqEENMRKEKQL 1004
Cdd:COG3096 490 RsqawqtarelLRRYRSQQALAQRLQQlRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEEL---EELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1005 LLDAQRQAALEKEEATATRRHLEEAKKEHTHL------------------------LESKQQLRRAIDDLRVRRVELESQ 1060
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVE 645
|
410 420
....*....|....*....|
gi 1958798735 1061 VDQLQTQSQRLQKHVSSLEA 1080
Cdd:COG3096 646 RDELAARKQALESQIERLSQ 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
764-1244 |
2.04e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 764 LEQLREQLEAEERSAQAALRAEK-EAEKEATLLQLREQLEGerreavaglekKHSTELEQLCSSLEAKHREV---ISNLQ 839
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERvLSDQRGSLDQLKAQIEE-----------KEEKDLHERLNGLESELAELdeeIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 840 KKIEGAQQKEEAqLQESLGRAEQRthqkvhqvieyEQELSSLLR--DKRQEVEREHERKMDKMKEEhwqemaearERYEA 917
Cdd:PRK02224 227 EQREQARETRDE-ADEVLEEHEER-----------REELETLEAeiEDLRETIAETEREREELAEE---------VRDLR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 918 EERKQRADLLGHLTGELErLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlaqlnvQEEN 997
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL------EERA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 998 MrkekqlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1077
Cdd:PRK02224 359 E--------ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1078 LEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKE 1157
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1158 FlvrqTRSMRRRQTALKAAQQHwrhelasAQEVDEDlpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQ 1237
Cdd:PRK02224 511 I----ERLEERREDLEELIAER-------RETIEEK---RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
....*..
gi 1958798735 1238 LESSLLE 1244
Cdd:PRK02224 577 LNSKLAE 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
667-1242 |
2.36e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 667 EKEEEhwLYQQKEKSLSLLKtqlQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAF------ENQIRAEQQTA--- 737
Cdd:TIGR02168 334 ELAEE--LAELEEKLEELKE---ELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqIASLNNEIERLear 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 738 LQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERS-AQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKH 816
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEElEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 817 S--TELEQLCSSLEAKHREVISNLQKKI----------------EGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQE- 877
Cdd:TIGR02168 489 ArlDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQn 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 878 ---------LSSLLRDKRQEVEREHerkmdKMKEEHWQEMAEARERYEAEERKQRADLLGH------LTGELERLRRAHE 942
Cdd:TIGR02168 569 elgrvtflpLDSIKGTEIQGNDREI-----LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRP 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 943 REL----------------------ESVRQEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRK 1000
Cdd:TIGR02168 644 GYRivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRK 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDAQRQAALEKEEATATRRHLEE----AKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVS 1076
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEEriaqLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1077 SLEAEVQRKQNILKEM---------AAETNAPPHPEPGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDL--------SMD 1139
Cdd:TIGR02168 800 ALREALDELRAELTLLneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeeleseleALL 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1140 SVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQevdEDLPGTKV-LENVRKNLDEETK-HLDEM 1217
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVrIDNLQERLSEEYSlTLEEA 956
|
650 660
....*....|....*....|....*
gi 1958798735 1218 KSAMRKGHDLLKKKEEKLNQLESSL 1242
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKI 981
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
930-1073 |
2.53e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 930 LTGELERLRRAHErELESVRQEQDQQLEDLRR--RHRDQERKLQDLEAELSS---RTKDVKARLAQLNVQEENMRKEKQL 1004
Cdd:COG4717 93 LQEELEELEEELE-ELEAELEELREELEKLEKllQLLPLYQELEALEAELAElpeRLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1005 LLDAQRQ-AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQK 1073
Cdd:COG4717 172 LAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
736-979 |
4.57e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 736 TALQRLREEAETLQKAERASLE-QKSRRALEQLREQLE-----AEERSAQAALRAEKEAEKEATLLQLREQLEGERREAV 809
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDaREQIELLEPIRELAEryaaaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 810 AGLEKKHStELEQLCSSLEAKHREvisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrdkrqEV 889
Cdd:COG4913 305 ARLEAELE-RLEARLDALREELDE----LEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------GL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 890 EREHERKmdkmkeehwqemaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQD---QQLEDLRRRHRDQ 966
Cdd:COG4913 374 PLPASAE------------------------------------EFAALRAEAAALLEALEEELEaleEALAEAEAALRDL 417
|
250
....*....|...
gi 1958798735 967 ERKLQDLEAELSS 979
Cdd:COG4913 418 RRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
933-1095 |
6.83e-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: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAhERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK------------ 1000
Cdd:COG4942 42 ELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLL------DAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH 1074
Cdd:COG4942 121 PLALLLspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180
....*....|....*....|.
gi 1958798735 1075 VSSLEAEVQRKQNILKEMAAE 1095
Cdd:COG4942 201 LARLEKELAELAAELAELQQE 221
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
921-1084 |
9.14e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 921 KQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1000
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1080
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
....
gi 1958798735 1081 EVQR 1084
Cdd:COG4372 172 ELQA 175
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
676-983 |
9.95e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 676 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLqKAERAS 755
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 756 LEQKSRRALEQLrEQLEAEERSAQAALRAEKE--AEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLCSSLE-AKHR 832
Cdd:TIGR02168 787 LEAQIEQLKEEL-KALREALDELRAELTLLNEeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEiEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 833 EVISNLQKKIEGAQqKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMD----KMKEEHWQEM 908
Cdd:TIGR02168 866 ELIEELESELEALL-NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRleglEVRIDNLQER 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 909 AEARERYEAEERKQ----RADLLGHLTGELERLRRAHER----------ELESVRQEQD---QQLEDLRRRHRDQERKLQ 971
Cdd:TIGR02168 945 LSEEYSLTLEEAEAlenkIEDDEEEARRRLKRLENKIKElgpvnlaaieEYEELKERYDfltAQKEDLTEAKETLEEAIE 1024
|
330
....*....|..
gi 1958798735 972 DLEAELSSRTKD 983
Cdd:TIGR02168 1025 EIDREARERFKD 1036
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-1081 |
1.18e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTEafENQIRAEQQTALQRLREEAETLQkAERASLEQKSRR------ALEQLREQLEAEERSAQAALR 783
Cdd:COG4717 71 KELKELEEELKEAEE--KEEEYAELQEELEELEEELEELE-AELEELREELEKlekllqLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 784 AEKEAEKEATLLQLREQLEGERREAvagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQkEEAQLQESLGRAEQR 863
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAEL-----AELQEELEELLEQLSLATEEELQDLAEELEELQQ-RLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 864 THQKVHQVIEYEQELSSLLRDKRQEVERE--------------------------------------HERKMDKMKEEHW 905
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 906 QEMAEARERYEAEERKQRAdllghLTGELERLRRAHERELESVRqEQDQQLEDLRRRHRDQERklQDLEAELSSRTKDVK 985
Cdd:COG4717 302 KEAEELQALPALEELEEEE-----LEELLAALGLPPDLSPEELL-ELLDRIEELQELLREAEE--LEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 986 ARLAQLNVQEENMRKEKqlLLDAQRQAALEKEEATATRRhLEEAKKEHTHLLE--SKQQLRRAIDDLRVRRVELESQVDQ 1063
Cdd:COG4717 374 ALLAEAGVEDEEELRAA--LEQAEEYQELKEELEELEEQ-LEELLGELEELLEalDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|....*...
gi 1958798735 1064 LQTQSQRLQKHVSSLEAE 1081
Cdd:COG4717 451 LREELAELEAELEQLEED 468
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
672-1245 |
2.35e-08 |
|
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: 58.83 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 672 HWLYQQKEKSLsllktqlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFENQIRaeqqtALQRLREEAETLQKA 751
Cdd:TIGR00618 242 HAYLTQKREAQ------------------------EEQLKKQQLLKQLRARIEELRAQEA-----VLEETQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 752 ERASLEQKsrrALEQLREQLEAEERSAQaalraekeaEKEATLLQLREQlegerREAVAglekKHSTELEQLCSSLEAKH 831
Cdd:TIGR00618 293 APLAAHIK---AVTQIEQQAQRIHTELQ---------SKMRSRAKLLMK-----RAAHV----KQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 832 REVISNLQKKIEGAQQKEEAQLQESLgraEQRTHQKVHQVIEYEQELSSLlrdkrqeverehERKMDKMKEEHWQEMAEA 911
Cdd:TIGR00618 352 SQEIHIRDAHEVATSIREISCQQHTL---TQHIHTLQQQKTTLTQKLQSL------------CKELDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 912 RERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQL 991
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 992 NVQEENMR--KEKQLLLDAQRQAALEKEeatATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQ 1069
Cdd:TIGR00618 497 LELQEEPCplCGSCIHPNPARQDIDNPG---PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1070 RLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPE---------------PGLHIEDLRKSLGTNENQEVSSSLSLSKEGI 1134
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlaceqhallrklqPEQDLQDVRLHLQQCSQELALKLTALHALQL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1135 DLSMDSVRHflsaegvAVRSAKEFlvrQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTKVLENVRKNLDeetKHL 1214
Cdd:TIGR00618 654 TLTQERVRE-------HALSIRVL---PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD---REF 720
|
570 580 590
....*....|....*....|....*....|.
gi 1958798735 1215 DEMKSAMRKGHDLLKKKEEKLNQLESSLLEE 1245
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
721-1248 |
7.38e-08 |
|
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: 57.07 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 721 SSTEAFENQIRAEQQTALQRLREEAETLQKAeraSLEQKSRraleqlreqLEAEERSAQAALRAEKEAEKEATLLQ---- 796
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRET---SLQQKMR---------LEAQAMELDALAVAEKAGQAEAEGLRaala 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 797 ----LREQL-EGERREavagLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQK----------EEAQLQESLGRAE 861
Cdd:pfam07111 126 gaemVRKNLeEGSQRE----LEEIQRLHQEQL-SSLTQAHEEALSSLTSKAEGLEKSlnsletkragEAKQLAEAQKEAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 862 QRTHQ--KVHQVIEYEQELSSLLRD----------KRQEVEREHERKMDKMKeeHWQEMAEARERYEAEERKQRADLLGH 929
Cdd:pfam07111 201 LLRKQlsKTQEELEAQVTLVESLRKyvgeqvppevHSQTWELERQELLDTMQ--HLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 930 LTGELERLRRAHErELESVRQEQDQQLEDLRRRHRDQ------ERKLQDLEAelSSRTKDVKARLAQLNVQEENMRKEKQ 1003
Cdd:pfam07111 279 LALQEEELTRKIQ-PSDSLEPEFPKKCRSLLNRWREKvfalmvQLKAQDLEH--RDSVKQLRGQVAELQEQVTSQSQEQA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1004 LLLDA--QRQAALEKEEATATRRHLE-----EAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHV 1075
Cdd:pfam07111 356 ILQRAlqDKAAEVEVERMSAKGLQMElsraqEARRRQQQQTASaEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1076 SSLEAEVQRKQNI---------LKEMAAETNAPPHPEP------GLHIEDLRKslgtnENQEVSSSLSLSKEGIDLSMDS 1140
Cdd:pfam07111 436 NRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAPpvdadlSLELEQLRE-----ERNRLDAELQLSAHLIQQEVGR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1141 VRHFLSAEgvavrsakeflvrqtrsmrrRQTALKAAQQhWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSA 1220
Cdd:pfam07111 511 AREQGEAE--------------------RQQLSEVAQQ-LEQELQRAQESLASV--GQQLEVARQGQQESTEEAASLRQE 567
|
570 580
....*....|....*....|....*....
gi 1958798735 1221 MRKGHDLLKKK-EEKLNQLESSLLEEVSD 1248
Cdd:pfam07111 568 LTQQQEIYGQAlQEKVAEVETRLREQLSD 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
777-1022 |
9.96e-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: 55.93 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 777 SAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLcssleAKHREVISNLQKKIEgAQQKEEAQLQES 856
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQL-----AALERRIAALARRIR-ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 857 LGRAEQRTHQKVHQVIEYEQELSSLLRdkRQEVEREHERKMDKMKEEHWQEMAEARE--RYEAEERKQRADLLGHLTGEL 934
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 935 ERLRRAHERE---LESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRtkdvKARLAQLNVQEENMRKekqlLLDAQRQ 1011
Cdd:COG4942 163 AALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEA----LIARLEA 234
|
250
....*....|.
gi 1958798735 1012 AALEKEEATAT 1022
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
716-884 |
1.12e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 716 RAQVQSSTEAFENQIR------AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAE 789
Cdd:COG3206 170 REEARKALEFLEEQLPelrkelEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 790 KE-----------ATLLQLREQ---LEGERREAVAGLEKKHST------ELEQLCSSLEAKHREVISNLQKKIEGAQQkE 849
Cdd:COG3206 250 GSgpdalpellqsPVIQQLRAQlaeLEAELAELSARYTPNHPDvialraQIAALRAQLQQEAQRILASLEAELEALQA-R 328
|
170 180 190
....*....|....*....|....*....|....*
gi 1958798735 850 EAQLQESLGRAEQRthqkVHQVIEYEQELSSLLRD 884
Cdd:COG3206 329 EASLQAQLAQLEAR----LAELPELEAELRRLERE 359
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
718-1022 |
1.24e-07 |
|
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: 56.29 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 718 QVQSSTEAFENQ-IRAEQQTALQRL--REEAETLQKAERASLEQKSRRALEQLREQLEAE---------------ERSAQ 779
Cdd:pfam17380 288 QQQEKFEKMEQErLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErelerirqeerkrelERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 780 AALRAEKEAEKEATLLQLREQLEGERreavagleKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGR 859
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNER--------VRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 860 AEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQ---EMAEARERYEAEERKQRADLlghltgELER 936
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraEEQRRKILEKELEERKQAMI------EEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 937 LRRAHERELEsvrQEQDQQLEDLRRRHRDQERKLQdLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK 1016
Cdd:pfam17380 514 KRKLLEKEME---ERQKAIYEEERRREAEEERRKQ-QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
....*.
gi 1958798735 1017 EEATAT 1022
Cdd:pfam17380 590 EYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
624-1087 |
1.55e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 624 EKEEEEEEEKeeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwlyQQKEKSLSLLKTQLQKAAEEEEKEEETQ 703
Cdd:PTZ00121 1378 KKADAAKKKA------------------------------------------EEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 704 IREEESQrlacLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaEERSAQAALR 783
Cdd:PTZ00121 1416 AKKKADE----AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE-EAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 784 AEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTEL---EQLCSSLEAKHREVISNLQ--KKIEGAQQKEEAQLQESLG 858
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKKADelKKAEELKKAEEKKKAEEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 859 RAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGEL---E 935
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 936 RLRRAHER------ELESVRQEQDQQLEDLRRRHRDQERKLQDL--EAELSSRTKDVKARLAQLNVQEENMRKEKQL--- 1004
Cdd:PTZ00121 1651 ELKKAEEEnkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnki 1730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1005 -LLDAQRQAALEKEEATATRRHLEEAKK-EHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEV 1082
Cdd:PTZ00121 1731 kAEEAKKEAEEDKKKAEEAKKDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
....*
gi 1958798735 1083 QRKQN 1087
Cdd:PTZ00121 1811 IEGGK 1815
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
812-1260 |
1.60e-07 |
|
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: 56.18 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 812 LEKKHsTELEQLCSSLEAKHREVISNLQKKiegaqQKEEAQLQESLgraeQRTHQKVHQVIEYEQELSSLLRDKRQEVER 891
Cdd:TIGR04523 209 KIQKN-KSLESQISELKKQNNQLKDNIEKK-----QQEINEKTTEI----SNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 892 eHERKMDkmkeehwqemaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQL-EDLRRRHRDQERKL 970
Cdd:TIGR04523 279 -NNKKIK----------------------------------ELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 971 QDLEAELSSRTKdvkaRLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDL 1050
Cdd:TIGR04523 324 EEIQNQISQNNK----IISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1051 RVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRkqniLKEMAAETNApphpepglHIEDLrkslgTNENqevsSSLSLS 1130
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNS--------EIKDL-----TNQD----SVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1131 KEGIDLSMDSVRHFLSAegvavrsakeflvrQTRSMRRRQTALKAAQqhwrhelasaQEVDEDLPGTKVLENVRKNLDEE 1210
Cdd:TIGR04523 456 IKNLDNTRESLETQLKV--------------LSRSINKIKQNLEQKQ----------KELKSKEKELKKLNEEKKELEEK 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958798735 1211 TKHL----DEMKSAMRKGHDLLKKKEEKLNQLESSLLEevsDEDTLKGSSIKKV 1260
Cdd:TIGR04523 512 VKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDELNK---DDFELKKENLEKE 562
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
679-1050 |
1.62e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 679 EKSLSLLKTQLqkaaeeeekeeetqireeesQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkaeRASLEQ 758
Cdd:TIGR02169 687 KRELSSLQSEL--------------------RRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKL----KERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 759 kSRRALEQLREQLEAEERSaQAALRAEKEaEKEATLLQLREQLEG-ERREAVAGLEK--KHSTELEQLCSSLEAKHREVI 835
Cdd:TIGR02169 742 -LEEDLSSLEQEIENVKSE-LKELEARIE-ELEEDLHKLEEALNDlEARLSHSRIPEiqAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 836 SNLQKKiegaqQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKR--QEVEREHERKMDKMKEEhwqemaeare 913
Cdd:TIGR02169 819 QKLNRL-----TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEelEEELEELEAALRDLESR---------- 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 914 ryeaeerkqradlLGHLTGELERLrRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------- 986
Cdd:TIGR02169 884 -------------LGDLKKERDEL-EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipee 949
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 987 RLAQLNVQEENMRKEKQLL-LDAQRQAALEKEEATATRrhLEEAKKEHTHLLESKQQLRRAIDDL 1050
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRaLEPVNMLAIQEYEEVLKR--LDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
732-1238 |
1.67e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 732 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleAEERSAQAALRAEKEAEKEatllQLREQLEGERREAVAG 811
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM--QMERDAMADIRRRESQSQE----DLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 812 ------LEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQQKEEAQLQE----------SLGRAEQRTHQKVHQVIEYE 875
Cdd:pfam15921 158 kclkedMLEDSNTQIEQL-RKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmstmhfrSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 876 QELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEerkqradllghLTGELERLRRAherelESVRQEQDQQ 955
Cdd:pfam15921 237 KGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-----------ITGLTEKASSA-----RSQANSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 956 LEDLRRRHRDQE----RKLQDLEAELSSRTKDVKarlaqlnvqeENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKK 1031
Cdd:pfam15921 301 LEIIQEQARNQNsmymRQLSDLESTVSQLRSELR----------EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1032 EHTHLlesKQQLRRAIDDLRVRRVELESQVDQLQTQSQR----------LQKHVSSLEAEVQRKQNILKEMAAETNapph 1101
Cdd:pfam15921 371 ESGNL---DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQ---- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1102 pepGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWR 1181
Cdd:pfam15921 444 ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798735 1182 HELASAQEVDEDLPGTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQL 1238
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
732-1050 |
2.07e-07 |
|
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: 54.92 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 732 AEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAAlRAEKEAEKEATLLQLREQLEGERREAVAG 811
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 812 LEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQEslGRAEQRTHQKVHQVIEYEQELSSLLrdKRQEVER 891
Cdd:pfam13868 122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKA--EREEEREAEREEIEEEKEREIARLR--AQQEKAQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 892 EHERKMDKMKEEHWQEmaeareryeaeerkqradllghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQ 971
Cdd:pfam13868 198 DEKAERDELRAKLYQE-------------------------EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 972 DLEAElssrtKDVKARLAQLNVQEENMRKEKQlllDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDL 1050
Cdd:pfam13868 253 AEEAE-----REEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
738-1096 |
2.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 738 LQRLREEAETLQKA---ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLE- 813
Cdd:COG4717 48 LERLEKEADELFKPqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 814 -------KKHSTELEQLCSSLEA--KHREVISNLQKKIEGAQQ---KEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL 881
Cdd:COG4717 128 lplyqelEALEAELAELPERLEEleERLEELRELEEELEELEAelaELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 882 LRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRAD---------------------------------LLG 928
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 929 HLTGELERLRRAHERELESVR-QEQDQQLEDLR-RRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLL 1006
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQaLPALEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1007 DAQRQAAL-------EKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR-----RVELESQVDQLQTQSQRLQKH 1074
Cdd:COG4717 368 LEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEELEEE 447
|
410 420
....*....|....*....|..
gi 1958798735 1075 VSSLEAEVQRKQNILKEMAAET 1096
Cdd:COG4717 448 LEELREELAELEAELEQLEEDG 469
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
729-1269 |
2.73e-07 |
|
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: 55.57 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 729 QIRAEQQTALQRLREEAETLQKAERASleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegERREA 808
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQL--STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE---EKAAA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 809 VAGLEKKHS---TELEQLCSSLEaKHREVISNLQKKIEGAQQ--KEE----AQLQESLGRAEQRTHQKVHQVIEYEQELS 879
Cdd:pfam01576 568 YDKLEKTKNrlqQELDDLLVDLD-HQRQLVSNLEKKQKKFDQmlAEEkaisARYAEERDRAEAEAREKETRALSLARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 880 SLLrDKRQEVEREHERKMDKMKEehwqemaeareryeaeeRKQRADLLGHLTGELERLRRAHERELESVRqEQDQQLED- 958
Cdd:pfam01576 647 EAL-EAKEELERTNKQLRAEMED-----------------LVSSKDDVGKNVHELERSKRALEQQVEEMK-TQLEELEDe 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 959 --------LRRRHRDQ------ERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEA----T 1020
Cdd:pfam01576 708 lqatedakLRLEVNMQalkaqfERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELeaqiD 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1021 ATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRvelesqvDQLQTQSQRLQKHVSSLEAEVQRKQNIL----------- 1089
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELEEARASR-------DEILAQSKESEKKLKNLEAELLQLQEDLaaserarrqaq 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1090 ---KEMAAETNAPPHPEPGLHIE----DLRKSLGTNENQEVSSSLSLSKE---GIDLSMDSVRHFLSAEGVA---VRSAK 1156
Cdd:pfam01576 861 qerDELADEIASGASGKSALQDEkrrlEARIAQLEEELEEEQSNTELLNDrlrKSTLQVEQLTTELAAERSTsqkSESAR 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1157 EFLVRQTRSMRRR--------QTALKAAQQHWRHELASA-----QEVDEDLPGTKVLENVRKNL-------DEETKHLDE 1216
Cdd:pfam01576 941 QQLERQNKELKAKlqemegtvKSKFKSSIAALEAKIAQLeeqleQESRERQAANKLVRRTEKKLkevllqvEDERRHADQ 1020
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958798735 1217 MKSAMRKGHDLLKkkeeklnQLESSlLEEVSDEDTLKGSSIKKVTFDLSDMDD 1269
Cdd:pfam01576 1021 YKDQAEKGNSRMK-------QLKRQ-LEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
716-1033 |
3.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 716 RAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLE--QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAT 793
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 794 LLQL----------------------------------------REQLEGERREAVAGLEKKHSTELEQLCSSLEAKHre 833
Cdd:COG4717 252 LLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALG-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 834 VISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQkvHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHwqemaeare 913
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ--------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 914 RYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDvkARLAQLNV 993
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798735 994 QEENMRKEKQLLldAQRQAALEKEEATAtRRHLEEAKKEH 1033
Cdd:COG4717 477 ELEELKAELREL--AEEWAALKLALELL-EEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
808-1087 |
3.48e-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: 54.38 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 808 AVAGLEKKHSTELEQLcssleakhREVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSsLLRDKRQ 887
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 888 EVEREhERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAheRELESVRQEQDQQLEDLRRRhrdqe 967
Cdd:COG4942 87 ELEKE-IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRAD----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 968 rklqdleaelssrtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAalekeeatatRRHLEEAKKEHTHLLESkqqlrrai 1047
Cdd:COG4942 159 -----------------LAELAALRAELEAERAELEALLAELEEE----------RAALEALKAERQKLLAR-------- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798735 1048 ddLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQN 1087
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
710-992 |
3.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTEAFE--NQIRAEQQTALQRLREEAETLQKAERASLEQKS----RRALEQLREQLEAEERSAQAALR 783
Cdd:COG4913 610 AKLAALEAELAELEEELAeaEERLEALEAELDALQERREALQRLAEYSWDEIDvasaEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 784 AEKEAEK-EATLLQLREQLEgERREAVAGLEKKHsTELEQLCSSLEAKhrevisnLQKKIEGAQQKEEAQLQESLGRAEQ 862
Cdd:COG4913 690 LEEQLEElEAELEELEEELD-ELKGEIGRLEKEL-EQAEEELDELQDR-------LEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 863 RTHQKvhqviEYEQELSSLLRDKRQEVEREHERKMDKMKE--EHWQEMAEARERYEAEERKQRAdLLGHLTGelERLRRA 940
Cdd:COG4913 761 DAVER-----ELRENLEERIDALRARLNRAEEELERAMRAfnREWPAETADLDADLESLPEYLA-LLDRLEE--DGLPEY 832
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 941 HERELESVRQEQDQQLEDLRRRHRDQERklqdleaelssrtkDVKARLAQLN 992
Cdd:COG4913 833 EERFKELLNENSIEFVADLLSKLRRAIR--------------EIKERIDPLN 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
923-1245 |
5.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 923 RADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1000
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDAQRQAALEKEEATATRR--HLEEAKKEHTHLLESKQQLRRAIDDLRVRRVE------------LESQVDQLQT 1066
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEElleqlslateeeLQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1067 QSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTnenqeVSSSLSLSKEGIDLsMDSVRHFLS 1146
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI-----AAALLALLGLGGSL-LSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1147 AEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEdlpgtkVLENVRKNLDEETKHLDEMKSAMRKGHD 1226
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE------LLAALGLPPDLSPEELLELLDRIEELQE 351
|
330
....*....|....*....
gi 1958798735 1227 LLKKKEEKLNQLESSLLEE 1245
Cdd:COG4717 352 LLREAEELEEELQLEELEQ 370
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
718-1084 |
7.08e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.29 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 718 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAerasleQKSRRALE-------QLREQLEAEERSAQAALRAEKEAEK 790
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERA------KQYQQVIDnfpklsaELRQQLNNERDEPRSVPPNMSTDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 791 EATLLQLREQLEGERREAVAGLEKKH--STELEQLCSSLEAKHR---EVISNLQKKIEGAQQKEEAQLqeSLGRAEQRTH 865
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDRAReiSDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQL--TALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 866 Q-KVHqvieyEQELSSLLRDKRQEVEReherkmdkMKEEHWQEmaeareryeaeeRKQRADL-LGHLTGELERLR-RAHE 942
Cdd:PRK10929 186 KaLVD-----ELELAQLSANNRQELAR--------LRSELAKK------------RSQQLDAyLQALRNQLNSQRqREAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 943 RELESVRQEQDQQlEDLRRRHRDQERKLQDLEAElssrtkdvkarlaqLNVQEENMrkekQLLLDAQRQAA---LEKEEA 1019
Cdd:PRK10929 241 RALESTELLAEQS-GDLPKSIVAQFKINRELSQA--------------LNQQAQRM----DLIASQQRQAAsqtLQVRQA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 1020 TATRRHLEEAKKEHTHLLES-------------KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1084
Cdd:PRK10929 302 LNTLREQSQWLGVSNALGEAlraqvarlpempkPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNR 379
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
950-1098 |
8.98e-07 |
|
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: 51.85 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 950 QEQDQQLEDLRRRHRDQERKLQDLEAELssrtKDVKARLAQLNVQEENMRKEKqllldAQRQAALEKEEATATR--RHLE 1027
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEI-----KRLELEIEEVEARIKKyeEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798735 1028 EAK--KEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1098
Cdd:COG1579 84 NVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
933-1035 |
1.83e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDL---EAELSSRTKDVKARLAQLNVQEENM-RKEKQLLLDA 1008
Cdd:PRK12704 65 EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEELeELIEEQLQEL 144
|
90 100
....*....|....*....|....*..
gi 1958798735 1009 QRQAALEKEEATAtrRHLEEAKKEHTH 1035
Cdd:PRK12704 145 ERISGLTAEEAKE--ILLEKVEEEARH 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
942-1095 |
2.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 942 ERELESVRQEQDQ---QLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEkQLLLDAQ-------RQ 1011
Cdd:COG3883 43 QAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-DVLLGSEsfsdfldRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1012 AALEKEeATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1091
Cdd:COG3883 122 SALSKI-ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
....
gi 1958798735 1092 MAAE 1095
Cdd:COG3883 201 LEAE 204
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
934-1095 |
2.53e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 934 LERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAE-----LSSRTKDVKARLAQLNVQeenmrkekqlLLDA 1008
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQ----------LAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1009 QRQAALEKEEATATRRHLEEAKKEHTHLLESK--QQLRRAIDDLRVRR--------------VELESQVDQLQTQ-SQRL 1071
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQlQQEA 311
|
170 180
....*....|....*....|....
gi 1958798735 1072 QKHVSSLEAEVQRKQNILKEMAAE 1095
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQ 335
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
721-1164 |
2.77e-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: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 721 SSTEAFENQIRAEQQTALQrLREEAETlQKAEraslEQKSRRALEQLREQLEAEERSAQAALRAEKEA----EKEATLLQ 796
Cdd:pfam05483 310 STQKALEEDLQIATKTICQ-LTEEKEA-QMEE----LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRleknEDQLKIIT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 797 LREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQ-KKIEGAQQKEEAQLQESLGRAEQRTHQ---KVHQVI 872
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDleiQLTAIK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 873 EYEQELSSLLRDKRQEVEREHERKM------DKMKEEHwQEMAEARERYEAEERKQRADLLGHLTGElERLRRAHER--- 943
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIeltahcDKLLLEN-KELTQEASDMTLELKKHQEDIINCKKQE-ERMLKQIENlee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 944 -------ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEK 1016
Cdd:pfam05483 542 kemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1017 EEATATRRHLE----EAKKEHTHLLESKQQLRRAID----DLRVRRVELESQVDQLQtQSQRLQKHVSSLEAEV-QRKQN 1087
Cdd:pfam05483 622 KKGSAENKQLNayeiKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIdKRCQH 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1088 ILKEMAAETNAPPHPEPGLhIEDLRKSLG--TNENQEVSS---SLSLSKEGIDLSMDSVRHFLSAEgvavRSAKEFLVRQ 1162
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKI-IEERDSELGlyKNKEQEQSSakaALEIELSNIKAELLSLKKQLEIE----KEEKEKLKME 775
|
..
gi 1958798735 1163 TR 1164
Cdd:pfam05483 776 AK 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
672-1018 |
4.35e-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: 51.65 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 672 HWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQqtalqRLREEAETLQKA 751
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE-----RMLKQIENLEEK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 752 ErasleQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQlegerreavaglekKHSTELEQLCSSLeakh 831
Cdd:pfam05483 543 E-----MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE--------------KQMKILENKCNNL---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 832 REVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVhQVIEYEQELSSLlRDKRQEVEREHERKMD--KMKEEHWQEMA 909
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI-KVNKLELELASA-KQKFEEIIDNYQKEIEdkKISEEKLLEEV 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 910 EARERYEAEERKQRADL---LGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA 986
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIdkrCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
330 340 350
....*....|....*....|....*....|..
gi 1958798735 987 RLAQLNVQEEnmRKEKqLLLDAQRQAALEKEE 1018
Cdd:pfam05483 758 LKKQLEIEKE--EKEK-LKMEAKENTAILKDK 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-1083 |
4.43e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 699 EEETQIREEESQRLACLRAQVQSSTEAFENQIRaEQQTALQRLREEAETLqkAERASLEQKSRRALEQLREQLEAEERSA 778
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVR-DLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 779 Q--------AALRAEKEAEKEATLLQLREQLEGERREAVAGLEkkhsTELEQLCSSLEaKHREVISNLQKKIEGAqQKEE 850
Cdd:PRK02224 327 RdrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVE-DRREEIEELEEEIEEL-RERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 851 AQLQESLGRAEQR------THQKVHqviEYEQELSSLLRDKRQEVErEHERKMDKMK-EEHWQEMAEARERYEAEERKQR 923
Cdd:PRK02224 401 GDAPVDLGNAEDFleelreERDELR---EREAELEATLRTARERVE-EAEALLEAGKcPECGQPVEGSPHVETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 924 ADLLGHLTGELERLRRAHERELESVRQ--EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvkaRLAQLNVQEENMRKE 1001
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRE----RAEELRERAAELEAE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1002 KQllldAQRQAALEK-EEATATRRHLEEAKKEHTHLLESKQQLRR-------------AIDDLRVRRVELESQVDQLQTQ 1067
Cdd:PRK02224 553 AE----EKREAAAEAeEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKREALAELNDERRER 628
|
410
....*....|....*.
gi 1958798735 1068 SQRLQKHVSSLEAEVQ 1083
Cdd:PRK02224 629 LAEKRERKRELEAEFD 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
728-1082 |
5.01e-06 |
|
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: 51.33 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 728 NQIRAEQQTALQRLREEAEtlqKAERASLEQKSR-----RALEQLREQLEAEERsAQAALRAEKEA---EKEATLLQLRE 799
Cdd:pfam01576 607 DQMLAEEKAISARYAEERD---RAEAEAREKETRalslaRALEEALEAKEELER-TNKQLRAEMEDlvsSKDDVGKNVHE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 800 qLEGERREAVAGLE--KKHSTELE-QLCSSLEAKHRevisnLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ 876
Cdd:pfam01576 683 -LERSKRALEQQVEemKTQLEELEdELQATEDAKLR-----LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 877 ELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLR----------RAHERELE 946
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilaqsKESEKKLK 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 947 SVRQEQDQQLEDL-----RRRHRDQERklQDLEAELSSRTKD----------VKARLAQLNVQEENMRKEKQLLLDAQRQ 1011
Cdd:pfam01576 837 NLEAELLQLQEDLaaserARRQAQQER--DELADEIASGASGksalqdekrrLEARIAQLEEELEEEQSNTELLNDRLRK 914
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 1012 AALEKEEATATRrhleEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSqrlqkhVSSLEAEV 1082
Cdd:pfam01576 915 STLQVEQLTTEL----AAERSTSQKSESaRQQLERQNKELKAKLQEMEGTVKSKFKSS------IAALEAKI 976
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1008-1256 |
5.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1008 AQRQAALE--KEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRK 1085
Cdd:COG4942 23 AEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1086 QNILKEMAAE---TNAPPHPEPGLHIEDLrkslgtnenQEVSSSLSLskegidlsMDSVRHFLSAEGVAVRSAKEFLVRQ 1162
Cdd:COG4942 103 KEELAELLRAlyrLGRQPPLALLLSPEDF---------LDAVRRLQY--------LKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1163 TRS---MRRRQTALKAAQQHWRHELASAQEVDEDLpgtkvLENVRKNLDEETKHLDEmksamrkghdlLKKKEEKLNQLE 1239
Cdd:COG4942 166 RAEleaERAELEALLAELEEERAALEALKAERQKL-----LARLEKELAELAAELAE-----------LQQEAEELEALI 229
|
250
....*....|....*..
gi 1958798735 1240 SSLLEEVSDEDTLKGSS 1256
Cdd:COG4942 230 ARLEAEAAAAAERTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
744-1093 |
6.85e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 744 EAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRA-------EKEAEKEATLLQLREQLEGERREAVAGLEKK 815
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDdLNNQILELEGYEMDYNSYLKSieslkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 816 HSTELEQLCSSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQR-------TH---QKVHQVIEYEQELSSLLRDK 885
Cdd:PRK01156 410 ELNEINVKLQDISSK----VSSLNQRIRALRENLD-ELSRNMEMLNGQsvcpvcgTTlgeEKSNHIINHYNEKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 886 RQEVERE------HERKMDKMKEEHWQEMAEARERYEAEERKQRADLlGHLTGELERLRRAHERELESVRQEQDQQLEDL 959
Cdd:PRK01156 485 IREIEIEvkdideKIVDLKKRKEYLESEEINKSINEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRYKSLKLEDL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 960 RRRHRD-----QERKLQDLEA------ELSSRTKDVKARLAQLNVQEE------------------------NMRKEKQL 1004
Cdd:PRK01156 564 DSKRTSwlnalAVISLIDIETnrsrsnEIKKQLNDLESRLQEIEIGFPddksyidksireieneannlnnkyNEIQENKI 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1005 LLDAQRQAALEKEEATATRRHLEEAKKEHT-HLLESK---QQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEA 1080
Cdd:PRK01156 644 LIEKLRGKIDNYKKQIAEIDSIIPDLKEITsRINDIEdnlKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
410
....*....|...
gi 1958798735 1081 EVQRKQNILKEMA 1093
Cdd:PRK01156 724 TLESMKKIKKAIG 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1049 |
8.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 839 QKKIEgAQQKEEAQLQESLGRAEQRthqkvhqvieyeqelsslLRDKRQEVEREHERKmdkmkeEHWQEMAEARERYEAE 918
Cdd:COG4913 609 RAKLA-ALEAELAELEEELAEAEER------------------LEALEAELDALQERR------EALQRLAEYSWDEIDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 919 ERKQRAdlLGHLTGELERLRRAHE--RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEE 996
Cdd:COG4913 664 ASAERE--IAELEAELERLDASSDdlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958798735 997 NMRKEKQLLLDAQRQAALEKEEATATRRHLEEA-KKEHTHLLESKQQLRRAIDD 1049
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERiDALRARLNRAEEELERAMRA 795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
862-1094 |
8.76e-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: 50.72 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 862 QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERKMDKMKeeHWQEmaeareryEAEERKQRADLLGHLT 931
Cdd:COG3096 812 QRLHQAFSQFVgghlavafapDPEAELA-ALRQRRSELERELAQHRAQEQ--QLRQ--------QLDQLKEQLQLLNKLL 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 932 GELERLRRA-HERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKARLAQLNVQEENMRKEKQLL 1005
Cdd:COG3096 881 PQANLLADEtLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFAL 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1006 LD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQ 1083
Cdd:COG3096 961 SEvVQRRPHFSYEDA-------VGLLGENSDLNEKlRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ 1033
|
250
....*....|.
gi 1958798735 1084 RKQNILKEMAA 1094
Cdd:COG3096 1034 TLQELEQELEE 1044
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
662-1080 |
9.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 662 EEEKEEKeeehwlYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSsteafenqiRAEQQTALQRL 741
Cdd:COG4717 104 LEELEAE------LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE---------LRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 742 REEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK-EATLLQLREQLEGERREAVAGLEKKHSTEL 820
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 821 EQLCSSLEAkhREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKM 900
Cdd:COG4717 249 RLLLLIAAA--LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 901 KEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRR-AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLeaelss 979
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLeELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL------ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 980 rtkdvKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATaTRRHLEEAKKEHTHLLESKQQLRRAIDDLR--VRRVEL 1057
Cdd:COG4717 401 -----KEELEELEEQLEELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREELAELEAELEQLEedGELAEL 474
|
410 420
....*....|....*....|...
gi 1958798735 1058 ESQVDQLQTQSQRLQKHVSSLEA 1080
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKL 497
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
717-1029 |
9.93e-06 |
|
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: 50.14 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 717 AQVQSSTEAFENQIRAEQ---QTALQRLREEAETLQK---AERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEK 790
Cdd:pfam09731 161 AHTDSLKEASDTAEISREkatDSALQKAEALAEKLKEvinLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 791 EATLL-QLREQLEGERREAVAGLEKKH------STELEQLCS----SLEAKHREVISNLQKKIEGAQQKEEAQLQESL-G 858
Cdd:pfam09731 241 LAKLVdQYKELVASERIVFQQELVSIFpdiipvLKEDNLLSNddlnSLIAHAHREIDQLSKKLAELKKREEKHIERALeK 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 859 RAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghLTGELERLR 938
Cdd:pfam09731 321 QKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--------------------------LRTELERQA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 939 RAHERELESVRQEQDQQLEdlRRRHRD------QERKLQDLE-AELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQR- 1010
Cdd:pfam09731 375 EAHEEHLKDVLVEQEIELQ--REFLQDikekveEERAGRLLKlNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVEAl 452
|
330
....*....|....*....
gi 1958798735 1011 QAALEKEEATATRRHLEEA 1029
Cdd:pfam09731 453 RSTLEDGSADSRPRPLVRE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-1249 |
1.02e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 709 SQRLACLRAQVQSSTEAFENQIRAeqqtalqrlreeaetlQKAERASLE---QKSRRALEQLREQLEAEERSAQAALRAE 785
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEE----------------ERKRRDKLTeeyAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 786 KEAEKEATLLQ-LREQLEGERREAVAGLEKKHS--TELEQLCSSLEAKHREVIS---NLQKKIEGAQQKEEaQLQESLGR 859
Cdd:TIGR02169 388 KDYREKLEKLKrEINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEekeDKALEIKKQEWKLE-QLAADLSK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 860 AEQRTHQKVHQVIEYEQELSSLlrdKRQEVEREHERKMdkmkeehWQEMAEARERYEAEERKQRADLLGhLTGELERLRR 939
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKL---QRELAEAEAQARA-------SEERVRGGRAVEEVLKASIQGVHG-TVAQLGSVGE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 940 AHERELES---------------------------------------VRQEQ---------------------DQQLE-- 957
Cdd:TIGR02169 536 RYATAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnkMRDERrdlsilsedgvigfavdlvefDPKYEpa 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 958 --------------DLRRRHRDQERkLQDLEAEL-----------------SSRTKDVKARLAQLNVQEENMRKEKQLLL 1006
Cdd:TIGR02169 616 fkyvfgdtlvvediEAARRLMGKYR-MVTLEGELfeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1007 DAQRQAaleKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQ 1086
Cdd:TIGR02169 695 SELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1087 NILKEMAAETNAPPHPEPGLHIEDLRKSLgtNENQEVSSSLSLSKEGIDLSMDSvrhfLSAEGVAVRSAKEFLVRQTRSM 1166
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAEL--SKLEEEVSRIEARLREIEQKLNR----LTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1167 RRRQTALKAAQQHWRHELASAQEVDEDLPG-TKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLESSL--- 1242
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAaLRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkak 925
|
....*..
gi 1958798735 1243 LEEVSDE 1249
Cdd:TIGR02169 926 LEALEEE 932
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
58-87 |
1.12e-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: 1.12e-05
10 20 30
....*....|....*....|....*....|
gi 1958798735 58 LPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:pfam00397 1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
731-1072 |
1.15e-05 |
|
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: 50.17 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 731 RAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKE--------ATLLQLREQLE 802
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEnaelqaelRTLQQAKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 803 GERREAVAGLEK--------------------KHSTELEQLCSSLEAKHREVIsNLQKKIEGAqqkeEAQLQESLGRAEQ 862
Cdd:pfam01576 405 HKRKKLEGQLQElqarlseserqraelaeklsKLQSELESVSSLLNEAEGKNI-KLSKDVSSL----ESQLQDTQELLQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 863 RTHQKV---HQVIEYEQELSSLLrdKRQEVEREHERKMDKMKEEHWQEMaeareryeAEERKQRADLLGHLTGeLERLRR 939
Cdd:pfam01576 480 ETRQKLnlsTRLRQLEDERNSLQ--EQLEEEEEAKRNVERQLSTLQAQL--------SDMKKKLEEDAGTLEA-LEEGKK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 940 AHERELESVRQ---EQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKA------RLAQLNVQEENMRKEKQLLLDAQR 1010
Cdd:pfam01576 549 RLQRELEALTQqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNlekkqkKFDQMLAEEKAISARYAEERDRAE 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 1011 QAALEKE-EATATRRHLEEAKKEHTHLLESKQQLRRAIDDL---------------RVRRVeLESQVDQLQTQSQRLQ 1072
Cdd:pfam01576 629 AEAREKEtRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvgknvheleRSKRA-LEQQVEEMKTQLEELE 705
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
676-975 |
1.19e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 676 QQKEKSLSLL--KTQLQKAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAER 753
Cdd:pfam17380 303 QEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 754 ASLEQKSRRalEQLREQLEAEER-SAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKHSTELEQLcssleakhR 832
Cdd:pfam17380 383 LQMERQQKN--ERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV--------R 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 833 EVISNLQKKIEGAQQKEEAQLQESLG-----RAEQRTHQKVHQVIEYEQElssllRDKRQEVEREHERKMDKMKEEHWQE 907
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKILEKELE-----ERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 908 MAEARERYEAEERKQRADLlghltgELERLRRAHEREL----ESVRQEQDQQLEDLRRRHRDQERKLQDLEA 975
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQ------EMEERRRIQEQMRkateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
926-1098 |
2.88e-05 |
|
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: 48.14 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 926 LLGHLTGELERLRRAHER--ELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK-----------------DVKA 986
Cdd:pfam19220 32 LIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVArlakleaalreaeaakeELRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 987 RLAQLNVQEENMrkEKQLLLDAQRQAALEKE------EATATRRHLEEAKKEhthLLESKQQLRRAIDDLRVRRVELESQ 1060
Cdd:pfam19220 112 ELRDKTAQAEAL--ERQLAAETEQNRALEEEnkalreEAQAAEKALQRAEGE---LATARERLALLEQENRRLQALSEEQ 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798735 1061 VDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNA 1098
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLAAEQAE 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
749-986 |
3.00e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 749 QKAERASLEQK---SRRALEQLREQLEAEERSAQAALRAEKEAEKE-ATLLQLREQLEGERREAVAGLEKKhSTELEQLC 824
Cdd:COG4942 18 QADAAAEAEAEleqLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAEL-EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 825 SSLEAKHREVISNLQKKIEGAQQKEEAQL--QESLGRAEQRThQKVHQVIEYEQELSSLLRDKRQEVEReherkmdkmKE 902
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAA---------LR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 903 EHWQEMAEARERYEAEERKQRADLLghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTK 982
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALE-----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 1958798735 983 DVKA 986
Cdd:COG4942 242 RTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-1021 |
3.63e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 728 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEA--EERSAQAALRAEKEAEKEATLLQLREQLEGEr 805
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 806 reaVAGLEKkhstELEQLcSSLEAKHREVISNLQKKiegaqqkeEAQLQESLGRAEQRTHQKVHQVIEYEQELSSL---- 881
Cdd:PRK03918 541 ---IKSLKK----ELEKL-EELKKKLAELEKKLDEL--------EEELAELLKELEELGFESVEELEERLKELEPFyney 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 882 --LRDKRQEVEREhERKMDKMKEEHWQ--EMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLE 957
Cdd:PRK03918 605 leLKDAEKELERE-EKELKKLEEELDKafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELE 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 958 DLRRRHRDQERKLQDLEAELSSRTK------DVKARLAQLNVQEENMRKEKQLLldaqRQAALEKEEATA 1021
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEELREKVKKYKALL----KERALSKVGEIA 749
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
59-89 |
4.12e-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: 4.12e-05
10 20 30
....*....|....*....|....*....|.
gi 1958798735 59 PKGWKPCQNITGDLYYFNFDTGQSIWDHPCD 89
Cdd:cd00201 1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
676-895 |
4.56e-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: 47.45 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 676 QQKEKSLSLLKTQLQKAAEEEEKEEETQIREEesQRLACLRAQVQSSTE---AFENQIrAEQQTALQRLREEAETLQKae 752
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARrirALEQEL-AALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 753 raSLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSLEAKHR 832
Cdd:COG4942 98 --ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 833 EVISNLQKKIE-----GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHER 895
Cdd:COG4942 175 ELEALLAELEEeraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
758-1024 |
4.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 758 QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQlreqlegERREAVAGLEKKHSTELEqlcssLEAKHREvISN 837
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEID-----VASAERE-IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 838 LQKKIE---------GAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSlLRDKRQEVEREHERKMDkmKEEHWQEM 908
Cdd:COG4913 673 LEAELErldassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAED--LARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 909 AEARERYEAEERKQRADLLGHLTGELERLRRAHERElesvrqeqDQQLEDLRRRH-RDQERKLQDLEAELSSRTkDVKAR 987
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRA--------EEELERAMRAFnREWPAETADLDADLESLP-EYLAL 820
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798735 988 LAQLNVQE--ENMRKEKQLLLDAQRQ------AALEKEEATATRR 1024
Cdd:COG4913 821 LDRLEEDGlpEYEERFKELLNENSIEfvadllSKLRRAIREIKER 865
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
935-1098 |
5.04e-05 |
|
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: 46.21 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 935 ERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKdvKARLAqLNVQEENMRKEKqllldAQRQAAL 1014
Cdd:pfam04012 24 EKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE--KAQAA-LTKGNEELAREA-----LAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1015 EKeeatatrrHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL--QTQSQRLQKHV---------SSLEAEVQ 1083
Cdd:pfam04012 96 EK--------QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVqtslgslstSSATDSFE 167
|
170
....*....|....*
gi 1958798735 1084 RKQNILKEMAAETNA 1098
Cdd:pfam04012 168 RIEEKIEEREARADA 182
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
833-1122 |
7.59e-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: 47.26 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 833 EVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLlrdkrqeverehERKMDKMKEEHWQEMAEAR 912
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEES------------KRETETGIQNLTAEIEQGQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 913 ERYEAEERKQRADLlGHLTGElERLRRAhERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLN 992
Cdd:COG5185 350 ESLTENLEAIKEEI-ENIVGE-VELSKS-SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 993 VQ--------EENMRKEKQLLLDAQRQAALEKEEATAtrrHLEEAKKEHthllesKQQLRRAIDDLRVRRVELESQVDQL 1064
Cdd:COG5185 427 RQieqatssnEEVSKLLNELISELNKVMREADEESQS---RLEEAYDEI------NRSVRSKKEDLNEELTQIESRVSTL 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798735 1065 QTQsqrLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHI---EDLRKSLGTNENQE 1122
Cdd:COG5185 498 KAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIlalENLIPASELIQASN 555
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
932-1096 |
8.50e-05 |
|
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: 46.81 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 932 GELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDV---KARLAQLNVQEENMRKEKQLLLDA 1008
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHeelEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1009 -----QRQAALEKEEATATRRHLEeakkEHTHLLESKQQLRRAIDDLRvrrvELESQVDQLQTQSQRLQKHVSSLEAEVQ 1083
Cdd:pfam07888 124 raaheARIRELEEDIKTLTQRVLE----RETELERMKERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|...
gi 1958798735 1084 RKQNILKEMAAET 1096
Cdd:pfam07888 196 ELRNSLAQRDTQV 208
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
709-853 |
9.32e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 709 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEAE-----ERSAQAALR 783
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEER-LVQKEEQLDARaekldNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 784 AEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELeqLCSSLEAKhreviSNLQKKIEGAQQKEEAQL 853
Cdd:PRK12705 111 EKALSARELELEELEKQLD-NELYRVAGLTPEQARKL--LLKLLDAE-----LEEEKAQRVKKIEEEADL 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-1050 |
9.55e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 608 RLCREEEEEEkeeeeeekeeeeeeekeeeeeeekeeegeeeekeekeeeeeeeeeeekeekeeehwLYQQKEKSLSLLKt 687
Cdd:TIGR02168 672 ILERRREIEE--------------------------------------------------------LEEKIEELEEKIA- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 688 qlqkaaeeeekeeetqireEESQRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASlEQKSRRALEQL 767
Cdd:TIGR02168 695 -------------------ELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLS 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 768 REQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGErreaVAGLEKKHSTELEQLcSSLEAKHREVISNLQKKIEGAQ- 846
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKALREAL-DELRAELTLLNEEAANLRERLEs 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 847 -QKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSlLRDKRQEVEREHERKmDKMKEEHWQEMAEARERYEAEERKQRAD 925
Cdd:TIGR02168 829 lERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEAL-LNERASLEEALALLRSELEELSEELREL 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 926 L--LGHLTGELERLRR---AHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENmrk 1000
Cdd:TIGR02168 907 EskRSELRRELEELREklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE--- 983
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 ekqllLDAQRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIDDL 1050
Cdd:TIGR02168 984 -----LGPVNLAAIEEYEELKERY--DFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-1095 |
1.10e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 640 EKEEEGEEEEKEEKEEEEEEEEEEEKEEKEEEHWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEESQRLACLRAQV 719
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 720 qSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKS--------------RRALEQLREQLEAEERSAQAALRAE 785
Cdd:TIGR02168 530 -SVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLV 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 786 KEAEK-----------------EATLLQLREQLEGE------------RREAVAGLEKKHSteleqlcSSLEAKHREvIS 836
Cdd:TIGR02168 609 KFDPKlrkalsyllggvlvvddLDNALELAKKLRPGyrivtldgdlvrPGGVITGGSAKTN-------SSILERRRE-IE 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 837 NLQKKIEGAQQKeEAQLQESLGRAEQrthqkvhQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEmaeARERYE 916
Cdd:TIGR02168 681 ELEEKIEELEEK-IAELEKALAELRK-------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE---QLEERI 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 917 AEERKQRADLLGHLTGELERLR--RAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSsrtkDVKARLAQLNVQ 994
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRER 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 995 EENMRKE----KQLLLDAQRQAALEKEEATA-------TRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRV-------E 1056
Cdd:TIGR02168 826 LESLERRiaatERRLEDLEEQIEELSEDIESlaaeieeLEELIEELESELEALLNERASLEEALALLRSELEelseelrE 905
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958798735 1057 LESQVDQLQTQSQRLQKHVSSLEAEVQR-KQNI--LKEMAAE 1095
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGlEVRIdnLQERLSE 947
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
931-1084 |
1.33e-04 |
|
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: 44.76 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 931 TGELERLRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQeenMRKEKQLLldaQR 1010
Cdd:pfam14988 49 TAELQTQLLQKEKEQASLKKEL-QALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDREAHLQ---FLKEKALL---EK 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798735 1011 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQR 1084
Cdd:pfam14988 122 QLQELRILELGERATRELKRKAQALKLAAKQALSEFCRSIKRENRQLQKELLQLIQETQALEAIKSKLENRKQR 195
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
728-1165 |
1.35e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 728 NQIRAEQQTALQRLRE--EAETLQKAERASLEQKSRRALEQLREQLEA-EERSAQAALRAEKEAEKEATLLQLREQLEGE 804
Cdd:COG5278 82 EEARAEIDELLAELRSltADNPEQQARLDELEALIDQWLAELEQVIALrRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 805 RREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRD 884
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 885 KRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHR 964
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 965 DQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLR 1044
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1045 RAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPPHPEPGLHIEDLRKSLGTNENQEVS 1124
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958798735 1125 SSLSLSKEGIDLSMDSVRHFLSAEGVAVRSAKEFLVRQTRS 1165
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
942-1096 |
1.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 942 ERELESVRQEQDQQLEDlrrrhrDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLlldaqrqaaLEKEEata 1021
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL---------LEKRE--- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 1022 trRHLEEAKKEHTHLLESKQQLRRAIDDLRvrrvelESQVDQLQtqsqrlqkHVSSLEAEvQRKQNILKEMAAET 1096
Cdd:PRK12704 110 --EELEKKEKELEQKQQELEKKEEELEELI------EEQLQELE--------RISGLTAE-EAKEILLEKVEEEA 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
861-1088 |
1.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 861 EQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHW----QEMAEARERYEAEERKQRADLLGHLTgELER 936
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELA-EAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 937 LRRAHERELESVRQE-----QDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKE-KQLLLDAQR 1010
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798735 1011 QAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRvelesqvDQLQTQSQRLQkhvsslEAEVQRKQNI 1088
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR-------ELYESLLQRLE------EARLAEALTV 385
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
934-1088 |
1.45e-04 |
|
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: 45.78 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 934 LERLRRAHERELESVRQEqDQQLedlrrrhRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRqAA 1013
Cdd:smart00787 142 LEGLKEGLDENLEGLKED-YKLL-------MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK-EK 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 1014 LEKEEatatrRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKH----VSSLEAEVQRKQNI 1088
Cdd:smart00787 213 LKKLL-----QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtfkeIEKLKEQLKLLQSL 286
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
938-1244 |
1.48e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 938 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDaQRQAALEKE 1017
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRD-EAIAAIDNE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1018 EATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKeMAAETN 1097
Cdd:PLN02939 115 QQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIK-LAAQEK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1098 AppHPE-PGLHIEDLRKSLGTNENQEVSSSLSLSKEGIDLSMDSVR-----HFLSAEGVAVRSAKEFLVRqtrsMRRRQT 1171
Cdd:PLN02939 194 I--HVEiLEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLlkddiQFLKAELIEVAETEERVFK----LEKERS 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 1172 ALKAAQQHWRHELASAQEVDEDLPGTKV------LENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEklnqLESSLLE 1244
Cdd:PLN02939 268 LLDASLRELESKFIVAQEDVSKLSPLQYdcwwekVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDK----LEASLKE 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
724-877 |
1.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 724 EAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaLEQLREQLEaeERSAQAALRAEKEAEKEATLLQLREQLEg 803
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLD--RKLELLEKREEELEKKEKELEQKQQELE- 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 804 ERREAVAGLEKKHSTELEQlcssleakhrevISNLqkkiegaqQKEEAQlQESLGRAEQRT-HQKVHQVIEYEQE 877
Cdd:PRK12704 128 KKEEELEELIEEQLQELER------------ISGL--------TAEEAK-EILLEKVEEEArHEAAVLIKEIEEE 181
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
845-1077 |
1.96e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 845 AQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER--EHERKMD---KMKEEHWQEMAEARERYEAEE 919
Cdd:PRK10929 20 ATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERakQYQQVIDnfpKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 920 RKQRADllghltgELE-RLRRAHERELESVR---QEQD-------------QQLEDLRRRHRDQERKLQDL--------E 974
Cdd:PRK10929 100 PNMSTD-------ALEqEILQVSSQLLEKSRqaqQEQDrareisdslsqlpQQQTEARRQLNEIERRLQTLgtpntplaQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 975 AELSSRTKDVKARLAQLNvqeenmrkekQLLLdAQRQAALEKEEAtatRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRR 1054
Cdd:PRK10929 173 AQLTALQAESAALKALVD----------ELEL-AQLSANNRQELA---RLRSELAKKRSQQLDAYLQALRNQLNSQRQRE 238
|
250 260
....*....|....*....|....*
gi 1958798735 1055 VE--LESqVDQLQTQSQRLQKHVSS 1077
Cdd:PRK10929 239 AEraLES-TELLAEQSGDLPKSIVA 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
761-1091 |
2.23e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 761 RRALEQLREQLEAE-----ERSAQAALRAEK--------------------EAEKEATLLQLREQLeGERREAVAGLEKK 815
Cdd:PRK04863 781 RAAREKRIEQLRAEreelaERYATLSFDVQKlqrlhqafsrfigshlavafEADPEAELRQLNRRR-VELERALADHESQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 816 HSTELEQLcssleAKHREVISNLQKKI-------EGAQQKEEAQLQESLGRAEQ-----RTHQKvhQVIEYEQELSSLlr 883
Cdd:PRK04863 860 EQQQRSQL-----EQAKEGLSALNRLLprlnllaDETLADRVEEIREQLDEAEEakrfvQQHGN--ALAQLEPIVSVL-- 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 884 dkrqeveREHERKMDKMKEEHWQemaearERYEAEERKQRADLLGHLtgeleRLRRAHERELESVR-QEQDQQL-EDLRR 961
Cdd:PRK04863 931 -------QSDPEQFEQLKQDYQQ------AQQTQRDAKQQAFALTEV-----VQRRAHFSYEDAAEmLAKNSDLnEKLRQ 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 962 RHRDQERKLQDLEAELssrtKDVKARLAQLNvqeenmrkekqllldaQRQAALeKEEATATRRHLEEAKKEHTHLleSKQ 1041
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYN----------------QVLASL-KSSYDAKRQMLQELKQELQDL--GVP 1049
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1042 QLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKE 1091
Cdd:PRK04863 1050 ADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
942-1255 |
2.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 942 ERELESVRQEQDQQLEDLRRRhrdqerkLQDLEAELSS----------RTKDVKARLAQLNVQEENMRKEKQLLldaQRQ 1011
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRER-------LEGLKRELSSlqselrrienRLDELSQELSDASRKIGEIEKEIEQL---EQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1012 AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQL-----QTQSQRLQKHVSSLEAEVQRKQ 1086
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1087 NILKEMAAETNApphpepglhiEDLRKSLGTNENQEVSSSLSLSKEGIDlsmdsvrhflsaegvavrsakeflvrqtrSM 1166
Cdd:TIGR02169 812 ARLREIEQKLNR----------LTLEKEYLEKEIQELQEQRIDLKEQIK-----------------------------SI 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1167 RRRQTALKAAQQHWRHELASAQEVDEDLpgTKVLENVRKNLDEETKHLDEMKSAMRKGHDLLKKKEEKLNQLE---SSLL 1243
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDL--ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklEALE 930
|
330
....*....|..
gi 1958798735 1244 EEVSDEDTLKGS 1255
Cdd:TIGR02169 931 EELSEIEDPKGE 942
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
57-87 |
2.31e-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: 2.31e-04
10 20 30
....*....|....*....|....*....|.
gi 1958798735 57 PLPKGWKPCQNITGDLYYFNFDTGQSIWDHP 87
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
718-1095 |
2.34e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 718 QVQSSTEAFENQiraEQQTALQRLREEAETLQKAERASLEQ--KSRRALEQLREQLEAEERSAQaalraekeaEKEATLL 795
Cdd:TIGR04523 292 QLKSEISDLNNQ---KEQDWNKELKSELKNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELT---------NSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 796 QLREQLEgERREAVAGLEKKHSTELEQLcSSLEAKhrevISNLQKKIEgAQQKEEAQLQESLgraeqRTHQKVHQVIEYE 875
Cdd:TIGR04523 360 EKQRELE-EKQNEIEKLKKENQSYKQEI-KNLESQ----INDLESKIQ-NQEKLNQQKDEQI-----KKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 876 QE-LSSLLRDKRQEVEREHERKMDKMKEEhwqemaeareryeaeerkqradllghltgelerlrraheRELESVRQEQDQ 954
Cdd:TIGR04523 428 IErLKETIIKNNSEIKDLTNQDSVKELII---------------------------------------KNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 955 QLEDLRRRHRDQERKLQDLEAELSSRTKDVKA---RLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKK 1031
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798735 1032 EhthlleskqqlrraiDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAE 1095
Cdd:TIGR04523 549 K---------------DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
924-1118 |
3.79e-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: 44.36 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 924 ADLLGHLTGELERLRRAHERELESVRQEQDQQ---LEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLnvqEENMRK 1000
Cdd:pfam09787 28 ASLKEGSGVEGLDSSTALTLELEELRQERDLLreeIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQEL---EEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDAQRQAALEKEEataTRRHLEEAKKEHTHLLESKQQLRRAIDDLRVR----------RVELESQVDQL------ 1064
Cdd:pfam09787 105 ERSARREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQltsksqssssQSELENRLHQLtetliq 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 1065 -QTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNapphPEPGLHIEDLRKSLGTN 1118
Cdd:pfam09787 182 kQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS----NGTSINMEGISDGEGTR 232
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
727-861 |
4.07e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 727 ENQIRAE---QQTALQRLREEAETLQKAERASL---EQKSRRALEQLREQLEAEERSAQAAlrAEKEAEKEATLLQLREQ 800
Cdd:COG2268 205 EAEAEREteiAIAQANREAEEAELEQEREIETAriaEAEAELAKKKAEERREAETARAEAE--AAYEIAEANAEREVQRQ 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798735 801 LEGERREAVAGLEKKhstELEQLCSSLEAKHREVISNLQKKIEgAQQKEEAQLQESLGRAE 861
Cdd:COG2268 283 LEIAEREREIELQEK---EAEREEAELEADVRKPAEAEKQAAE-AEAEAEAEAIRAKGLAE 339
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
724-819 |
4.10e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 724 EAFENQIRAEQQTALQRLREEAETLQKAERASLE-----QKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLR 798
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREVQRQLEIAEREreielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK 335
|
90 100
....*....|....*....|.
gi 1958798735 799 EQLEGERREAVAGLEKKHSTE 819
Cdd:COG2268 336 GLAEAEGKRALAEAWNKLGDA 356
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
931-1258 |
5.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 931 TGELERLRRAHERELESVRQEqdqqLEDLRRRHRDQERKLQDLEAELSsRTKDVKARLAQLNVQEENMRKEKQLLLDAQR 1010
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1011 Q-----AALEK-----EEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSSLE- 1079
Cdd:PRK03918 263 EleeriEELKKeieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEe 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1080 -----AEVQRKQNILKE--------MAAETNAPPHPEP--GLHIEDLRKSLGTNEN--QEVSSSL--------SLSKEGI 1134
Cdd:PRK03918 343 lkkklKELEKRLEELEErhelyeeaKAKKEELERLKKRltGLTPEKLEKELEELEKakEEIEEEIskitarigELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1135 DLsMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTA-LKAAqqhwRHELASAQEVDEDLpgTKVLENVRKNLDEETKH 1213
Cdd:PRK03918 423 EL-KKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRI----EKELKEIEEKERKL--RKELRELEKVLKKESEL 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958798735 1214 LdemksAMRKGHDLLKKKEEKLNQLESSLLEEVSDE-DTLKGSSIK 1258
Cdd:PRK03918 496 I-----KLKELAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIK 536
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
739-871 |
5.55e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 739 QRLREEAETLQKAERASLEQK-SRRALEQLREQLEAE----ERSAQAALRAEKE------AEKEATLLQLREQLEgerre 807
Cdd:COG1842 30 QAIRDMEEDLVEARQALAQVIaNQKRLERQLEELEAEaekwEEKARLALEKGREdlareaLERKAELEAQAEALE----- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 808 avaglekkhsTELEQLcSSLEAKHREVISNLQKKIEGA-QQKEEAQLQESLGRAEQRTHQKVHQV 871
Cdd:COG1842 105 ----------AQLAQL-EEQVEKLKEALRQLESKLEELkAKKDTLKARAKAAKAQEKVNEALSGI 158
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
710-977 |
6.47e-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: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTEAFEnQIRaEQQTALQRLREEAETLqkaERASLEQKsrraLEQLREQLEAEERSAQAALRAEKEAE 789
Cdd:COG3096 850 RELAQHRAQEQQLRQQLD-QLK-EQLQLLNKLLPQANLL---ADETLADR----LEELREELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 790 KEATLLQ-LREQLEGERREAVAGLEKKHS-TELEQLCSSLEakhrEVISNLQ--KKIEGAQQKEEA-----QLQESLGRA 860
Cdd:COG3096 921 QLEPLVAvLQSDPEQFEQLQADYLQAKEQqRRLKQQIFALS----EVVQRRPhfSYEDAVGLLGENsdlneKLRARLEQA 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 861 EQ-------RTHQKVHQVIEYEQELSSLL--RDKRQEVEREHERKMdkmkeehwQEMAEARERYEAEERKQRADllgHLT 931
Cdd:COG3096 997 EEarreareQLRQAQAQYSQYNQVLASLKssRDAKQQTLQELEQEL--------EELGVQADAEAEERARIRRD---ELH 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958798735 932 GELERLRrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAEL 977
Cdd:COG3096 1066 EELSQNR-SRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
745-1029 |
6.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 745 AETLQKAERASLEQKSRRALEQLREQLEAEERSAQAAlraekeaekEATLLQLREQlegerrEAVAGLEKKHSTELEQLc 824
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEA---------EAALEEFRQK------NGLVDLSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 825 SSLEAKhrevISNLQKKIEGAQQKEEaQLQESLGRAEQRTHQKVhqvieyEQELSSLLRDKRQEVEREHERKMDKMKEEH 904
Cdd:COG3206 222 SELESQ----LAEARAELAEAEARLA-ALRAQLGSGPDALPELL------QSPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 905 wQEMAEareryeaeerkqradllghLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELsSRTKDV 984
Cdd:COG3206 291 -PDVIA-------------------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPEL 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958798735 985 KARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEA 1029
Cdd:COG3206 350 EAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
938-1095 |
7.51e-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: 44.27 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 938 RRAHERELESVRQEQDQQLEDLRRRhrDQERK-LQDLEAELSSRTKDVKARlaqlnvQEENMRKEKQLLLDAQRQAAL-- 1014
Cdd:pfam10168 556 REEIQKRVKLLKLQKEQQLQELQSL--EEERKsLSERAEKLAEKYEEIKDK------QEKLMRRCKKVLQRLNSQLPVls 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1015 --EKEEatatrrhleeaKKEHTHLLESKQQLRRAIDDLRVRrveLESQVDQLQTQSQRLQKHVSSLEAEvQRK--QNILK 1090
Cdd:pfam10168 628 daEREM-----------KKELETINEQLKHLANAIKQAKKK---MNYQRYQIAKSQSIRKKSSLSLSEK-QRKtiKEILK 692
|
....*
gi 1958798735 1091 EMAAE 1095
Cdd:pfam10168 693 QLGSE 697
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
728-1094 |
8.02e-04 |
|
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: 43.37 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 728 NQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEaeersaqaalraEKEAEKEATLLQLREQLEGERRE 807
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEE------------ERKEERKRYRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 808 AVAGLEKKhsteleqlcssleAKHREVISNLQKKIegaqQKEEAQLQESLGRAEQRTHQKVHQVIEyeqelsslLRDKRQ 887
Cdd:pfam13868 89 RQEEYEEK-------------LQEREQMDEIVERI----QEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 888 EVEREHERKMDKMKEEHWQEMAEARERYeaeerkqradllghltgELERLRRAHERELESVRQEQDQQLEDLRRRHRDQe 967
Cdd:pfam13868 144 ELEKEEEREEDERILEYLKEKAEREEER-----------------EAEREEIEEEKEREIARLRAQQEKAQDEKAERDE- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 968 rklqdleaelssrtkdvkarLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKehtHLLESKQQLRRAI 1047
Cdd:pfam13868 206 --------------------LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKE---RRLAEEAEREEEE 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958798735 1048 DDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAA 1094
Cdd:pfam13868 263 FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAE 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
998-1254 |
8.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 998 MRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVSS 1077
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1078 LEAEVQRKQNILKEMAAETNApphpepglHIEDLRKSLGTNENQEVSSSLSLSkegidLSMDSVRHFLSAeGVAVRSAKE 1157
Cdd:COG4942 81 LEAELAELEKEIAELRAELEA--------QKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRR-LQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1158 FLVRQTRSMRRRQTALKAAQQhwrhELASAQevdedlpgtKVLENVRKNLDEETKHLDEMKSAMRKghdLLKKKEEKLNQ 1237
Cdd:COG4942 147 ARREQAEELRADLAELAALRA----ELEAER---------AELEALLAELEEERAALEALKAERQK---LLARLEKELAE 210
|
250
....*....|....*..
gi 1958798735 1238 LESSLLEEVSDEDTLKG 1254
Cdd:COG4942 211 LAAELAELQQEAEELEA 227
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
710-1070 |
8.88e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTE---AFENQIRAEQQTALQRL----REEAETLQKAERASLEqksrRALEQLREQLEAEERSAQAA- 781
Cdd:NF041483 134 QELAERRQTVESHVNenvAWAEQLRARTESQARRLldesRAEAEQALAAARAEAE----RLAEEARQRLGSEAESARAEa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 782 ----LRAEKEAEK----------EAT--LLQLREQLEGERREAvagleKKHSTEL----EQLCSSLEAKHREVISNLQKK 841
Cdd:NF041483 210 eailRRARKDAERllnaastqaqEATdhAEQLRSSTAAESDQA-----RRQAAELsraaEQRMQEAEEALREARAEAEKV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 842 IEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER-------EHERKMDKMKEEHWQEMAEARER 914
Cdd:NF041483 285 VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQaladaraEAEKLVAEAAEKARTVAAEDTAA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 915 YEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQErklQDLEAELSSRTKDVKARLAQLNVQ 994
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQA---EQLKGAAKDDTKEYRAKTVELQEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 995 EENMRKEKQLLL------------DAQRQAALEKEEATATRRHL----------------EEAKKEHTHLLESKQQLRRA 1046
Cdd:NF041483 442 ARRLRGEAEQLRaeavaegerirgEARREAVQQIEEAARTAEELltkakadadelrstatAESERVRTEAIERATTLRRQ 521
|
410 420 430
....*....|....*....|....*....|..
gi 1958798735 1047 IDDLRVR--------RVELESQVDQLQTQSQR 1070
Cdd:NF041483 522 AEETLERtraeaerlRAEAEEQAEEVRAAAER 553
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
982-1082 |
1.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 982 KDVKARLAQLNVQEENMRKEKQLLlDAQRQAALEKEEATATRRH--LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELES 1059
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEA-SFERLAELRDELAELEEELeaLKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|...
gi 1958798735 1060 QVDQLQtqsQRLQKHVSSLEAEV 1082
Cdd:COG0542 493 ELAELE---EELAELAPLLREEV 512
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
732-1011 |
1.08e-03 |
|
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: 43.66 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 732 AEQQTALQRLREEAETLQKAERASLEQkSRRALEQLREQLEAeersaqaaLRAEKeAEKEATLLQLREQLEGERREAVAG 811
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELES-LKKENKDLKEKVSA--------LQPEL-TEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 812 LEKKHSTELE-----QLCSSLEAKHREV----------------ISNLQKKIE------GAQQKEEAQLQESLGRAEQRT 864
Cdd:pfam10174 516 DSKLKSLEIAveqkkEECSKLENQLKKAhnaeeavrtnpeindrIRLLEQEVArykeesGKAQAEVERLLGILREVENEK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 865 HQKVHQVIEYEQELSSLLRDKRQEVeREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRR---AH 941
Cdd:pfam10174 596 NDKDKKIAELESLTLRQMKEQNKKV-ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQeldAT 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 942 ERELESVRQ---EQDQQLEDLRRRHRDQ-----ERKLQDLEAELSSrtKDVKARLAQLN------VQEENM--RKEKQLL 1005
Cdd:pfam10174 675 KARLSSTQQslaEKDGHLTNLRAERRKQleeilEMKQEALLAAISE--KDANIALLELSsskkkkTQEEVMalKREKDRL 752
|
....*.
gi 1958798735 1006 LDAQRQ 1011
Cdd:pfam10174 753 VHQLKQ 758
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
722-843 |
1.17e-03 |
|
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: 42.56 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 722 STEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRA-LEQLREQLEAEERSAQAALRaekeaekeatllQLREQ 800
Cdd:cd16269 178 SKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEqQRELEQKLEDQERSYEEHLR------------QLKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958798735 801 LEGERREAVAGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE 843
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
929-1063 |
1.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 929 HLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER--------KLQDLEAELSSRTKDVKARLAQLNVQEENMRK 1000
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRqearrereELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDA-------QRQAALEKEEATATRRhlEEAKKEHTHLLESKQQLRRAIddlRVRRVELESQVDQ 1063
Cdd:PRK12705 110 REKALSAReleleelEKQLDNELYRVAGLTP--EQARKLLLKLLDAELEEEKAQ---RVKKIEEEADLEA 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
906-1051 |
1.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 906 QEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQER---KLQDLEAELSSRTK 982
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 983 DVKARLAQLNVQEENMRKEkqllldAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLR 1051
Cdd:PRK12705 113 ALSARELELEELEKQLDNE------LYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
742-815 |
1.91e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.53 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 742 REE--AETLQKAERASLEQKsrRALEQLREQL------------EAEERSAQ--AALRAEKEAEKEATLLQLREQLEGER 805
Cdd:PRK05759 36 RQKkiADGLAAAERAKKELE--LAQAKYEAQLaearaeaaeiieQAKKRAAQiiEEAKAEAEAEAARIKAQAQAEIEQER 113
|
90
....*....|
gi 1958798735 806 REAVAGLEKK 815
Cdd:PRK05759 114 KRAREELRKQ 123
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
841-1085 |
2.06e-03 |
|
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: 42.33 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 841 KIEGAQQKEEAQLQESLGRAEQR-THQKVHQVIEYEQELssLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEE 919
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRrRDQKRQETLERERRL--LLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 920 RKQRADLLGHLTGELERLRRAHERElESVRQEQDQQL---EDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEE 996
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEA-EQRKQCQEQRLkekEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQEN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 997 NMRKE-----KQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRaiddlRVRRVELESQVDQLQT--QSQ 1069
Cdd:pfam15558 173 NLSELlnhqaRKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELRE-----KAQKEEEQFQRAKWRAeeKEE 247
|
250
....*....|....*.
gi 1958798735 1070 RLQKHVSSLEAEVQRK 1085
Cdd:pfam15558 248 ERQEHKEALAELADRK 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
718-855 |
2.09e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 718 QVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERasLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQL 797
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ--LEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 798 REQLEGERREAVAGL----EKKHSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQE 855
Cdd:PRK09510 148 KAEAEAKRAAAAAKKaaaeAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
661-903 |
2.69e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 661 EEEEKEEKEEEHWLYQQKEKSLSLLKTQLQKAAEEEEKEEETQIREEES-QRLACLRAQVQSSTEAFENQIRAEQQTALQ 739
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAlEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 740 RLREEAETLQKAERASLEQKSR-----RALEQLREQLEAEERSAQAALRAEKEaEKEATLLQLREQLEGERREAVAGLEK 814
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERleeeiTKEELLQELLLKEEELEEQKLKDELE-SKEEKEKEEKKELEEESQKLNLLEEK 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 815 khsTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHE 894
Cdd:pfam02463 916 ---ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
....*....
gi 1958798735 895 RKMDKMKEE 903
Cdd:pfam02463 993 DELEKERLE 1001
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
727-814 |
2.82e-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: 39.34 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 727 ENQIRAEQQTAlQRLREEAETLQKAERASLEQKSRRALEQLRE-QLEAEERSAQAALRAEKEAEKEatLLQLREQLEGER 805
Cdd:cd06503 32 EEKIAESLEEA-EKAKEEAEELLAEYEEKLAEARAEAQEIIEEaRKEAEKIKEEILAEAKEEAERI--LEQAKAEIEQEK 108
|
....*....
gi 1958798735 806 REAVAGLEK 814
Cdd:cd06503 109 EKALAELRK 117
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1095 |
2.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 862 QRTHQKVHQVI----------EYEQELSsLLRDKRQEVEREHERkmdkmkeehwQEMAEARERYEAEERKQRADLLGHLT 931
Cdd:PRK04863 813 QRLHQAFSRFIgshlavafeaDPEAELR-QLNRRRVELERALAD----------HESQEQQQRSQLEQAKEGLSALNRLL 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 932 GELERLRR-AHERELESVRQEQDQQLEDLR--RRHRDQERKLQDLEAELSSRTKD---VKARLAQLNVQEENMRKEKQLL 1005
Cdd:PRK04863 882 PRLNLLADeTLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFAL 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1006 LD-AQRQAALEKEEAtatrrhlEEAKKEHTHLLES-KQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQkhvsSLEAEVQ 1083
Cdd:PRK04863 962 TEvVQRRAHFSYEDA-------AEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLA----SLKSSYD 1030
|
250
....*....|..
gi 1958798735 1084 RKQNILKEMAAE 1095
Cdd:PRK04863 1031 AKRQMLQELKQE 1042
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
320-574 |
3.18e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 320 PKASSSPAAPGLDPggdqPNRVSKKEQEEDPVEAEEEASREDSAAKEPKEPSALEES--ASDASEESGIHEHLKDPQHSE 397
Cdd:PHA03307 117 PPPTPPPASPPPSP----APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSrqAALPLSSPEETARAPSSPPAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 398 SGTSGPKSFLRLDIGLRGRVSEHLLDGNMPSPA-----------LGGGHWEAQGLGQEEQDDSRSSRSEPQSKHTQVSER 466
Cdd:PHA03307 193 PPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaaddagassSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 467 EQP--RSTLHSQATEEGPLRTLEGQPEgqPGKDSVASPAPLSFLQREQVLSPPAFPERAEEKHSQAEELGLGQQEAEETE 544
Cdd:PHA03307 273 SGWngPSSRPGPASSSSSPRERSPSPS--PSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS 350
|
250 260 270
....*....|....*....|....*....|
gi 1958798735 545 EKVEVSPSSPVSPEVQTAEPAAPQKQFSEA 574
Cdd:PHA03307 351 PSPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
709-983 |
3.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 709 SQRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQleaEERSAQAALRAEKEA 788
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKM 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 789 EKEatllqlREQLEGERREAVAGLEKKHSTELEQLCSSleaKHREVISNLQKKIEGAQQKEEAQLQESLGRAE-QRTHQK 867
Cdd:TIGR00618 686 QSE------KEQLTYWKEMLAQCQTLLRELETHIEEYD---REFNEIENASSSLGSDLAAREDALNQSLKELMhQARTVL 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 868 VHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHE----- 942
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsr 836
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958798735 943 -RELESVRQEQDQQLEDLRRRHRDQERKLQDlEAELSSRTKD 983
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQE-QAKIIQLSDK 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
677-1029 |
3.41e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 677 QKEKSLSLLKTQLqkaaeeeekeeetqireeesqrlaclrAQVQSSTEafENQIRAEQ-QTALQRLrEEAETLQKAERAS 755
Cdd:COG3096 386 AAEEEVDSLKSQL---------------------------ADYQQALD--VQQTRAIQyQQAVQAL-EKARALCGLPDLT 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 756 LEQKSRRaLEQLREQLEA---EERSAQAALRAEKEAEKE-ATLLQLREQLEGE--RREAvaglekkHSTELEQLCSSLEA 829
Cdd:COG3096 436 PENAEDY-LAAFRAKEQQateEVLELEQKLSVADAARRQfEKAYELVCKIAGEveRSQA-------WQTARELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 830 KHRevisnlqkkiegAQQkeEAQLQESLGRAEQRTHQKvHQVIEYEQELSsllrdKRQEVEREHERKMDKMKEEHWQema 909
Cdd:COG3096 508 QAL------------AQR--LQQLRAQLAELEQRLRQQ-QNAERLLEEFC-----QRIGQQLDAAEELEELLAELEA--- 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 910 eareryeaeerkQRADLLGHLTGELERlRRAHERELESVRQEQdQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLA 989
Cdd:COG3096 565 ------------QLEELEEQAAEAVEQ-RSELRQQLEQLRARI-KELAARAPAWLAAQDALERLREQSGEALADSQEVTA 630
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958798735 990 QLnvqeenmrkekQLLLDAQRQAALEKEEATATRRHLEEA 1029
Cdd:COG3096 631 AM-----------QQLLEREREATVERDELAARKQALESQ 659
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
715-855 |
3.75e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.78 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 715 LRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRaleqLREQLEAEERSAQAALRAEKEAEKEATL 794
Cdd:PRK00106 58 IKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESR----LTERATSLDRKDENLSSKEKTLESKEQS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798735 795 LQLREQLEGERREAVAGLEKKHSTELEQLCSSLEAKHREVI-----SNLQKKIEGAQQKEEAQLQE 855
Cdd:PRK00106 134 LTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIIlaeteNKLTHEIATRIREAEREVKD 199
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
933-1028 |
4.09e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQA 1012
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*.
gi 1958798735 1013 ALEKEEATATRRHLEE 1028
Cdd:COG0542 495 AELEEELAELAPLLRE 510
|
|
| 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 ... |
729-800 |
4.39e-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: 38.83 E-value: 4.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 729 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQ 800
Cdd:pfam00430 51 AALAEAEQQLKEARAEAQEI----IENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQ 118
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
926-1091 |
5.09e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 926 LLGHLTGELErlrrAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEKQLL 1005
Cdd:PHA02562 189 KIDHIQQQIK----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1006 LDAQRQAALEKEEATATRRH---------LEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVDQLQTQSQRLQKHVS 1076
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKN 344
|
170
....*....|....*
gi 1958798735 1077 SLEAEVQRKQNILKE 1091
Cdd:PHA02562 345 KISTNKQSLITLVDK 359
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
921-1092 |
5.13e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 921 KQRADLLGHLtgelerlrraherelesvrQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTkdvkARLAQLNVQeenmRK 1000
Cdd:PRK11637 68 QQRASLLAQL-------------------KKQEEAISQASRKLRETQNTLNQLNKQIDELN----ASIAKLEQQ----QA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1001 EKQLLLDAQRQAALEKEEATATRRHL--EEAKKEH------THLLESKQQlrrAIDDLRVRRVELESQVDQL---QTQSQ 1069
Cdd:PRK11637 121 AQERLLAAQLDAAFRQGEHTGLQLILsgEESQRGErilayfGYLNQARQE---TIAELKQTREELAAQKAELeekQSQQK 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958798735 1070 RL------------------QKHVSSLEAEVQRKQNILKEM 1092
Cdd:PRK11637 198 TLlyeqqaqqqkleqarnerKKTLTGLESSLQKDQQQLSEL 238
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
826-991 |
5.20e-03 |
|
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: 40.90 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 826 SLEAKHREVISNLQKKIEGAQQKEE--AQLQES---------------LGRAEQRTHQKVHQVIEYEQELSSLlRDKRQE 888
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKliASLKEGsgvegldsstaltleLEELRQERDLLREEIQKLRGQIQQL-RTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 889 VEREHERKMDKMKEehwqemaeareryeaeerkQRADLLGHLTGElERLRRAHERELESVRQEQDQQLEDLRR------- 961
Cdd:pfam09787 80 LEAQQQEEAESSRE-------------------QLQELEEQLATE-RSARREAEAELERLQEELRYLEEELRRskatlqs 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958798735 962 RHRDQERKLQDLEAELSSRT------KDVKARLAQL 991
Cdd:pfam09787 140 RIKDREAEIEKLRNQLTSKSqssssqSELENRLHQL 175
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
710-793 |
5.34e-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: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTEAFENQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLeaeerSAQAALRAEKEAE 789
Cdd:COG0711 59 EKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV-----ADLAVAIAEKILG 133
|
....
gi 1958798735 790 KEAT 793
Cdd:COG0711 134 KELD 137
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
736-836 |
5.36e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 736 TALQRLREEAETLqKAERASLEQKSRRALEQLREQLEAEERSAQ---AALRAEKEAEKEAT--LLQLREQLEgERREAVA 810
Cdd:COG0542 411 EELDELERRLEQL-EIEKEALKKEQDEASFERLAELRDELAELEeelEALKARWEAEKELIeeIQELKEELE-QRYGKIP 488
|
90 100
....*....|....*....|....*.
gi 1958798735 811 GLEKKHsTELEQLCSSLEAKHREVIS 836
Cdd:COG0542 489 ELEKEL-AELEEELAELAPLLREEVT 513
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
728-1016 |
5.38e-03 |
|
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: 40.79 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 728 NQIRAEQQTALQRLREEAETLQKAERASLEQKSR------------RALEQLREQ-----LEAEERSAQAALRAEKEAEK 790
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLERARQEAEQRkqcqeqrlkekeEELQALREQnslqlQERLEEACHKRQLKEREEQK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 791 EATLLQLREQLEGERREAvaGLEKKHSTELEQLCSSLEAKHREVISNLQKKIE-------GAQQKEEAQLQESLGRAEQR 863
Cdd:pfam15558 168 KVQENNLSELLNHQARKV--LVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEerhrelrEKAQKEEEQFQRAKWRAEEK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 864 THQ-KVHQvieyeqELSSLLRDKRQEVEREHERKMDKMKEEHWQEmaeareryeAEERKQRADLLghLTGELERLRRAHE 942
Cdd:pfam15558 246 EEErQEHK------EALAELADRKIQQARQVAHKTVQDKAQRARE---------LNLEREKNHHI--LKLKVEKEEKCHR 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798735 943 RELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKarlaqlnvQEENMRKEKQLLLDAQRQAALEK 1016
Cdd:pfam15558 309 EGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVR--------EETNNRTFDKMALEAQLHASLQR 374
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
752-1060 |
5.62e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 752 ERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEatllqlreqlegERREAVAGLEKKHSTELEQLCSSLEAK- 830
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNS------------YEEDSELKPSGQGGLDEEEAFLDRTAKr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 831 HREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVErEHERKMDKMKEEHWQEMAE 910
Cdd:pfam02029 72 EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 911 ARERYEAEERKQRADLlghlTGELERLRRAHERELESVRQEQDQQLED---LRRRHRDQERKLQDLEAELSSRTKDVKAR 987
Cdd:pfam02029 151 QAEEEGEEEEDKSEEA----EEVPTENFAKEEVKDEKIKKEKKVKYESkvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 988 LAQLNV-----QEENMRKEKQLLLDAQRQ--AALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1060
Cdd:pfam02029 227 QGGLSQsqereEEAEVFLEAEQKLEELRRrrQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE 306
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
729-842 |
5.66e-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: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 729 QIRAEQQTALQRLREEAETLqkaeRASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLegeRREA 808
Cdd:COG0711 52 AALAEYEEKLAEARAEAAEI----IAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV---ADLA 124
|
90 100 110
....*....|....*....|....*....|....
gi 1958798735 809 VAGLEKKHSTELEqlcsslEAKHREVISNLQKKI 842
Cdd:COG0711 125 VAIAEKILGKELD------AAAQAALVDRFIAEL 152
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
738-891 |
5.90e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 738 LQRLREEAE-TLQKAERASLEqksrraleqLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREavagLEKKH 816
Cdd:PRK00106 26 MKSAKEAAElTLLNAEQEAVN---------LRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREE----IEQEF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798735 817 STELEQLcSSLEAKHREVISNLQKKIEGAQQKEEAqlqesLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVER 891
Cdd:PRK00106 93 KSERQEL-KQIESRLTERATSLDRKDENLSSKEKT-----LESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
674-967 |
6.02e-03 |
|
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: 41.10 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 674 LYQQKEKslsllktqlqkaaeeeekeeetqireeeSQRLACLRAQVQSSTEAFENQIRA--EQQTALQRLREEAETLQKA 751
Cdd:COG5185 270 LGENAES----------------------------SKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 752 E-RASLEQKSRR---ALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKKhSTELEQLCSSL 827
Cdd:COG5185 322 EaEQELEESKREtetGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST-KESLDEIPQNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 828 EAKHREVISNLQKKIeGAQQKEEAQLQeslgRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQE 907
Cdd:COG5185 401 RGYAQEILATLEDTL-KAADRQIEELQ----RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 908 mAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQE 967
Cdd:COG5185 476 -VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
710-851 |
6.31e-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: 39.91 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 710 QRLACLRAQVQSSTEAFEnQIRAEQQTALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEErsaqaalRAEKEAE 789
Cdd:COG1579 38 DELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLK-------RRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 790 KEatLLQLREQLEgERREAVAGLEKKHStELEQLCSSLEAKHREVISNLQKKIEGAQQKEEA 851
Cdd:COG1579 110 DE--ILELMERIE-ELEEELAELEAELA-ELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
948-1062 |
6.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 948 VRQEQDQQLEDLRrrhrDQERKLQDLEAELSSRTKD----VKARLAQLNVQEENMRKEKQLLLDAQRQaalEKEEATATR 1023
Cdd:COG0542 402 VRMEIDSKPEELD----ELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARWEA---EKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958798735 1024 RHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1062
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
938-1086 |
7.64e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 938 RRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSRTKDVKARlAQLNVQEENMRKEKQLLLDAQRQaalEKE 1017
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAE-AAYEIAEANAEREVQRQLEIAER---ERE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798735 1018 EAtatrrhLEEAKKEhthllESKQQLRRAIddlrVRRVELESQVDQLQTQsqrlqkhvssLEAEVQRKQ 1086
Cdd:COG2268 292 IE------LQEKEAE-----REEAELEADV----RKPAEAEKQAAEAEAE----------AEAEAIRAK 335
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
671-1097 |
7.67e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 671 EHWLYQQKEKSlsllktqlqkAAEEEEKEEETQIREEESQRLACLRAQVQSSTEAFEnQIRAEQQTALQ----RLREEAE 746
Cdd:pfam05483 154 RHLCNLLKETC----------ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRVQAENARLemhfKLKEDHE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 747 TLQKaerasLEQKSRRaleqlreqlEAEERSAQAALRAEKEAEKEATLLQLREQLEgERREAVAGLEKKHSTELEQLCSS 826
Cdd:pfam05483 223 KIQH-----LEEEYKK---------EINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQDENLKEL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 827 LEAKH------REVISNLQKKIEgAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQ-----------------ELSSLLR 883
Cdd:pfam05483 288 IEKKDhltkelEDIKMSLQRSMS-TQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcSLEELLR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 884 DKRQEVER-EHERKMDKM----KEEHWQEMAEARERYEAEERKqradlLGHLTGELERLRRaHERELESVRQEQDQQLED 958
Cdd:pfam05483 367 TEQQRLEKnEDQLKIITMelqkKSSELEEMTKFKNNKEVELEE-----LKKILAEDEKLLD-EKKQFEKIAEELKGKEQE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 959 LRRRHRDQERKLQDLEAELSSRTKDVKARLAQLNVQEENMRKEK-----------QLLLDAQR----------QAALEKE 1017
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknieltahcdKLLLENKEltqeasdmtlELKKHQE 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1018 EATATRRHLEEAKKEHTHLLESKQQLRraiDDLRVRRVELESQVDQLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETN 1097
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
933-1060 |
7.75e-03 |
|
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: 38.53 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 933 ELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEAELSSR--------------TKDVKARLAQLNVQEENM 998
Cdd:pfam07321 3 RLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEeqrlyaeiqgklvlLKELEKVKQQVALLRENE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798735 999 RKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQ 1060
Cdd:pfam07321 83 ADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELE 144
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
955-1100 |
9.20e-03 |
|
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: 39.12 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 955 QLEDLRRRHRDQERKLQDLEAE---LSSRTKDVKARLAQLNVQEENMRKEKQLLLDAqrqaaleKEEATATRRHLEEAKK 1031
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQEnkrLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-------KARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1032 EHTHLLESKQQLRRAIDDLRVRRVELESQVDQ-LQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPP 1100
Cdd:pfam13851 107 EHEVLEQRFEKVERERDELYDKFEAAIQDVQQkTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLDP 176
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
736-1071 |
9.24e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 40.56 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 736 TALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEATLLQLREQLEGERREAVAGLEKK 815
Cdd:COG2203 342 IAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 816 HSTELEQLCSSLEAKHREVISNLQKKIEGAQQKEEAQLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHER 895
Cdd:COG2203 422 LLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALS 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 896 KMDKMKEEHWQEMAEARERYEAEERKQRADLLGHLTGELERLRRAHERELESVRQEQDQQLEDLRRRHRDQERKLQDLEA 975
Cdd:COG2203 502 ALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELAL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 976 ELSSRTKDVKARLAQLNVQEENMRKEKQLLLDAQRQAALEKEEATATRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRV 1055
Cdd:COG2203 582 ALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLA 661
|
330
....*....|....*.
gi 1958798735 1056 ELESQVDQLQTQSQRL 1071
Cdd:COG2203 662 TELDLILDSSLLLGLL 677
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
709-1031 |
9.45e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 709 SQRLACLRAQVQSSTE---------------AFENQIRAEQQtALQRLREEAETLQKAERASlEQKSRRALEQLREQLEA 773
Cdd:COG3096 798 AEQYAKASFDVQKLQRlhqafsqfvgghlavAFAPDPEAELA-ALRQRRSELERELAQHRAQ-EQQLRQQLDQLKEQLQL 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 774 EER-SAQAALRAEKEAekEATLLQLREQLEgERREAVAGLEK--KHSTELEQLCSSLE---AKHREV---ISNLQKKIEG 844
Cdd:COG3096 876 LNKlLPQANLLADETL--ADRLEELREELD-AAQEAQAFIQQhgKALAQLEPLVAVLQsdpEQFEQLqadYLQAKEQQRR 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 845 AQQKEEAqLQESLGRAEQRTHQKVHQVIEYEQELSSLLRDKRQEVEREHERKMDKMKEehwqemaeaRERYEAEERKQRA 924
Cdd:COG3096 953 LKQQIFA-LSEVVQRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQ---------AQAQYSQYNQVLA 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 925 DLLGHLTGELERLRRAhERELESVRQEQDQQLEDLRRRHRDQerklqdLEAELSSRTKDVKARLAQLNVQEENMRkekql 1004
Cdd:COG3096 1023 SLKSSRDAKQQTLQEL-EQELEELGVQADAEAEERARIRRDE------LHEELSQNRSRRSQLEKQLTRCEAEMD----- 1090
|
330 340
....*....|....*....|....*..
gi 1958798735 1005 llDAQRQAALEKEEATATRRHLEEAKK 1031
Cdd:COG3096 1091 --SLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
861-1250 |
9.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 861 EQRTHQKVHQVIEYEQELSSLLRDK--RQEVEREHERKMDKMKEEHWQEMAEARERYEAEERK-----QRADLLGHLTGE 933
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimkldNEIKALKSRKKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 934 LERLRRAHERELESVRQEQDQQLEDLRRRH----RDQERKLQDLEAELSSRTKDVK-------------ARLA-QLNVQE 995
Cdd:TIGR00606 281 MEKDNSELELKMEKVFQGTDEQLNDLYHNHqrtvREKERELVDCQRELEKLNKERRllnqektellveqGRLQlQADRHQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 996 ENMRKEKQLLLDAQRQAALEKEEATA-------------TRRHLEEAKKEHTHLLESKQQLRRAIDDLRVRRVELESQVD 1062
Cdd:TIGR00606 361 EHIRARDSLIQSLATRLELDGFERGPfserqiknfhtlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1063 QLQTQSQRLQKHVSSLEAEVQRKQNILKEMAAETNAPphpepglhiEDLRKSLG------TNENQEVSSSLSLSKEGIDL 1136
Cdd:TIGR00606 441 TIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD---------QELRKAERelskaeKNSLTETLKKEVKSLQNEKA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798735 1137 SMDSVRHFLSAEGVAVRSAKEFLVRQTRSMRRRQTALKAAQQ-HWRHELASAQEVDeDLPGTKVLENVRKNLDEETKHLD 1215
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiKSRHSDELTSLLG-YFPNKKQLEDWLHSKSKEINQTR 590
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958798735 1216 E---------MKSAMRKGH--DLLKKKEEKLNQLESSLLEEVSDED 1250
Cdd:TIGR00606 591 DrlaklnkelASLEQNKNHinNELESKEEQLSSYEDKLFDVCGSQD 636
|
|
| |
