|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
146-458 |
3.14e-148 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 427.41 E-value: 3.14e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82654948 386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-142 |
2.12e-27 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 107.82 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 14 GFSSGSAIAGGVKRVAFSSGSM------SGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSsrrgggGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82654948 88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-427 |
4.75e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 144 TAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLqqqttttspKSLDPFFETYINALRKNLDTLSNDKGRLQSELK 223
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------RLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 224 MMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEInftrvlyEAELAQMQthvsdtsvvl 303
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELE---------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 304 smdnnrnlDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQH--GDSLKTTKNEISELNRMIQR-----LRA 376
Cdd:TIGR02168 369 --------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEaelkeLQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 82654948 377 EIENIKKQSQTLQASVADAEQRGELALKdaysKRAELETALQKAKEDLARL 427
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELRE----ELEEAEQALDAAERELAQL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-456 |
5.49e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINf 280
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 281 trvLYEAELAQMQTHVSDTSVVLSMDNNRnldldgiIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQhgdslKTT 360
Cdd:COG1196 334 ---ELEEELEELEEELEEAEEELEEAEAE-------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 361 KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQ---RGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250
....*....|....*....
gi 82654948 438 KLALDVEIATYRKLLEGEE 456
Cdd:COG1196 479 LAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-450 |
7.69e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 313 LDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHG--DSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQA 390
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82654948 391 SVADAEQRGELALKDAYSKRAELETALQK---AKEDLARLLRDYQALMNVKLALDVEIATYRK 450
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-453 |
3.11e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 217 RLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINftrvlyeaELAQMQTHV 296
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 297 SDTsvvlsmdnnrNLDLDGIIAEVRAQYEDiARKSKAEVESwyqiKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRA 376
Cdd:TIGR02168 753 SKE----------LTELEAEIEELEERLEE-AEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 377 EIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
162-414 |
4.12e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 162 DKVRFLEQQNKVLETKWNLLQQQTTTtspksldpfFETYINALRKnldtLSNDKgrlQSELKMMQDSVEDFKTKYEEEIN 241
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRK----KNGEN---IARKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 242 KRTAAENDFVVLKKDVDAAY----MIKVELEAKMESLKDEINFTRVLYEAElAQMQThvsdtsvvLSMDNNRNLDLDGII 317
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ--------ISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 318 AEVRAQYEDIarkskaeveswyQIKVQQLQMSADQHGD---SLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVAD 394
Cdd:PHA02562 309 KELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
|
250 260
....*....|....*....|....*
gi 82654948 395 AEqrGELA-----LKDAYSKRAELE 414
Cdd:PHA02562 377 NA--EELAklqdeLDKIVKTKSELV 399
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
134-456 |
1.36e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQT------TTTSPKSLDPFFETY---INA 203
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 204 LRKNLDTLSNDKGRLQSE---LKMMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 280 FTRVlyeAELAQMQTHVSDTSVVLSmdnnrNLDLDGIIA---EVRAQYEDIARKSK------AEVESWYQIKVQQLqmsa 350
Cdd:PRK01156 557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQeieigfPDDKSYIDKSIREI---- 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 351 DQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQaSVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRD 430
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
330 340
....*....|....*....|....*.
gi 82654948 431 YQALMNVKLALDVEIATYRKLLEGEE 456
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-436 |
4.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 266 ELEAKMESLKDEINFTRVLYE---AELAQMQTHVSDTSVVLSMDNNRnLDLDGI---IAEVRAQYEDIaRKSKAEVEswy 339
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEaleAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERL-DASSDDLA--- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 340 qikvqQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALK---DAYSKRAELETA 416
Cdd:COG4913 689 -----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAV 763
|
170 180
....*....|....*....|
gi 82654948 417 LQKAKEDLARLLRDYQALMN 436
Cdd:COG4913 764 ERELRENLEERIDALRARLN 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-453 |
1.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 191 KSLDPFFETY----------INALRKNLDTLSndkgRLQSELKMMQDSVE---DFKTKYEE-EINKRTAAENDFVVLKKD 256
Cdd:COG4913 207 GDLDDFVREYmleepdtfeaADALVEHFDDLE----RAHEALEDAREQIEllePIRELAERyAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 257 VDAAYMIKVELEAKMESLKDEINFTrvlyEAELAQMQTHVSDtsvvlsmdnnrnldLDGIIAEVRAQYEDIArkskaeve 336
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARL----EAELERLEARLDA--------------LREELDELEAQIRGNG-------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 337 swyQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETA 416
Cdd:COG4913 337 ---GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
250 260 270
....*....|....*....|....*....|....*..
gi 82654948 417 LQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
286-426 |
3.41e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 286 EAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKTTKN 362
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82654948 363 EISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLAR 426
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-449 |
4.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 198 ETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKtkyeeeinkrtaAENDFVVLKKDVDAAYMIKVELEAKMESLKDE 277
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 278 INFTRVLYEAELAQMQTHVSDTSVVLsmDNNRNLDLDGIIAEVRAQYEDIARKSKAEveswyQIKVQQLQmsadqhgDSL 357
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPN-----HPDVIALR-------AQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 358 KTTKNEI-SELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGeLALKDAYSKRAELETALQKAKEDLARLLRDYQALmn 436
Cdd:COG3206 301 AALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA-- 377
|
250
....*....|...
gi 82654948 437 vKLALDVEIATYR 449
Cdd:COG3206 378 -RLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-450 |
5.09e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 203 ALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTR 282
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 283 vlyeAELAQMQTHVSDTSVVLSMdNNRNLDLDGIIAevRAQYEDIARKSKaevesWYQIKVQQLQmsadQHGDSLKTTKN 362
Cdd:COG4942 97 ----AELEAQKEELAELLRALYR-LGRQPPLALLLS--PEDFLDAVRRLQ-----YLKYLAPARR----EQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 363 EIselnrmiQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALD 442
Cdd:COG4942 161 EL-------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*...
gi 82654948 443 VEIATYRK 450
Cdd:COG4942 234 AEAAAAAE 241
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
138-427 |
5.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 138 EIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQttttspksldpffetyINALRKNLDTLSNDKGR 217
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE----------------IERLSIEYNNAMDDYNN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 218 LQSELKMMQdSVEDFKTKYEEEINKrtaaendfvvLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVS 297
Cdd:PRK01156 237 LKSALNELS-SLEDMKNRYESEIKT----------AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 298 DtsvvlsMDNNRNLdLDGIIAEVRaQYEDIARKSkAEVESWYQ--IKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLR 375
Cdd:PRK01156 306 D------IENKKQI-LSNIDAEIN-KYHAIIKKL-SVLQKDYNdyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLK 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 82654948 376 AEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARL 427
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL 428
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
201-434 |
5.84e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 201 INALRKNLDTLSNDKGRLQSELKMMQDSVE----------DFKTKYEEEINKRTAA-ENDFVVLKKDVDAAYMIKVELEA 269
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiQGKNESLEKVSSLTAQlESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 270 KMESLKDeinFTRVLYEAELAQMQTHVSDTSVVLSMD---------NNRNLDLDGIIAEVRAQYEDIARKSKAeVESWYQ 340
Cdd:pfam15921 494 SERTVSD---LTASLQEKERAIEATNAEITKLRSRVDlklqelqhlKNEGDHLRNVQTECEALKLQMAEKDKV-IEILRQ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 341 iKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIK-------KQSQTLQASVADAE-QRGEL---------AL 403
Cdd:pfam15921 570 -QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLElEKVKLvnagserlrAV 648
|
250 260 270
....*....|....*....|....*....|.
gi 82654948 404 KDAYSKRAELETALQKAKEDLARLLRDYQAL 434
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-470 |
8.68e-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: 42.35 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 317 IAEVRAQYEDIARK---SKAEVESwYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVA 393
Cdd:TIGR02168 679 IEELEEKIEELEEKiaeLEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 394 DAEQR----------GELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECRMSGEC 463
Cdd:TIGR02168 758 ELEAEieeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
....*..
gi 82654948 464 KSAVSIS 470
Cdd:TIGR02168 838 RRLEDLE 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-440 |
1.07e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 125 QSLLTPLQVEIDPEIQKIRtAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPKSLDPffETYINAL 204
Cdd:TIGR02168 711 EEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 205 RKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVL 284
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 285 YEAELAQmqthvsdtsvvlsmdnnrnldLDGIIAEVRAQYEDIARKSKAEveswyqikvQQLQMSADQHGDSLKTTKNEI 364
Cdd:TIGR02168 868 IEELESE---------------------LEALLNERASLEEALALLRSEL---------EELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82654948 365 SELNRMIQRLRAEIENIKKQSQTLQASVADaeqRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLA 440
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
266-454 |
1.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 266 ELEAKMESLKDEINFT---RVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQyEDIARKSKAEVESWYQIK 342
Cdd:COG4942 31 QLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-IAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 343 VQQLQMSADQHGDSLKTTKNEISELNRMIQRL-------RAEIENIKKQSQTLQASVADAE-QRGELA--LKDAYSKRAE 412
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylaparREQAEELRADLAELAALRAELEaERAELEalLAELEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 82654948 413 LETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEG 454
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
266-456 |
1.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 266 ELEAKMESLKDEINFTRVLYEAELAQMQThvsdtsvvlsmdnnrnldLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQ 345
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAE------------------LEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 346 LQMSADqhgdsLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKE 422
Cdd:COG1196 298 ARLEQD-----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEA 372
|
170 180 190
....*....|....*....|....*....|....
gi 82654948 423 DLARLLRDYQALMNVKLALDVEIATYRKLLEGEE 456
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
199-431 |
1.65e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 199 TYINAlRKNLDTLSNDKgrlQSELKMMQDSVEDFKTKYEEEINKRTAAENdfvVLKKDVDA-----------------AY 261
Cdd:pfam12128 647 ALKNA-RLDLRRLFDEK---QSEKDKKNKALAERKDSANERLNSLEAQLK---QLDKKHQAwleeqkeqkreartekqAY 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 262 MIKVE--LEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKsKAEVESWY 339
Cdd:pfam12128 720 WQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYF 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 340 QIkvqqLQMSADQHGDSLKTTKNEIS--------ELNRMIQRLRAEIENIKKQSQTLQA---------SVADAEQRGELA 402
Cdd:pfam12128 799 DW----YQETWLQRRPRLATQLSNIEraiselqqQLARLIADTKLRRAKLEMERKASEKqqvrlsenlRGLRCEMSKLAT 874
|
250 260 270
....*....|....*....|....*....|
gi 82654948 403 LK-DAYSKRAELETALQKAKEDLARLLRDY 431
Cdd:pfam12128 875 LKeDANSEQAQGSIGERLAQLEDLKLKRDY 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-437 |
1.69e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 346 LQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQR------------GELA-----LKDAYS 408
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraleQELAaleaeLAELEK 90
|
90 100
....*....|....*....|....*....
gi 82654948 409 KRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQ 119
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
264-456 |
1.74e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 264 KVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEVE-----SW 338
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 339 YQIKVQQLQMSADQH----GDSLKTTKNEISELNRMIQR-------LRAEIENIKKQSQTLQASVADAEQRGE------L 401
Cdd:pfam05557 84 YLEALNKKLNEKESQladaREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQnlekqqS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82654948 402 ALKDAYSKRAELETALQK----------AKEDLARL---------LRDYQALMNV----KLALDVEIATYRKLLEGEE 456
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREHNKHLNEnienKLLLKEEVEDLKRKLEREE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-450 |
2.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 361 KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELalkdayskrAELETALQKAKEDLARLLRDYQALMNVKLA 440
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL---------AELLQELEELKAELRELAEEWAALKLALEL 501
|
90
....*....|
gi 82654948 441 LDVEIATYRK 450
Cdd:COG4717 502 LEEAREEYRE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
267-453 |
4.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 267 LEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLS--MDNNRNLDLDG-------IIAEVRAQYEDiARKSKAEVES 337
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEeaklllqQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 338 WYQIKVQQLQMSADQHGD-----SLKTTKNEISELNRMIQRLRA-------EIENIKKQSQTLQASVADAEQRGELALKD 405
Cdd:COG3206 241 RLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 82654948 406 AY----SKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:COG3206 321 ELealqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-443 |
4.26e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 202 NALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKmESLKDEINFT 281
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEK-AAAYDKLEKT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 282 RVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAE---VRAQYEDiaRKSKAEVESwYQIKVQQLQMSadQHGDSLK 358
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAE--ERDRAEAEA-REKETRALSLA--RALEEAL 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 359 TTKNEISELNRMiqrLRAEIENIKKQSQTLQASVADAEQrgelalkdaySKRAeLETALQKAKEDLARLLRDYQALMNVK 438
Cdd:pfam01576 650 EAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELER----------SKRA-LEQQVEEMKTQLEELEDELQATEDAK 715
|
....*
gi 82654948 439 LALDV 443
Cdd:pfam01576 716 LRLEV 720
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
318-425 |
5.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 318 AEVRAQYEDIARKSKAEVESwyQIKVQQLQMSADQHgDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADA-- 395
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtr 115
|
90 100 110
....*....|....*....|....*....|
gi 82654948 396 EQRGELALKDAYSKRAELETALQKAKEDLA 425
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-434 |
6.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRT----AAENDFVVLKKdvdaaymIKVELEAKMESLKD 276
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLkelePFYNEYLELKD-------AEKELEREEKELKK 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 277 EinftrvlyEAELAQMQTHVSDTsvvlsmdnnrnldlDGIIAEVRAQYEDIARKskaeveswyqikvqqlqMSADQHgds 356
Cdd:PRK03918 624 L--------EEELDKAFEELAET--------------EKRLEELRKELEELEKK-----------------YSEEEY--- 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 357 lKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRgelaLKDAYSKRAELETaLQKAKEDLARL---LRDYQA 433
Cdd:PRK03918 662 -EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEK-LEKALERVEELrekVKKYKA 735
|
.
gi 82654948 434 L 434
Cdd:PRK03918 736 L 736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-450 |
6.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 198 ETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKMESLKDE 277
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 278 InftRVLYEAELAqmqthVSDTSVVLSMDNnrnldldgiiaevraqYEDIARKskaeveswyqikVQQLQMSADQHGDSL 357
Cdd:COG3883 92 A---RALYRSGGS-----VSYLDVLLGSES----------------FSDFLDR------------LSALSKIADADADLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 358 KTtkneiselnrmIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG3883 136 EE-----------LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250
....*....|...
gi 82654948 438 KLALDVEIATYRK 450
Cdd:COG3883 205 LAAAEAAAAAAAA 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-446 |
7.87e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82654948 310 NLD-LDGIIAEVRAQYEDIAR-KSKAEveswyqiKVQQLQMSADQHgdSLKTTKNEISELNRMIQRLRAEIENIKKQSQT 387
Cdd:COG1196 187 NLErLEDILGELERQLEPLERqAEKAE-------RYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82654948 388 LQASVADAEQRGELALKDAYSKRAELETA---LQKAKEDLARLLRDYQALMNVKLALDVEIA 446
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLE 319
|
|
|