|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
136-449 |
4.65e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 434.35 E-value: 4.65e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSkNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKT 215
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 216 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLS 295
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 296 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835922520 376 CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 449
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-133 |
4.13e-34 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 125.92 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 14 GFSCGSAIVGGGKRGAFSSVSMS------GGAGRCSSGGFGSRSLYNLRGNKSISMSVAGSRQGACFGGAGGFGTGGFGG 87
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835922520 88 GFGGSFSGKGGPG------------------------------FPVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 133
Cdd:pfam16208 81 GGFGGGGGGGFGGgggfgggfggggyggggfggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-425 |
2.80e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 165 LETKWNLLQQQT-TTTSSKNL-EPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDfktkYEEEINKRTAAENDFV 242
Cdd:TIGR02168 198 LERQLKSLERQAeKAERYKELkAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 243 VLKKDVDAAYlnkVELEAKVDSLNDEINFL---KVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA 319
Cdd:TIGR02168 274 LEVSELEEEI---EELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 320 QRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRG------- 390
Cdd:TIGR02168 351 EELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkl 430
|
250 260 270
....*....|....*....|....*....|....*.
gi 1835922520 391 -ENALKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168 431 eEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-425 |
6.48e-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: 55.45 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 133 VRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTssKNLEPLFETYLSVLRKQLDTLGNDKGRLQSE 212
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 213 LKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaylNKVELEAKVDSLNDEINFLKvlydAELSQMQTHVSDTSV 292
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 293 VLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtkvqqlqisvdqhgdNLKNTKSEIAELNRMIQRLRAEIENI 372
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835922520 373 KKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-433 |
1.20e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 192 LSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINF 271
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 272 LKVLYDAELSQmqthvsdtsvvLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQhgdnlKNT 351
Cdd:COG1196 335 LEEELEELEEE-----------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 352 KSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLA 431
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
..
gi 1835922520 432 LD 433
Cdd:COG1196 479 LA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
131-425 |
1.80e-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: 54.29 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 131 QKVRTEERE-QIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGNDKGRL 209
Cdd:TIGR02168 216 KELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK---------LEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 210 QSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMqthvsd 289
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 290 tsvvlsmdnnrnldldsiiAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 367
Cdd:TIGR02168 361 -------------------EELEAELEELESRLEELEEQLetLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1835922520 368 EIENIKKQCQTLQVSVADAEQRGENA-LKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAA 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-444 |
6.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 303 DLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISvdqhGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVS 382
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNG----GDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835922520 383 VADAE--------------QRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG4913 375 LPASAeefaalraeaaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-447 |
9.96e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 245 KKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQThvsdtsvvlsmdnnrnldLDSIIAEVRAQYEEIAQRSKA 324
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE------------------LEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 325 EAEALYQ--TKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQR---GENALKDAHS 399
Cdd:COG1196 286 AQAEEYEllAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEE 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1835922520 400 KRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-447 |
1.33e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 301 NLD-LDSIIAEVRAQYEEIA-QRSKAE-----AEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIK 373
Cdd:COG1196 187 NLErLEDILGELERQLEPLErQAEKAEryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 374 KQCQTLQVSVADAEQRGENALKDAHSKRVELEAA----------LQQAKEELARMLREYQELMSVKLALDIEIATYRKLL 443
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLeqdiarleerRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
....
gi 1835922520 444 EGEE 447
Cdd:COG1196 347 EEAE 350
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-459 |
1.64e-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: 50.83 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 304 LDSIIAEVRAQYEEIAQRSKAEAEALYQTK--VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 382 SVADAEQRGENALKDAHSKRV---ELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK---LLEGEEYRMSGECQ 455
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403
|
....
gi 1835922520 456 SAVS 459
Cdd:TIGR02168 404 RLEA 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-444 |
2.35e-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: 50.44 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINflkvlydaELSQMQTHV 287
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 288 SDTsvvlsmdnnrNLDLDSIIAEVRAQYEEiAQRSKAEAEAlyqtKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 367
Cdd:TIGR02168 753 SKE----------LTELEAEIEELEERLEE-AEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 368 EIENIKKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
129-375 |
3.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 129 EIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKwnlLQQQTTTTSSKNLE-PLFETYLSVLRKQLDTLGNDKG 207
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLK---------------------KDVDAAYLNKVELEAKVDSLN 266
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskeKELKKLNEEKKELEEKVKDLT 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 267 DEINFLKVLYD---AELSQMQTHVSD-TSVVLSMDNNrnLDLDSIIAEVRAQYEEIAQrSKAEAEALyQTKVQQLQISVD 342
Cdd:TIGR04523 517 KKISSLKEKIEkleSEKKEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELID 592
|
250 260 270
....*....|....*....|....*....|...
gi 1835922520 343 QHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
258-464 |
3.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 258 LEAKVDSLNDEINFLK---VLYDAELSQMQTHVSD---TSVVLSMDNNRNLDLDSIiAEVRAQYEEiAQRSKAEAEALYQ 331
Cdd:COG3206 166 LELRREEARKALEFLEeqlPELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 332 TKVQQLQISVDQHGDNLKNT-----KSEIAELNRM--------------IQRLRAEIENIKKQcqtLQVSVADAEQRGEN 392
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviqqlRAQLAELEAElaelsarytpnhpdVIALRAQIAALRAQ---LQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835922520 393 ALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG-EEYRMSGEcQSAVSISVVS 464
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEA-LTVGNVRVID 392
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
135-410 |
4.18e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 135 TEEREQIKLLNNKFASFIDKVQFLEQQN-----KVLETKWNLL-------QQQTTTTSSKNLEPLFETYLSVlRKQLDTL 202
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATvelhlSNIENKKNELldiiveiKKHIHGEINKDLNKILEDFKNK-EKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 203 GNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQ 282
Cdd:TIGR01612 771 INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 283 MQTHVsdtsvvlSMDNNRNLDLDSiiaeVRAQYEEIAQRSKAEaealyqtkvqqlqISVDQHGD---NLKNTKSEIAELN 359
Cdd:TIGR01612 848 VDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAE-------------ISDDKLNDyekKFNDSKSLINEIN 903
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1835922520 360 RMIQRLRAEIENIKKQCQTLQVSVADAEqrgenALKDAHSKRVELEAALQQ 410
Cdd:TIGR01612 904 KSIEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-444 |
4.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 257 ELEAKVDSLNDEINFLKVLY---DAELSQMQTHVSDTSVVLSMDNNRnLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtk 333
Cdd:COG4913 614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 334 VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRG------------ENALKDAHSKR 401
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralleerfAAALGDAVERE 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835922520 402 V---------ELEAALQQAKEELARMLREYQEL-MSVKLALDIEIAT---YRKLLE 444
Cdd:COG4913 767 LrenleeridALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
191-402 |
5.27e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 191 YLSVLRKQLDTLGndkgRLQSELKTMQDSVEDFKTKYEEEINKRtaAENDFVVLKKDVDAaYLNKV-ELEAKVDSLNDEI 269
Cdd:PRK05771 51 LLTKLSEALDKLR----SYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEKIEKEIKE-LEEEIsELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 270 NFLKVL--YDAELSQMQTHvSDTSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQTK---V 334
Cdd:PRK05771 124 ERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgF 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835922520 335 QQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADA----EQRGENALKDAHSKRV 402
Cdd:PRK05771 203 ERLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
189-417 |
1.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 189 ETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDaaylnkvELEAKVDSLNDE 268
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 269 I-NFLKVLYDAELSqmqthVSDTSVVLSMDN-----NRNLDLDSIIAEVRAQYEEI--AQRSKAEAEALYQTKVQQLQIS 340
Cdd:COG3883 88 LgERARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835922520 341 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELAR 417
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
125-447 |
1.35e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 125 EIDPE-IQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQT------TTTSSKNLEPLFETYlsvlrk 197
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHY------ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 198 qldtlGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAEndfvvlKKDVDA--AYLNKVE-LEAKVDSLNDEINFLK- 273
Cdd:PRK01156 475 -----NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE------SEEINKsiNEYNKIEsARADLEDIKIKINELKd 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 274 --VLYDAELSQMQT-HVSDTSVVLSMDNNRNLDLDSI-IAEVRAQYEEIAQRSKAEAEALYQTKVQQLQIS--------- 340
Cdd:PRK01156 544 khDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksire 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 341 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQvSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLR 420
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702
|
330 340
....*....|....*....|....*..
gi 1835922520 421 EYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMK 729
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
303-418 |
2.01e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.58 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 303 DLDSIIAEVRAQYEEI-AQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQR----------LRAEIEN 371
Cdd:COG1566 80 DLQAALAQAEAQLAAAeAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqeldeARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1835922520 372 IKKQCQTLQVSVADAEQ--RGENALKDAHSKRVELEAALQQAKEELARM 418
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAglREEEELAAAQAQVAQAEAALAQAELNLART 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-449 |
3.68e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 304 LDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835922520 382 SVADAEQRgenaLKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 449
Cdd:COG1196 324 ELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
277-417 |
4.84e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 277 DAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEiAQRSKAEAEALY---QTKVQQLQISVDQHGDNLKNTKS 353
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835922520 354 EIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELAR 417
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-434 |
1.44e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 195 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINflkv 274
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN---- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 275 lydaelsQMQTHVSDTSVVLsmDNNRNL---------DLDSIIAE---VRAQYEEiaQRSKAEAEAL-YQTKVqqlqISV 341
Cdd:pfam01576 577 -------RLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEAReKETRA----LSL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 342 DQHGDNLKNTKSEIAELNRMiqrLRAEIENIkkqcqtlqVSVADAEqrGENALKDAHSKRVeLEAALQQAKEELARMLRE 421
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQ---LRAEMEDL--------VSSKDDV--GKNVHELERSKRA-LEQQVEEMKTQLEELEDE 707
|
250
....*....|...
gi 1835922520 422 YQELMSVKLALDI 434
Cdd:pfam01576 708 LQATEDAKLRLEV 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-447 |
1.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 303 DLDSIIAEVRAQYEEIAQRSKAEAEALYQT----KVQQLQISVDQHGD---NLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSwdeiDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835922520 376 CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLRE-YQELM------SVKLALDIEIATYRKLLEGEE 447
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALgdaverELRENLEERIDALRARLNRAE 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
304-441 |
1.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 304 LDSIIAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLKN--TKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 382 SVADAEQRGENALKDAhsKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK 441
Cdd:COG4717 454 ELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-447 |
1.83e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 195 LRKQLDTLGNDKGR------LQSELKTMQDSV-----EDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVD 263
Cdd:COG1196 198 LERQLEPLERQAEKaeryreLKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 264 SLNDEINflkvlydaelsQMQthvsdtsvvlsmdnNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqtkvQQLQISVDQ 343
Cdd:COG1196 278 ELELELE-----------EAQ--------------AEEYELLAELARLEQDIARLEERRRELEERL-----EELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 344 HGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARmLREYQ 423
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELE 406
|
250 260
....*....|....*....|....
gi 1835922520 424 ELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEAL 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
153-385 |
2.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 153 DKVQFLEQQNKVLETKWNLLQQQTTTtssknleplFETYLSVLRKQLDtlgNDKGRLQSELKTMQDSVEDFKTkyeeEIN 232
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKA----EIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 233 KRTAAENDFVVLKKDVDAAyLNK-----VELEAKVDSLNDEINFLKvlydaELSQMQTHVSDTSvvlsmdnnrnlDLDSI 307
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAA-LNKlntaaAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDR 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835922520 308 IAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVAD 385
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTA--IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
136-458 |
2.12e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKNLEPL-FETYLSVLRKQLDTLGNDKGRLQSELK 214
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 215 TMQdsVEdfKTKYEEEINKRTAAENDFVVLKKDVDAAYLnkvELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVL 294
Cdd:pfam15921 587 AMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 295 SMDNNRNLDLDSIIAEvraqYEEIAQRSKAEAEALYQT------KVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAE 368
Cdd:pfam15921 660 NEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTtnklkmQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 369 IENIKKQCQTLQVSVADAEQRGENALKDAH---SKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG 445
Cdd:pfam15921 736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
330
....*....|...
gi 1835922520 446 EEYRMSgECQSAV 458
Cdd:pfam15921 816 ASLQFA-ECQDII 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-441 |
2.56e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 197 KQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKvly 276
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 277 dAELSQMQTHVSDTSVVLSMDNNRNLDL------DSIIAEVRAQY-EEIAQRSKAEAEALYQTKVQqlqisvdqhgdnlk 349
Cdd:COG4942 97 -AELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYlKYLAPARREQAEELRADLAE-------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 350 ntkseiaelnrmIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVK 429
Cdd:COG4942 162 ------------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 1835922520 430 LALDIEIATYRK 441
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
134-426 |
2.79e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 134 RTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKNLEPlfETYLSVLRKQLDTLGNDKGRLQSEL 213
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH--EARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 214 KTMQDSVEDFKTKYEEEINKRTAAENDFVV-------LKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYD------AEL 280
Cdd:pfam07888 153 ERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrsLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeAEN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 281 SQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVraqyeeIAQRSKAEAEaLYQTKVQQLQISVD----------------QH 344
Cdd:pfam07888 233 EALLEELRSLQERLNASERKVEGLGEELSSM------AAQRDRTQAE-LHQARLQAAQLTLQladaslalregrarwaQE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 345 GDNLKNT----KSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLR 420
Cdd:pfam07888 306 RETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
....*.
gi 1835922520 421 EYQELM 426
Cdd:pfam07888 386 EKQELL 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
303-425 |
3.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 303 DLDSIIAEVRAQYEEI------AQRSKAEAEALYQTKVQQLQISVDQHGdNLKNTK------SEIAELNRMIQRLRAEIE 370
Cdd:COG1579 35 ELEDELAALEARLEAAkteledLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKeyealqKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1835922520 371 NIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-447 |
3.42e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 188 FETYLSVLRKQLDTLGNDKGRLQsELKTMQDSVEDFKtkYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLND 267
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 268 EINFLKVLydaeLSQMQTHVSDtsvvlsMDNNRNLDLDSIIAEVRAqyeEIAQRSKAEAEalYQTKVQQLQisvdqhgDN 347
Cdd:TIGR02169 266 RLEEIEQL----LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDAE-------ER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 348 LKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGE-------------NALKDAHSKRVEleaALQQAKEE 414
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefAETRDELKDYRE---KLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|...
gi 1835922520 415 LARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
129-444 |
4.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 129 EIQKVRTEEREQIKLLNNKFASF---IDKVQFLEQQNKVLETKWNLLQQQTTTTSSKNLEPLFETYlSVLRKQLDTLGND 205
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 206 KGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDF--------VVLKKDVDAAYLNKVEL------------------- 258
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIagvlflvlgllallfllla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 259 --EAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ 336
Cdd:COG4717 295 reKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 337 LQISVD-----------QHGDNLKNTKSEIAELNRMIQRLRAEI---------ENIKKQCQTLQVSVADAEQRgenaLKD 396
Cdd:COG4717 375 LLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEE----LEE 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1835922520 397 AHSKRVELEAALQQAKE--ELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG4717 451 LREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
309-416 |
7.45e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 309 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHgDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ-VSVADAE 387
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKdDNDEETR 115
|
90 100 110
....*....|....*....|....*....|
gi 1835922520 388 QRGENA-LKDAHSKRVELEAALQQAKEELA 416
Cdd:PRK11281 116 ETLSTLsLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
187-429 |
8.25e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 187 LFETYLSVLRKQLDTLGNDKGRLQSELKTMQdsvedfktKYEEEINKRTAAENDfvvlkkdvdaaylnkvELEAKVDSLN 266
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYN--------KNIEEQRKKNGENIA----------------RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 267 DEINFLKvlydAELSQMQTHVSDtsVVLSMDNNRNL--DLDSIIAEVRAQYEEIAQRSK---------------AEAEAL 329
Cdd:PHA02562 227 EEAKTIK----AEIEELTDELLN--LVMDIEDPSAAlnKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 330 Y---QTKVQQLQISVDQ---HGDNLKNTKSEIAELNRMIQRLRAEIENIKkqcQTLQVSVADAeqrgenalKDAHSKRVE 403
Cdd:PHA02562 301 ItkiKDKLKELQHSLEKldtAIDELEEIMDEFNEQSKKLLELKNKISTNK---QSLITLVDKA--------KKVKAAIEE 369
|
250 260
....*....|....*....|....*.
gi 1835922520 404 LEAALQQAKEELARMLREYQELMSVK 429
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTK 395
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
237-441 |
8.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 237 AENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYD---AELSQMQTHVSDTsvvlsmdnnrNLDLDSIIAEVRA 313
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 314 QYEEIAQRskaeAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRM----------IQRLRAEIENIKKQCQTLQVSV 383
Cdd:COG3883 84 RREELGER----ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIadadadlleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835922520 384 ADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK 441
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-433 |
9.08e-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: 42.03 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 130 IQKVRTEEREQIKLLNNKFASFIDKVQFL--EQQNKVletkwNLLQQQttttSSKNLEPLF---ETYLSVLRKQLDTLGN 204
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALksESQNKI-----ELLLQQ----HQDRIEQLIsehEVEITGLTEKASSARS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 205 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAylnKVELEAKVDSLNDEInflkVLYDAELSQMQ 284
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSD---LESTVSQLRSELREA---KRMYEDKIEELEKQL----VLANSELTEAR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 285 THVSDTSvvlsmDNNRNLD--LDSIIAEVRAQYEEIAQRsKAEAEALYQTKVQQlQISVDqhgdnlkNTKSEIAELNRMI 362
Cdd:pfam15921 363 TERDQFS-----QESGNLDdqLQKLLADLHKREKELSLE-KEQNKRLWDRDTGN-SITID-------HLRRELDDRNMEV 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835922520 363 QRLRAEIENIKKQCQTlQVSVADAEQRGENalkDAHSKRVELEAALQQAKEELARMLreyQELMSVKLALD 433
Cdd:pfam15921 429 QRLEALLKAMKSECQG-QMERQMAAIQGKN---ESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLE 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-423 |
1.12e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 195 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEInflkv 274
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 275 lydAELSQMQTHVsdtsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRskaeaeaLYQTKVQQLQISVDQHGDNLKNTKSE 354
Cdd:TIGR02169 754 ---ENVKSELKEL----------EARIEELEEDLHKLEEALNDLEAR-------LSHSRIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835922520 355 IAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRgenalKDAHSKRVELeaaLQQAKEELARMLREYQ 423
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-----IKSIEKEIEN---LNGKKEELEEELEELE 874
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
309-424 |
1.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 309 AEVRAQYEEIAQRSKAEAE--------ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ 380
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1835922520 381 vsvADAEQRGEN--ALKDAHSKRVELEAALQQAKEELARMLREYQE 424
Cdd:PRK12704 138 ---EEQLQELERisGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-447 |
1.30e-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: 41.58 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 350 NTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKR---VELEAALQQAKEELARMLREYQELM 426
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLS 753
|
90 100
....*....|....*....|.
gi 1835922520 427 SVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAE 774
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
303-444 |
1.43e-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: 40.29 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 303 DLDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA------------- 367
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 368 ---EIENIKKQCQTLqvsvadaeqrgENALKDAHSKRVELEAALQQAKEELARMLREYQELmsvKLALDIEIATYRKLLE 444
Cdd:COG1579 94 lqkEIESLKRRISDL-----------EDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-445 |
2.00e-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: 40.52 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 232 NKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLkvlyDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEV 311
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 312 RAQYEEIAQRSKAEAEALYQTKvQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQ--- 388
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAera 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835922520 389 RGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG 445
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-436 |
2.29e-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: 40.81 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 195 LRKQLDTLgndkgRLQSELktmqdsVEDFKTKYEEEINKrtaaendfvvlkkDVDAAYLNKVELEAKVDSLNDEINFLKV 274
Cdd:TIGR02168 198 LERQLKSL-----ERQAEK------AERYKELKAELREL-------------ELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 275 LYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALyQTKVQQLQISVDQHGDNL 348
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANL-ERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 349 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLqvsvadaeqrgENALKDAHSKRVELEAALQQAKEELARMLREYQELMSV 428
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEEL-----------EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
....*...
gi 1835922520 429 KLALDIEI 436
Cdd:TIGR02168 402 IERLEARL 409
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
302-419 |
2.40e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 39.04 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 302 LDLDSIIAEVRAqyeeiAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:pfam02321 69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143
|
90 100 110
....*....|....*....|....*....|....*...
gi 1835922520 382 SVADAEQrGENALKDAHSKRVELEAALQQAKEELARML 419
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-372 |
3.23e-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: 40.43 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 134 RTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGNDKGRLQSEL 213
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---------LKALREALDELRAELTLLNEEA 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 214 KTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSD---T 290
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEleeL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 291 SVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRsKAEAEALYQTKVQQL----QISVDQHGDNLKNTKSEIAELNRMIQRLR 366
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 1835922520 367 AEIENI 372
Cdd:TIGR02168 979 NKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-444 |
3.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 126 IDPEIQKVRTEEREQIKLLNNKFAsfiDKVQFLEQQNKVLETkwNLLQQQTTTTSSKN-LEPLFETYLSVLRKQLDTLGN 204
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQ---DRIEQLISEHEVEIT--GLTEKASSARSQANsIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 205 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQ 284
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 285 THVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIaQRSKAEAEALY---QTKVQQLQISVDQHGDNLKNTKSEIAELNRM 361
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV-QRLEALLKAMKsecQGQMERQMAAIQGKNESLEKVSSLTAQLEST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 362 IQRLRAEIENIKKQCQTLQVS---VAD---AEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKL---AL 432
Cdd:pfam15921 474 KEMLRKVVEELTAKKMTLESSertVSDltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTeceAL 553
|
330
....*....|..
gi 1835922520 433 DIEIATYRKLLE 444
Cdd:pfam15921 554 KLQMAEKDKVIE 565
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
352-414 |
4.70e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 37.83 E-value: 4.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835922520 352 KSEIAELNRMIQRLRAEIENIKKQcqtlqvsvadAEQRGENALKDAHSKRVE--------LEAALQQAKEE 414
Cdd:COG0576 5 EAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLAEdllpvldnLERALAAAEED 65
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-415 |
5.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 195 LRKQLDTLGndkgRLQSELKTMQDSVE---DFKTKYEE-EINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEIN 270
Cdd:COG4913 230 LVEHFDDLE----RAHEALEDAREQIEllePIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 271 FLkvlyDAELSQMQTHVSDT-----SVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalYQTKVQQLQISVDQhg 345
Cdd:COG4913 306 RL----EAELERLEARLDALreeldELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR--LEALLAALGLPLPA-- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 346 dnlknTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSK------------------RVELEAA 407
Cdd:COG4913 378 -----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniparllalRDALAEA 452
|
....*...
gi 1835922520 408 LQQAKEEL 415
Cdd:COG4913 453 LGLDEAEL 460
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
210-375 |
5.20e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 38.78 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 210 QSELKTMQDSVEDFKTKYEEEINKrtaaendfvvLKKDVDaaylnkvELEAKVDSLNDEINFLKVLYDAE-------LSQ 282
Cdd:pfam15397 62 KKQLQQAKAELQEWEEKEESKLNK----------LEQQLE-------QLNAKIQKTQEELNFLSTYKDKEypvkavqIAN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 283 MQTHVSDTSvvlsmDNNRN--LDLDSIIAEVRAQYEEIAQRSK--------AEAEALYQTKVQQLQIS-------VDQHG 345
Cdd:pfam15397 125 LVRQLQQLK-----DSQQDelDELEEMRRMVLESLSRKIQKKKekilsslaEKTLSPYQESLLQKTRDnqvmlkeIEQFR 199
|
170 180 190
....*....|....*....|....*....|
gi 1835922520 346 DNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam15397 200 EFIDELEEEIPKLKAEVQQLQAQRQEPREV 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
129-429 |
6.72e-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: 39.32 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 129 EIQKVRTEEREQIKLLNNKFASfidkvqfLEQQNKVLETKWNLLQQQttttssKNLEPLFETyLSVLRKQLDTLgndkgr 208
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEK------KQFEKIAEE-LKGKEQELIFL------ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 209 LQSELKTMQD-SVEDFKTKYEEEINKRTAAEndfvvLKKDVDAAYLNKVELEAKVDSLndeinflkVLYDAELSQmqtHV 287
Cdd:pfam05483 445 LQAREKEIHDlEIQLTAIKTSEEHYLKEVED-----LKTELEKEKLKNIELTAHCDKL--------LLENKELTQ---EA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 288 SDTSVVLSM---DNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ---LQISVDQHGDNLKNTKSEIAELNRM 361
Cdd:pfam05483 509 SDMTLELKKhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835922520 362 IQRLRAEIENIKKQCQTLQVSVADAEQRGEnALK---DAHSKRV--------ELEAALQQAKEELARMLREYQELMSVK 429
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENK-ALKkkgSAENKQLnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
304-425 |
7.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 304 LDSIIAEVRAQYEEIAQRSKA-----EAEALYQtKVQQLQISVDQHGDNLKNTKSEIAELNRM---IQRLRAEIENIKKQ 375
Cdd:COG4717 100 LEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEE 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1835922520 376 CQTLQvsvADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:COG4717 179 LEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-389 |
7.54e-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: 38.59 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 129 EIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQttttssknleplfetyLSVLRKQLDTLGNDKGR 208
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 209 LQSELKTMQDsvedfktkyeeeinkrtaaendfvVLKKDVDAAYLNkveleakvdSLNDEINFLkvLYDAELSQMQTHVS 288
Cdd:COG4942 95 LRAELEAQKE------------------------ELAELLRALYRL---------GRQPPLALL--LSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 289 DTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQR--SKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLR 366
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAEraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|...
gi 1835922520 367 AEIENIKKQCQTLQVSVADAEQR 389
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
125-444 |
8.45e-03 |
|
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: 38.85 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 125 EIDPEIQKVRTEEREQIKLLNNKFASFIDKvqflEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGN 204
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKILEQQIKDLNDK---------LKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 205 DKGRLQSELKTMQDSVEDFKTKY---EEEINKRTAAENDFV--VLKKDVDAAYLN---------KVELEAKVDSLNDEI- 269
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELnklEKQKKENKKNIDKFLteIKKKEKELEKLNnkyndlkkqKEELENELNLLEKEKl 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 270 NFLKVLYDA--ELSQMQTHVSdtsvVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALYQTKVQQLQISV 341
Cdd:TIGR04523 184 NIQKNIDKIknKLLKLELLLS----NLKKKIQKNKSLESQISELKKQNNQLKdniekkQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 342 DQHGDN----------LKNTKSEIAELNRMIQRLRAEIENIKKQ-CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQ 410
Cdd:TIGR04523 260 DEQNKIkkqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350
....*....|....*....|....*....|....
gi 1835922520 411 AKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
300-447 |
9.69e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.69 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 300 RNLDLDSIIAEVRAQY--EEIAQRSKAEAEALYQTKVQQLQISVDQhgdNLKNTKSEIAELNRMIQRLRAEIENIKKQcq 377
Cdd:COG2433 361 PDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVEELEAE-- 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835922520 378 tlqvsVADAEQRGEnalkdahskrvELEAALQQAKEELARMLREYQELMsvklALDIEIATYRKLLEGEE 447
Cdd:COG2433 436 -----LEEKDERIE-----------RLERELSEARSEERREIRKDREIS----RLDREIERLERELEEER 485
|
|
| |
