|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
224-537 |
3.34e-160 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 460.93 E-value: 3.34e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 224 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSkNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKT 303
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 304 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLS 383
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 384 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 463
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694950035 464 CQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 537
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
88-221 |
3.28e-32 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 121.69 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 88 GFSCGSAIVGGGKRGAFSSVSMS------GGAGRCSPGGFGSRSLYNLRGNKSISMSVA--GSRQGACFGGAGGFGTGGF 159
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAggGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694950035 160 GAGGFGAGFGTGGFGGGFGGSFSGKGGPG--------------FPVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 221
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFGGGFGGGGYGGGgfggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-513 |
8.35e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 285 KQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFL---K 361
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 362 VLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNT 439
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 440 KSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRV--------ELEAALQQAKEELARMLREYQ 511
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaeleELEEELEELQEELERLEEALE 464
|
..
gi 694950035 512 EL 513
Cdd:TIGR02168 465 EL 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-513 |
2.08e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 221 VRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTssKNLEPLFETYLSVLRKQLDTLGNDKGRLQSE 300
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 301 LKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaymNKVELEAKVDSLNDEINFLKvlydAELSQMQTHVSDTSV 380
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 381 VLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtkvqqlqisvdqhgdNLKNTKSEIAELNRMIQRLRAEIENI 460
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 694950035 461 KKQCQTLQASVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
217-503 |
7.86e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKwnlLQQQTTTTSSK--NLEPLfETYLSVLRKQLDTLGNDK 294
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKdeQIKKL-QQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 295 GRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLK---------------------KDVDAAYMNKVELEAKVDSL 353
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskeKELKKLNEEKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 354 NDEINFLKVLYD---AELSQMQTHVSD-TSVVLSMDNNrnLDLDSIIAEVRAQYEEIAQrSKAEAEALyQTKVQQLQISV 429
Cdd:TIGR04523 516 TKKISSLKEKIEkleSEKKEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELI 591
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694950035 430 DQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLqasvadaeqrgENALKDAHSKRVELEAALQQAKEEL 503
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL-----------SSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-513 |
8.69e-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: 58.91 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 219 QKVRTEERE-QIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGNDKGRL 297
Cdd:TIGR02168 216 KELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK---------LEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 298 QSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMqthvsd 377
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL------ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 378 tsvvlsmdnnrnldldsiiAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 455
Cdd:TIGR02168 361 -------------------EELEAELEELESRLEELEEQLetLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 694950035 456 EIENIKKQCQTLQASVADAEQRGENA-LKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
280-521 |
8.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 280 LSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINF 359
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 360 LKVLYDAELSQmqthvsdtsvvLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQhgdnlKNT 439
Cdd:COG1196 335 LEEELEELEEE-----------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 440 KSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLA 519
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
..
gi 694950035 520 LD 521
Cdd:COG1196 479 LA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-535 |
7.28e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 396 IAEVRAQYEEIAQRSKAEAEALYQ--TKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD 473
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694950035 474 AEQR---GENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 535
Cdd:COG1196 349 AEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-532 |
8.18e-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: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 296 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflkvlydaELSQMQTHV 375
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--------QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 376 SDTsvvlsmdnnrNLDLDSIIAEVRAQYEEiAQRSKAEAEAlyqtKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 455
Cdd:TIGR02168 753 SKE----------LTELEAEIEELEERLEE-AEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 456 EIENIKKQCQTLQASVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 532
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-547 |
1.16e-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: 55.06 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 392 LDSIIAEVRAQYEEIAQRSKAEAEALYQTK--VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 469
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 470 SVADAEQRGENALKDAHSKRV---ELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK---LLEGEEYRMSGECQ 543
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403
|
....
gi 694950035 544 SAVS 547
Cdd:TIGR02168 404 RLEA 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
389-535 |
1.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 389 NLD-LDSIIAEVRAQYEEIA-QRSKAE-----AEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIK 461
Cdd:COG1196 187 NLErLEDILGELERQLEPLErQAEKAEryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 462 KQCQTLQASVADAEQRGENALKDAHSKRVELEAA----------LQQAKEELARMLREYQELMSVKLALDIEIATYRKLL 531
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLeqdiarleerRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
....
gi 694950035 532 EGEE 535
Cdd:COG1196 347 EEAE 350
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
213-535 |
1.64e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 213 EIDPE-IQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQT------TTTSSKNLEPLFETYlsvlrk 285
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHY------ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 286 qldtlGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAEndfvvlKKDVDA--AYMNKVE-LEAKVDSLNDEINFLK- 361
Cdd:PRK01156 475 -----NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE------SEEINKsiNEYNKIEsARADLEDIKIKINELKd 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 362 --VLYDAELSQMQT-HVSDTSVVLSMDNNRNLDLDSI-IAEVRAQYEEIAQRSKAEAEALYQTKVQQLQIS--------- 428
Cdd:PRK01156 544 khDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksire 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 429 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQaSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLR 508
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702
|
330 340
....*....|....*....|....*..
gi 694950035 509 EYQELMSVKLALDIEIATYRKLLEGEE 535
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-532 |
1.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 392 LDSIIAEVRAQYEEIAQ---RSKAEAEALyQTKVQQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTL 467
Cdd:COG4913 293 LEAELEELRAELARLEAeleRLEARLDAL-REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694950035 468 --------------QASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 532
Cdd:COG4913 372 glplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
277-505 |
2.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 277 ETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDaaymnkvELEAKVDSLNDE 356
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 357 I-NFLKVLYDAELSqmqthVSDTSVVLSMDN-----NRNLDLDSIIAEVRAQYEEI--AQRSKAEAEALYQTKVQQLQIS 428
Cdd:COG3883 88 LgERARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 429 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELAR 505
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
346-552 |
2.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 346 LEAKVDSLNDEINFLK---VLYDAELSQMQTHVSD---TSVVLSMDNNRNLDLDSIiAEVRAQYEEiAQRSKAEAEALYQ 419
Cdd:COG3206 166 LELRREEARKALEFLEeqlPELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 420 TKVQQLQISVDQHGDNLKNT-----KSEIAELNRM--------------IQRLRAEIENIKKQcqtLQASVADAEQRGEN 480
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviqqlRAQLAELEAElaelsarytpnhpdVIALRAQIAALRAQ---LQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694950035 481 ALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG-EEYRMSGEcQSAVSISVVS 552
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEA-LTVGNVRVID 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
391-532 |
2.33e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 391 DLDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIK--KQCQT 466
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694950035 467 LQASVADAEQR---GENALKDAHSKRVELEAALQQAKEELARMLREYQELmsvKLALDIEIATYRKLLE 532
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
345-532 |
3.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 345 ELEAKVDSLNDEINFLKVLY---DAELSQMQTHVSDTSVVLSMDNNRnLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtk 421
Cdd:COG4913 614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 422 VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRG------------ENALKDAHSKR 489
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralleerfAAALGDAVERE 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 694950035 490 V---------ELEAALQQAKEELARMLREYQEL-MSVKLALDIEIAT---YRKLLE 532
Cdd:COG4913 767 LrenleeridALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-526 |
6.42e-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: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 392 LDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 469
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 470 SVADAEQRGENA----------LKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIAT 526
Cdd:COG1196 324 ELAELEEELEELeeeleeleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
391-506 |
1.02e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.20 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 391 DLDSIIAEVRAQYEEI-AQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQR----------LRAEIEN 459
Cdd:COG1566 80 DLQAALAQAEAQLAAAeAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqeldeARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 694950035 460 IKKQCQTLQASVADAEQ--RGENALKDAHSKRVELEAALQQAKEELARM 506
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAglREEEELAAAQAQVAQAEAALAQAELNLART 208
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
223-498 |
1.84e-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: 51.21 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 223 TEEREQIKLLNNKFASFIDKVRFLEQQN-----KVLETKWNLL-------QQQTTTTSSKNLEPLFETYLSVlRKQLDTL 290
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATvelhlSNIENKKNELldiiveiKKHIHGEINKDLNKILEDFKNK-EKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 291 GNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQ 370
Cdd:TIGR01612 771 INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 371 MQTHVsdtsvvlSMDNNRNLDLDSiiaeVRAQYEEIAQRSKAEaealyqtkvqqlqISVDQHGD---NLKNTKSEIAELN 447
Cdd:TIGR01612 848 VDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAE-------------ISDDKLNDyekKFNDSKSLINEIN 903
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 694950035 448 RMIQRLRAEIENIKKQCQTLQASVADAEqrgenALKDAHSKRVELEAALQQ 498
Cdd:TIGR01612 904 KSIEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
343-535 |
2.14e-06 |
|
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: 50.89 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 343 KVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEA------ 416
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELnrlkkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 417 -------LYQTKVQQLQisvdQHGDNLKNTKSEIAELNRMIQR-------LRAEIENIKKQCQTLQASVADAEQRGEN-- 480
Cdd:pfam05557 84 ylealnkKLNEKESQLA----DAREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQNle 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 481 ----ALKDAHSKRVELEAALQQ----------AKEELARM---------LRE----YQELMSVKLALDIEIATYRKLLEG 533
Cdd:pfam05557 160 kqqsSLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREhnkhLNENIENKLLLKEEVEDLKRKLER 239
|
..
gi 694950035 534 EE 535
Cdd:pfam05557 240 EE 241
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
241-473 |
2.34e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 241 DKVRFLEQQNKVLETKWNLLQQQTTTtssknleplFETYLSVLRKQLDtlgNDKGRLQSELKTMQDSVEDFKTkyeeEIN 320
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKA----EIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 321 KRTAAENDFVVLKKDVDAAY----MNKVELEAKVDSLNDEINFLKvlydaELSQMQTHVSDTSvvlsmdnnrnlDLDSII 396
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDRI 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 397 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD 473
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTA--IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
217-532 |
2.42e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASF---IDKVRFLEQQNKVLETKWNLLQQQTTTTSSKNLEPLFETYlSVLRKQLDTLGND 293
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 294 KGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDF--------VVLKKDVDAAYMNKVEL------------------- 346
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIagvlflvlgllallfllla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 347 --EAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ 424
Cdd:COG4717 295 reKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 425 LQISVD-----------QHGDNLKNTKSEIAELNRMIQRLRAEI---------ENIKKQCQTLQASVADAEQRgenaLKD 484
Cdd:COG4717 375 LLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEE----LEE 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 694950035 485 AHSKRVELEAALQQAKE--ELARMLREYQELMSVKLALDIEIATYRKLLE 532
Cdd:COG4717 451 LREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
283-522 |
2.64e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflkv 362
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN---- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 363 lydaelsQMQTHVSDTSVVLsmDNNRNL---------DLDSIIAE---VRAQYEEiaQRSKAEAEAL-YQTKVqqlqISV 429
Cdd:pfam01576 577 -------RLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEAReKETRA----LSL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 430 DQHGDNLKNTKSEIAELNRMiqrLRAEIENIkkqcqtlqasVADAEQRGENALKDAHSKRVeLEAALQQAKEELARMLRE 509
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQ---LRAEMEDL----------VSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELEDE 707
|
250
....*....|...
gi 694950035 510 YQELMSVKLALDI 522
Cdd:pfam01576 708 LQATEDAKLRLEV 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
276-535 |
4.47e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 276 FETYLSVLRKQLDTLGNDKGRLQsELKTMQDSVEDFKtkYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLND 355
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 356 EINFLKVLydaeLSQMQTHVSDtsvvlsMDNNRNLDLDSIIAEVRAqyeEIAQRSKAEAEalYQTKVQQLQisvdqhgDN 435
Cdd:TIGR02169 266 RLEEIEQL----LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDAE-------ER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 436 LKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGE-------------NALKDAHSKRVEleaALQQAKEE 502
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefAETRDELKDYRE---KLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|...
gi 694950035 503 LARMLREYQELMSVKLALDIEIATYRKLLEGEE 535
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
365-505 |
5.86e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 365 DAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEI-AQRSK--------AEAEALYQTKVQQLQISVDqhgdn 435
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRlqallaelAGAGAAAEGRAGELAQELD----- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 436 lkNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELAR 505
Cdd:PRK09039 127 --SEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-529 |
7.23e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 285 KQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKvly 364
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 365 dAELSQMQTHVSDTSVVLSMDNNRN-LDL-----DSIIAEVRAQY-EEIAQRSKAEAEALYQTKVQqlqisvdqhgdnlk 437
Cdd:COG4942 97 -AELEAQKEELAELLRALYRLGRQPpLALllspeDFLDAVRRLQYlKYLAPARREQAEELRADLAE-------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 438 ntkseiaelnrmIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVK 517
Cdd:COG4942 162 ------------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 694950035 518 LALDIEIATYRK 529
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
391-513 |
8.56e-06 |
|
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: 47.23 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 391 DLDSIIAEVRAQYEEI------AQRSKAEAEALYQTKVQQLQISVDQHGdNLKNTK------SEIAELNRMIQRLRAEIE 458
Cdd:COG1579 35 ELEDELAALEARLEAAkteledLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKeyealqKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 694950035 459 NIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-532 |
8.60e-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: 48.86 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 218 IQKVRTEEREQIKLLNNKFasfidkvRFLEQQNKVLETKwnllqqqtTTTSSKNLEPLFETyLSVLRKQLDTLGNDKGRL 297
Cdd:TIGR04523 59 LDKNLNKDEEKINNSNNKI-------KILEQQIKDLNDK--------LKKNKDKINKLNSD-LSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 298 QSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEI-NFLKVLYDA--ELSQMQTH 374
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlNIQKNIDKIknKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 375 VSdtsvVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALYQTKVQQLQISVDQHGDN----------LKN 438
Cdd:TIGR04523 203 LS----NLKKKIQKNKSLESQISELKKQNNQLKdniekkQQEINEKTTEISNTQTQLNQLKDEQNKIkkqlsekqkeLEQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 439 TKSEIAELNRMIQRLRAEIENIKKQ-CQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVK 517
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
330
....*....|....*
gi 694950035 518 LALDIEIATYRKLLE 532
Cdd:TIGR04523 359 SEKQRELEEKQNEIE 373
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
279-490 |
1.05e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 279 YLSVLRKQLDTLGndkgRLQSELKTMQDSVEDFKTKYEEEINKRtaAENDFVVLKKDVDAaYMNKV-ELEAKVDSLNDEI 357
Cdd:PRK05771 51 LLTKLSEALDKLR----SYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEKIEKEIKE-LEEEIsELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 358 NFLKVL--YDAELSQMQTHvSDTSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQTK---V 422
Cdd:PRK05771 124 ERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgF 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694950035 423 QQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADA----EQRGENALKDAHSKRV 490
Cdd:PRK05771 203 ERLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
283-535 |
1.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLGNDKGR------LQSELKTMQDSV-----EDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVD 351
Cdd:COG1196 198 LERQLEPLERQAEKaeryreLKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 352 SLNDEINflkvlydaelsQMQthvsdtsvvlsmdnNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqtkvQQLQISVDQ 431
Cdd:COG1196 278 ELELELE-----------EAQ--------------AEEYELLAELARLEQDIARLEERRRELEERL-----EELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 432 HGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARmLREYQ 511
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELE 406
|
250 260
....*....|....*....|....
gi 694950035 512 ELMSVKLALDIEIATYRKLLEGEE 535
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEAL 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
224-546 |
1.40e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 224 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSKNLEPL-FETYLSVLRKQLDTLGNDKGRLQSELK 302
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 303 TMQdsVEdfKTKYEEEINKRTAAENDFVVLKKDVDAAYMnkvELEAKVDSLNDEinflKVLYDAELSQMQTHVSDT---- 378
Cdd:pfam15921 587 AMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELE----KVKLVNAGSERLRAVKDIkqer 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 379 -SVVLSMDNNRNlDLDSIIAEvraqYEEIAQRSKAEAEALYQT------KVQQLQISVDQHGDNLKNTKSEIAELNRMIQ 451
Cdd:pfam15921 656 dQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEEMETTtnklkmQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 452 RLRAEIENIKKQCQTLQASVADAEQRGENALKDAH---SKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYR 528
Cdd:pfam15921 731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
330
....*....|....*...
gi 694950035 529 KLLEGEEYRMSgECQSAV 546
Cdd:pfam15921 811 VALDKASLQFA-ECQDII 827
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
325-529 |
1.80e-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: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 325 AENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYD---AELSQMQTHVSDTsvvlsmdnnrNLDLDSIIAEVRA 401
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 402 QYEEIAQRskaeAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRM----------IQRLRAEIENIKKQCQTLQASV 471
Cdd:COG3883 84 RREELGER----ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIadadadlleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694950035 472 ADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK 529
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-529 |
2.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 392 LDSIIAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGD---------NLKNTKSEIAELNRMIQRLRAEIENIKK 462
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQEL--KEELEELEEQLEELLGeleellealDEEELEEELEELEEELEELEEELEELRE 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 463 QCQTLQASVADAEQRGENAlkdahskrvELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK 529
Cdd:COG4717 454 ELAELEAELEQLEEDGELA---------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
217-517 |
3.66e-05 |
|
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: 47.02 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASfidkvrfLEQQNKVLETKWNLLQQQttttssKNLEPLFETyLSVLRKQLDTLgndkgr 296
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEK------KQFEKIAEE-LKGKEQELIFL------ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 297 LQSELKTMQD-SVEDFKTKYEEEINKRTAAEndfvvLKKDVDAAYMNKVELEAKVDSLndeinflkVLYDAELSQmqtHV 375
Cdd:pfam05483 445 LQAREKEIHDlEIQLTAIKTSEEHYLKEVED-----LKTELEKEKLKNIELTAHCDKL--------LLENKELTQ---EA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 376 SDTSVVLSM---DNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ---LQISVDQHGDNLKNTKSEIAELNRM 449
Cdd:pfam05483 509 SDMTLELKKhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694950035 450 IQRLRAEIENIKKQCQTLQASVADAEQRGEnALK---DAHSKRV--------ELEAALQQAKEELARMLREYQELMSVK 517
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENK-ALKkkgSAENKQLnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-535 |
5.79e-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: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 391 DLDSIIAEVRAQYEEIAQRSKAEAEALYQT----KVQQLQISVDQHGD---NLKNTKSEIAELNRMIQRLRAEIENIKKQ 463
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSwdeiDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694950035 464 CQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLRE-YQELM------SVKLALDIEIATYRKLLEGEE 535
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALgdaverELRENLEERIDALRARLNRAE 786
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-514 |
6.36e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 222 RTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSKNLEPlfETYLSVLRKQLDTLGNDKGRLQSEL 301
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH--EARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 302 KTMQDSVEDF-KTKYEEEINKRT------AAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYD------AEL 368
Cdd:pfam07888 153 ERMKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeAEN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 369 SQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVraqyeeIAQRSKAEAEaLYQTKVQQLQISVD----------------QH 432
Cdd:pfam07888 233 EALLEELRSLQERLNASERKVEGLGEELSSM------AAQRDRTQAE-LHQARLQAAQLTLQladaslalregrarwaQE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 433 GDNLKNT----KSEIAELNRMIQRLRAEIENIKKQCQTLQASVAdaEQRGENALKDAHSKR--VELEAALQQAKEELARM 506
Cdd:pfam07888 306 RETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELG--REKDCNRVQLSESRRelQELKASLRVAQKEKEQL 383
|
....*...
gi 694950035 507 LREYQELM 514
Cdd:pfam07888 384 QAEKQELL 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
391-518 |
8.99e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 391 DLDSIIAEVRAQYEEIAQrSKAEAEALyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQAS 470
Cdd:COG4372 53 ELEQAREELEQLEEELEQ-ARSELEQL-EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 694950035 471 ---VADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKL 518
Cdd:COG4372 131 rkqLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
397-504 |
1.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 397 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHgDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQAS-VADAE 475
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETR 115
|
90 100 110
....*....|....*....|....*....|
gi 694950035 476 QRGENA-LKDAHSKRVELEAALQQAKEELA 504
Cdd:PRK11281 116 ETLSTLsLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-533 |
1.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 320 NKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLkvlyDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEV 399
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 400 RAQYEEIAQRSKAEAEALYQTKvQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAE---Q 476
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaerA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 477 RGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG 533
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-532 |
1.39e-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: 45.05 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLgndkgRLQSELktmqdsVEDFKTKYEEEINKrtaaendfvvlkkDVDAAYMNKVELEAKVDSLNDEINFLKV 362
Cdd:TIGR02168 198 LERQLKSL-----ERQAEK------AERYKELKAELREL-------------ELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 363 LYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALyQTKVQQLQISVDQHGDNL 436
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANL-ERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 437 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRG---ENALKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250
....*....|....*....
gi 694950035 514 MSVKLALDIEIATYRKLLE 532
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLE 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-539 |
1.40e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEeinkrtaAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEInflkv 362
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 363 lydAELSQMQTHVsdtsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRskaEAEALYQTKVQQLQISVDQHGDNLKNTKSE 442
Cdd:TIGR02169 754 ---ENVKSELKEL----------EARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 443 IAELNRMIQR---LRAEIENIKKQCQTLQASVADAEQRGEN---ALKDAHSKRVELEAALQQAKEELARMLREYQELMSV 516
Cdd:TIGR02169 818 EQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260
....*....|....*....|...
gi 694950035 517 KLALDIEIATYRKLLEGEEYRMS 539
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLS 920
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-521 |
1.40e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 286 QLDTLGND-KGRLQSELKTMQDSVEDFKTKYEEEIN----KRTAAENDFVVLK----------KDVDAAYMNKV-ELEAK 349
Cdd:pfam15921 246 QLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITglteKASSARSQANSIQsqleiiqeqaRNQNSMYMRQLsDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 350 VDSLNDEINFLKVLYDAELSQMQTHVsdtsvVLSmdnnrnldlDSIIAEVRAQYEEIAQRSKAEAEALYQ------TKVQ 423
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQL-----VLA---------NSELTEARTERDQFSQESGNLDDQLQKlladlhKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 424 QLQISVDQH--------GDNLK--NTKSEIAELNRMIQRLRAEIENIKKQCQTlQASVADAEQRGENalkDAHSKRVELE 493
Cdd:pfam15921 392 ELSLEKEQNkrlwdrdtGNSITidHLRRELDDRNMEVQRLEALLKAMKSECQG-QMERQMAAIQGKN---ESLEKVSSLT 467
|
250 260
....*....|....*....|....*...
gi 694950035 494 AALQQAKEELARMLreyQELMSVKLALD 521
Cdd:pfam15921 468 AQLESTKEMLRKVV---EELTAKKMTLE 492
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
390-507 |
1.51e-04 |
|
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: 42.89 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 390 LDLDSIIAEVRAqyeeiAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 469
Cdd:pfam02321 69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143
|
90 100 110
....*....|....*....|....*....|....*...
gi 694950035 470 SVADAEQrGENALKDAHSKRVELEAALQQAKEELARML 507
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
223-516 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 223 TEEREQIKLLN---NKFASFI----DKVRFLEQQNKVLETKWNLLQQQTTTTSSKNLEplfetylsvLRKQLDTLGNDKG 295
Cdd:pfam01576 169 AEEEEKAKSLSklkNKHEAMIsdleERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE---------LQAQIAELRAQLA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 296 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKvlydaelsqmqTHV 375
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK-----------TEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 376 SDTsvvlsmdnnrnldLDSIIA--EVRAQYE-EIAQRSKA-EAEA-LYQTKVQQLQI----SVDQHGDNLKNTKSEIAEL 446
Cdd:pfam01576 309 EDT-------------LDTTAAqqELRSKREqEVTELKKAlEEETrSHEAQLQEMRQkhtqALEELTEQLEQAKRNKANL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694950035 447 NRMIQRLRAEIENIKKQCQTLQASVADAEQR---GENALKDAHSKRVELEAALQQAKEELARMLREYQELMSV 516
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-477 |
1.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQttttssknleplfetyLSVLRKQLDTLGNDKGR 296
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 297 LQSELKTMQDsvedfktkyeeeinkrtaaendfvVLKKDVDAAYMNkveleakvdSLNDEINFLkvLYDAELSQMQTHVS 376
Cdd:COG4942 95 LRAELEAQKE------------------------ELAELLRALYRL---------GRQPPLALL--LSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 377 DTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQR--SKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLR 454
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAEraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|...
gi 694950035 455 AEIENIKKQCQTLQASVADAEQR 477
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
267-513 |
1.72e-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: 43.37 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 267 TSSKNLEPLFEtyLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEeinkrtaaendfvvLKKDVDAAYMNKVEL 346
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEA--------------AKTELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 347 EAKVDSLNDEInflkvlydAELSQMQTHVSdtsvvlsmdNNRnlDLDSIIAEVraqyeEIAQRSKAEAEalyqtkvqqlq 426
Cdd:COG1579 65 ELEIEEVEARI--------KKYEEQLGNVR---------NNK--EYEALQKEI-----ESLKRRISDLE----------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 427 isvdqhgdnlkntkSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEEL-AR 505
Cdd:COG1579 110 --------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPE 175
|
....*...
gi 694950035 506 MLREYQEL 513
Cdd:COG1579 176 LLALYERI 183
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
217-513 |
2.29e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKwnlLQQQTTTTSSKNleplfetYLSVlRKQLDTLGNDKGR 296
Cdd:pfam06160 122 EVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEE---FSQFEELTESGD-------YLEA-REVLEKLEEETDA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 297 LQSELKTMQDSVEDFKTKYEEEINkrtaaendfvvlkkdvdaaymnkvELEAKVDSL-NDEINFLKVLYDAELSQMQTHV 375
Cdd:pfam06160 191 LEELMEDIPPLYEELKTELPDQLE------------------------ELKEGYREMeEEGYALEHLNVDKEIQQLEEQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 376 SDTSVVLSmdnnrNLDLDSIIAEVRAQYEEIAQ-----RSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELN--- 447
Cdd:pfam06160 247 EENLALLE-----NLELDEAEEALEEIEERIDQlydllEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQqsy 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 448 ----RMIQRLR---AEIENIKKQCQTLQASVADAEQ----------RGENALKDAHSKRVELEAALQ-------QAKEEL 503
Cdd:pfam06160 322 tlneNELERVRgleKQLEELEKRYDEIVERLEEKEVayselqeeleEILEQLEEIEEEQEEFKESLQslrkdelEAREKL 401
|
330
....*....|
gi 694950035 504 ARMLREYQEL 513
Cdd:pfam06160 402 DEFKLELREI 411
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
214-532 |
2.66e-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: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 214 IDPEIQKVRTEEREQIKLLNNKFAsfiDKVRFLEQQNKVLETkwNLLQQQTTTTSSKN-LEPLFETYLSVLRKQLDTLGN 292
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQ---DRIEQLISEHEVEIT--GLTEKASSARSQANsIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 293 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflKVLydAELSQMQ 372
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQ--KLL--ADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 373 THVS------------DTSVVLSMDNNRNlDLDSIIAEVRaQYEEIAQRSKAEAealyQTKVQQLQISVDQHGDNLKNTK 440
Cdd:pfam15921 391 KELSlekeqnkrlwdrDTGNSITIDHLRR-ELDDRNMEVQ-RLEALLKAMKSEC----QGQMERQMAAIQGKNESLEKVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 441 SEIAELNRMIQRLRAEIENIKKQCQTLQAS---VAD---AEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELM 514
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544
|
330 340
....*....|....*....|.
gi 694950035 515 SVKL---ALDIEIATYRKLLE 532
Cdd:pfam15921 545 NVQTeceALKLQMAEKDKVIE 565
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
298-463 |
2.93e-04 |
|
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: 43.02 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 298 QSELKTMQDSVEDFKTKYEEEINKrtaaendfvvLKKDVDaaymnkvELEAKVDSLNDEINFLKVLYDAE-------LSQ 370
Cdd:pfam15397 62 KKQLQQAKAELQEWEEKEESKLNK----------LEQQLE-------QLNAKIQKTQEELNFLSTYKDKEypvkavqIAN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 371 MQTHVSDTSvvlsmDNNRN--LDLDSIIAEVRAQYEEIAQRSK--------AEAEALYQTKVQQLQIS-------VDQHG 433
Cdd:pfam15397 125 LVRQLQQLK-----DSQQDelDELEEMRRMVLESLSRKIQKKKekilsslaEKTLSPYQESLLQKTRDnqvmlkeIEQFR 199
|
170 180 190
....*....|....*....|....*....|
gi 694950035 434 DNLKNTKSEIAELNRMIQRLRAEIENIKKQ 463
Cdd:pfam15397 200 EFIDELEEEIPKLKAEVQQLQAQRQEPREV 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-513 |
3.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 392 LDSIIAEVRAQYEEIAQRSKA-----EAEALYQtKVQQLQISVDQHGDNLKNTKSEIAElnrmIQRLRAEIENIKKQCQT 466
Cdd:COG4717 100 LEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAE 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 694950035 467 LQASVADAEQRG----ENALKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:COG4717 175 LQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
296-509 |
4.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 296 RLQSELKTMQDSVEDFKTKYEEEINKRTAAE----------NDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYD 365
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 366 aELSQMQTHVSDTSVVLSMDNN----RNLDLDSIIAEVRAQYEEI---AQRSKAEAEALYQtKVQQLQISVDQHGDNLKN 438
Cdd:PRK02224 290 -ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLRE-DADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 439 TKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENA----------LKDAHSKRVELEAALQQAKEEL--ARM 506
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAedfleelreeRDELREREAELEATLRTARERVeeAEA 447
|
...
gi 694950035 507 LRE 509
Cdd:PRK02224 448 LLE 450
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
397-512 |
4.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 397 AEVRAQYEEIAQRSKAEAE--------ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ 468
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 694950035 469 ASvadAEQRGEN--ALKDAHSKRVELEAALQQAKEELARMLREYQE 512
Cdd:PRK12704 138 EE---QLQELERisGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
199-529 |
4.69e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 199 EVTINQSLLTPLHVEIDPEIQKVRTEEREQIKLLNNK--FASFIDKVRF--------------LEQQNKVLETKWNLLQQ 262
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlnIQKNIDKIKNkllklelllsnlkkKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 263 QTTTtssknleplfetylsvLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMN 342
Cdd:TIGR04523 226 QNNQ----------------LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 343 KVELEAKVDSLND--EINFLKVLYDaELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYE--EIAQRSKAEAEALY 418
Cdd:TIGR04523 290 LNQLKSEISDLNNqkEQDWNKELKS-ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 419 QTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENaLKdahSKRVELEAALQQ 498
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LK---ETIIKNNSEIKD 444
|
330 340 350
....*....|....*....|....*....|.
gi 694950035 499 AKEELARMLREYQELMSVKLALDIEIATYRK 529
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
273-512 |
5.24e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 273 EPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTK-YEEEINK--------RTAAEND---FVVLKKDVDAAY 340
Cdd:cd22656 25 EEEYRKRLGISSDIDDKLSSDFDPLLDAYKSIKDHCTDFKDDtYPSIVSLagdiynyaQNAGGTIdsyYAEILELIDDLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 341 MNKVELEAK---------VDSLNDEIN---------------FLKVLyDAELSQMQTHVSDTSVVLSMDNNRNL--DLDS 394
Cdd:cd22656 105 DATDDEELEeakktikalLDDLLKEAKkyqdkaakvvdkltdFENQT-EKDQTALETLEKALKDLLTDEGGAIArkEIKD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 395 IIAEVRAQYEEIAQRSKAEAEAL------YQTKVQ---QLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQ 465
Cdd:cd22656 184 LQKELEKLNEEYAAKLKAKIDELkaliadDEAKLAaalRLIADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLD 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 694950035 466 TLQASVADAEQrgenALKDAHSKRVELEAAlQQAKEELARMLREYQE 512
Cdd:cd22656 264 SLKDLLEDDIS----KIPAAILAKLELEKA-IEKWNELAEKADKFRQ 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-508 |
5.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLGNDKGRLQSELKTMQDSVEdfktkyeEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKV 362
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELE-------EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 363 LYDA-----ELSQMQTHVSdtsvvlsmdnnrnlDLDSIIAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLK 437
Cdd:COG4717 124 LLQLlplyqELEALEAELA--------------ELPERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694950035 438 N-TKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGEnalkdahskRVELEAALQQAKEELARMLR 508
Cdd:COG4717 188 LaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE---------QLENELEAAALEERLKEARL 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
438-535 |
5.57e-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: 43.12 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 438 NTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKR---VELEAALQQAKEELARMLREYQELM 514
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLS 753
|
90 100
....*....|....*....|.
gi 694950035 515 SVKLALDIEIATYRKLLEGEE 535
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAE 774
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
227-467 |
6.77e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.86 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 227 EQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSKNleplfeTYLSVLRKQLDTLGNDkgrLQSELKTMQd 306
Cdd:pfam09728 18 EKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSEL------SKAILAKSKLEKLCRE---LQKQNKKLK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 307 svEDFKTKYEEEINKRTAAENDFVVLKKDVDAaYMNKVElEAKVDSLNDEINF---LKVLYD-AELSQMQTHvsdtsvvl 382
Cdd:pfam09728 88 --EESKKLAKEEEEKRKELSEKFQSTLKDIQD-KMEEKS-EKNNKLREENEELrekLKSLIEqYELRELHFE-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 383 SMdnNRNLDLDSIIAEVRAQYEEIA-QRSKAEAEAL----YQTKVQQL---------QISVdqHGDNLKNTKSEIAELNR 448
Cdd:pfam09728 156 KL--LKTKELEVQLAEAKLQQATEEeEKKAQEKEVAkareLKAQVQTLsetekelreQLNL--YVEKFEEFQDTLNKSNE 231
|
250
....*....|....*....
gi 694950035 449 MIQRLRAEIENIKKQCQTL 467
Cdd:pfam09728 232 VFTTFKKEMEKMSKKIKKL 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-503 |
7.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 283 LRKQLDTLGndkgRLQSELKTMQDSVE---DFKTKYEE-EINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEIN 358
Cdd:COG4913 230 LVEHFDDLE----RAHEALEDAREQIEllePIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 359 FLkvlyDAELSQMQTHVSDT-----SVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalYQTKVQQLQISVDQHG 433
Cdd:COG4913 306 RL----EAELERLEARLDALreeldELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR--LEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 434 DNLKNTKSEIAELNRMIQRLRAEIEN-----------IKKQCQTLQASVADAEQRGENALKDAHSKRVELEAALQQAKEE 502
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEalaeaeaalrdLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
.
gi 694950035 503 L 503
Cdd:COG4913 460 L 460
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
297-505 |
7.56e-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: 42.85 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 297 LQSELKTMQDSVEDFKTKYEEEINKRTAAEndfvvlkkdvdaayMNKVELEAKVDSLNDEINFLKVLYDA---ELSQMQT 373
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--------------LEKVTTEAKIKKLEEDILLLEDQNSKlskERKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 374 HVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqtkvQQLQISVDQHGDNLKNTKSEIAELNRMIQRL 453
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGR-----QELEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 694950035 454 RAEIENIKKQCQTLQASVADAEQRGENALKdahsKRVELEAALQQAKEELAR 505
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALK----KIRELEAQISELQEDLES 282
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
404-532 |
8.95e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 404 EEIAQRSKAEAEALyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRgenaLK 483
Cdd:COG4372 30 SEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE----LE 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 694950035 484 DAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 532
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
339-535 |
1.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 339 AYMNKVeLEAKVDSLNDEINFLKVLYDAELSQMQTHvsdtsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAlY 418
Cdd:PHA02562 166 SEMDKL-NKDKIRELNQQIQTLDMKIDHIQQQIKTY-----------NKNIEEQRKKNGENIARKQNKYDELVEEAKT-I 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 419 QTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ---------CQTLQASVADAEQRgenaLKDAHSKR 489
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvCPTCTQQISEGPDR----ITKIKDKL 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694950035 490 VELEAALQQAK---EELARMLREYQELMSVKLALDIEIATYRKLLEGEE 535
Cdd:PHA02562 309 KELQHSLEKLDtaiDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-509 |
1.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 213 EIDPEIQKVRTEEREQIKLLNNKfaSFIDKVRFLEQQNKVLETKwnllqqqtttTSSKNLEPLFETY--LSVLRKQLDTL 290
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEK----------LKKYNLEELEKKAeeYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 291 GNDKGRLQSELKtmqdSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaymnkvELEAK----VDSLNDEINFLKVLYDA 366
Cdd:PRK03918 538 KGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLK----------ELEELgfesVEELEERLKELEPFYNE 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 367 ELSqmqthVSDTSVVLSMDNNRnldLDSIIAEVRAQYEEIAqRSKAEAEALyQTKVQQLQISVDQhgDNLKNTKSEIAEL 446
Cdd:PRK03918 604 YLE-----LKDAEKELEREEKE---LKKLEEELDKAFEELA-ETEKRLEEL-RKELEELEKKYSE--EEYEELREEYLEL 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694950035 447 NRMIQRLRAEIENIKKQCQTLQASVADAEQRgenaLKDAHSKRVELEaALQQAKEELARmLRE 509
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELE-KLEKALERVEE-LRE 728
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
407-512 |
1.41e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.20 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 407 AQRSKAEAEALyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLqasvadaeqrgENALKDAH 486
Cdd:pfam10473 47 AENSKAEVETL-KAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSL-----------ENLLEEKE 114
|
90 100
....*....|....*....|....*.
gi 694950035 487 SKRVELEAALQQAKEELARMLREYQE 512
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQLKELNE 140
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
388-543 |
1.66e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.04 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 388 RNLDLDSIIAE---VRAQYEEIAQRSKAEAEAlyqtKVQQLQISVDQHGDNLKNTKSEIAELNR-------MIQRLRAEI 457
Cdd:pfam05010 37 ENLEMRKIVAEfekTIAQMIEEKQKQKELEHA----EIQKVLEEKDQALADLNSVEKSFSDLFKryekqkeVISGYKKNE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 458 ENIKKQCQTLQASVADAEQRGEnALKdAHSkrvelEAALQQAKEELARMLREYQElmsvklaldiEIATYRKLLEGEEYR 537
Cdd:pfam05010 113 ESLKKCAQDYLARIKKEEQRYQ-ALK-AHA-----EEKLDQANEEIAQVRSKAKA----------ETAALQASLRKEQMK 175
|
....*..
gi 694950035 538 M-SGECQ 543
Cdd:pfam05010 176 VqSLERQ 182
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
388-535 |
1.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 388 RNLDLDSIIAEVRAQY--EEIAQRSKAEAEALYQTKVQQLQISVDQhgdNLKNTKSEIAELNRMIQRLRAEIEnikkqcq 465
Cdd:COG2433 361 PDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVE------- 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 466 TLQASVADAEQRGEnalkdahskrvELEAALQQAKEELARMLREYQELMsvklALDIEIATYRKLLEGEE 535
Cdd:COG2433 431 ELEAELEEKDERIE-----------RLERELSEARSEERREIRKDREIS----RLDREIERLERELEEER 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-460 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 217 EIQKVRTEEREQIKLLNNKFASFIDkvRFLEQQNKVLETKWNLLQQQTTTTSSknleplfETYLSVLRKQLDTLGNDKGR 296
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESL-------ERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 297 LQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLkvlyDAELSQMQTHVS 376
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL----RRELEELREKLA 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 377 DTSVVLSMDNNRnldLDSIIAEVRAQYEEIAQrskaEAEALYQTKVqqlqisvdqhgdnlkntkSEIAELNRMIQRLRAE 456
Cdd:TIGR02168 926 QLELRLEGLEVR---IDNLQERLSEEYSLTLE----EAEALENKIE------------------DDEEEARRRLKRLENK 980
|
....
gi 694950035 457 IENI 460
Cdd:TIGR02168 981 IKEL 984
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
248-505 |
1.96e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 248 QQNKVLETKWNLLQQQTTTTSSKNLEplFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEeinkrtaaen 327
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQR--AEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE---------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 328 dfvvLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQyeeia 407
Cdd:pfam19220 200 ----LETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQ----- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 408 QRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRM---IQRLRAEIEN----IKKQCQTLQASVADAEQRGEN 480
Cdd:pfam19220 271 LRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQfqeMQRARAELEEraemLTKALAAKDAALERAEERIAS 350
|
250 260 270
....*....|....*....|....*....|..
gi 694950035 481 -------ALKDAHSKRVELEAALQQAKEELAR 505
Cdd:pfam19220 351 lsdriaeLTKRFEVERAALEQANRRLKEELQR 382
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
385-512 |
2.00e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 385 DNNRNlDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISvdQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQC 464
Cdd:PRK11637 43 SDNRD-QLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAIS--QASRKLRETQNTLNQLNKQIDELNASIAKLEQQQ 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694950035 465 QTLQASVA---DA------------------EQRGE------NALKDAHSKRVEleaALQQAKEELARMLREYQE 512
Cdd:PRK11637 120 AAQERLLAaqlDAafrqgehtglqlilsgeeSQRGErilayfGYLNQARQETIA---ELKQTREELAAQKAELEE 191
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
213-546 |
2.30e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 213 EIDPEIQKVRTEERE-QIKL--LNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSSKNLEPlfETYLSVLRKQLDT 289
Cdd:pfam10174 293 QLKQELSKKESELLAlQTKLetLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEK--ESFLNKKTKQLQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 290 LGNDKGRLQSELKTMQDSVeDFKtkyEEEINkrtaaendfvVLKKdvdaaymnkvELEAKVDSLNDEINFLKVLYDAeLS 369
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDML-DVK---ERKIN----------VLQK----------KIENLQEQLRDKDKQLAGLKER-VK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 370 QMQTHVSDTSVVLSMdnnrnldldsiIAEVRAQYEEIAQRSKAEAEALYQTKVQQLqisvDQHGDNLKNTKSEIAELNRM 449
Cdd:pfam10174 426 SLQTDSSNTDTALTT-----------LEEALSEKERIIERLKEQREREDRERLEEL----ESLKKENKDLKEKVSALQPE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 450 IQRLRAEIENIKKQCQTLQASVADaeqrgenalKDAHSKrvELEAALQQAKEELARMLREYQELMSVKLA--LDIEIATY 527
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSGLK---------KDSKLK--SLEIAVEQKKEECSKLENQLKKAHNAEEAvrTNPEINDR 559
|
330 340
....*....|....*....|..
gi 694950035 528 RKLLEGEEYRM---SGECQSAV 546
Cdd:pfam10174 560 IRLLEQEVARYkeeSGKAQAEV 581
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
440-502 |
2.33e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 38.98 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694950035 440 KSEIAELNRMIQRLRAEIENIKKQcqtlqasvadAEQRGENALKDAHSKRVE--------LEAALQQAKEE 502
Cdd:COG0576 5 EAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLAEdllpvldnLERALAAAEED 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
398-533 |
2.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 398 EVRAQYEEIAQRSKAEAEALYQTKVQQLQI-SVDQHGDNLKNTKSEIAElnrMIQRLRAEIENIKKQCQTLQASVADAEQ 476
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAeAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEE 356
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 694950035 477 RGenalKDAHSKRVELEAALQQAKEElarmLREYQELMSvklALDIEIATYRKLLEG 533
Cdd:PRK02224 357 RA----EELREEAAELESELEEAREA----VEDRREEIE---ELEEEIEELRERFGD 402
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
445-506 |
3.09e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 3.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694950035 445 ELNRMIQRLRAEIENIKKQCQTLQASVADAEQR---GENALKDAHSKRVELEAALQQAKEELARM 506
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
346-530 |
3.63e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.34 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 346 LEAKVDSLNDEINFLKVLYDAELSQMQT----------------HVSDT-SVVLSMDNNRNLDLDSIIAEVRAQYEEIA- 407
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIaqqkeskflenlaslkHENDNlSSMLNRKERRLKDLEDQLSELKNSYEELTe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 408 ---------QRSKAEAEALYQtKVQQLQIS----VDQHGDNLKNTKSEIAELNRMIQRLRAEIEnikKQCQTLQASVADA 474
Cdd:pfam17078 88 snkqlkkrlENSSASETTLEA-ELERLQIQydalVDSQNEYKDHYQQEINTLQESLEDLKLENE---KQLENYQQRISSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 694950035 475 EQRGENALKDAHSKRVELEAALQQAKEELARMLreyqELMSVKLALDIEIATYRKL 530
Cdd:pfam17078 164 DKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKL----DSLAQLLDLPSWLNLYPES 215
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
396-515 |
3.97e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 396 IAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKS-EIAELNRM--IQRLRAEIEN---IKKQCQTLQA 469
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEreEAELEADVRKpaeAEKQAAEAEA 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 694950035 470 SvADAEQRGENALKDAHSKRVELEAA----LQQAKEELARMLREYQELMS 515
Cdd:COG2268 326 E-AEAEAIRAKGLAEAEGKRALAEAWnklgDAAILLMLIEKLPEIAEAAA 374
|
|
| Prefoldin_alpha |
cd00584 |
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ... |
401-516 |
4.06e-03 |
|
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467468 [Multi-domain] Cd Length: 121 Bit Score: 37.59 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 401 AQYEEIaqrsKAEAEALyQTKVQQLQI---SVDQHGDNLKNTKSEIAELNRMIQR---LRAEIENIKKQCQTLQASVAdA 474
Cdd:cd00584 3 EQLQEL----REQIEAL-QEEIEQLEEeqaEIDEAKEALEELKKEGSEVLVPLGGnayVRAEVVDIDKVIVHLGLGYY-A 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 694950035 475 EQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSV 516
Cdd:cd00584 77 ERDPDGAIEILEKKEDELDKRIEELQAELAELEDEYDQLEQQ 118
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-532 |
4.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 222 RTEE-REQIKLLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTtttssKNLEPLFETyLSVLRKQLDTLGNDKGRLQSE 300
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-----KELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 301 LKTMQDSVEDFKTKYEEEINKRTAAENdfvvLKKDVDAaYmnkVELEAKVDSLNDEINFLKVL---YDAELSQMQTHVSD 377
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKE----LKEKAEE-Y---IKLSEFYEEYLDELREIEKRlsrLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 378 tsvvLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyQTKVQQLQISVDQHG---------------------DNL 436
Cdd:PRK03918 333 ----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGltpeklekeleelekakeeieEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 437 KNTKSEIAELNRMIQRLRAEIENIKK---QCQTLQASVADAEQrgENALKDAHSKRVELEAALQQAKEELARMLREYQEL 513
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330
....*....|....*....
gi 694950035 514 MSVkLALDIEIATYRKLLE 532
Cdd:PRK03918 486 EKV-LKKESELIKLKELAE 503
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
434-513 |
5.60e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 37.23 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 434 DNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALkDAHSKRVEleaALQQAKEELARMLREYQEL 513
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEDIK---ALQALREELNELKAEIAEL 76
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
434-519 |
6.15e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 39.64 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 434 DNLKNTKSEIA-----ELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENAL---KDAHSKRVELEAALQQAKEElAR 505
Cdd:pfam14817 65 DKGKAESRQSAaarrlELQKEIERLRAEISRLDKQLEARELELSREEAERERALdeiSDSRHRQLLLEAYDQQCEEA-RK 143
|
90
....*....|....
gi 694950035 506 MLREYQELMSVKLA 519
Cdd:pfam14817 144 ILAEDHQRLQGQLQ 157
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
434-532 |
6.76e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 434 DNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD-AEQRgenalkDAHSKRV-ELEAALQQAKEELARMLREYQ 511
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKElAEKR------DELNAQVkELREEAQELREKRDELNEKVK 74
|
90 100
....*....|....*....|.
gi 694950035 512 ELMSVKLALDIEIATYRKLLE 532
Cdd:COG1340 75 ELKEERDELNEKLNELREELD 95
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
419-504 |
7.57e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.94 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694950035 419 QTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQcqtLQASVADAEQRGENALKDAHSKRVELEAALQQ 498
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKE---LANAQAQALQTAQNNLATAQAALANAEARLAK 336
|
....*.
gi 694950035 499 AKEELA 504
Cdd:TIGR04320 337 AKEALA 342
|
|
| |
