|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
146-459 |
2.54e-146 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 423.18 E-value: 2.54e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 146 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTTtSVKNLEPFFEAYINALRKQVDSLANDKGRLQSELKI 225
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 226 MQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRVLYAAELSQMQTQVSDTSVVLS 305
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 306 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQ 385
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148356276 386 CQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLEGEECR 459
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-143 |
1.09e-31 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 119.76 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 14 GFSCGSAIVGGVKKAAFSSASMS------GGAGRCSSGGFGSRSLYNLGGNKSISISMA-GCRQGAGFGAAGGFGAAGGF 86
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAgGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148356276 87 GSGFGAGGFGSGFGGSFGG-------------------RGGAGFPVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 143
Cdd:pfam16208 81 GGFGGGGGGGFGGGGGFGGgfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-435 |
3.09e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 143 VRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTTtsVKNLEPFFEAYINALRKQVDSLANDKGRLQSE 222
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ--LRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 223 LKIMQDSVED---YKTKYEDEINKRAAAEndfvvlkkdvDAAYMNKVELEAKVDALNDEINFLRvlyaAELSQMQTQVSD 299
Cdd:TIGR02168 749 IAQLSKELTEleaEIEELEERLEEAEEEL----------AEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 300 TSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQ--QLQTSVDQHGDSLRNTKNEISELNRLIQRLRA 377
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148356276 378 EIENVKKQcqtlqgsvadaeqrgevaLKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:TIGR02168 895 ELEELSEE------------------LRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-457 |
4.17e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 135 EIDPE-IQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQT------TTTSVKNLEPFFEAY---INA 204
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 205 LRKQVDSLANDKGRLQSElKIMQDSVEDYKTKyeDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRV 284
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEK-IVDLKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 285 LYAAELSQMQTQVSDTSVVLSmdnnrNLDLDSIiaevRAQYEEIAQRSKAEAEALYQIKV---------QQLQTSVDQHG 355
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIgfpddksyiDKSIREIENEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 356 DSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGsVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL 707
|
330 340
....*....|....*....|..
gi 148356276 436 MSVKLALDIEIATYRKLLEGEE 457
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-443 |
1.66e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 202 INALRKQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINf 281
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 282 lrvLYAAELSQMQTQVSDTSVVLSmdnnrnlDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQLQTSVDQhgdslRNT 361
Cdd:COG1196 334 ---ELEEELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 362 KNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLA 441
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
..
gi 148356276 442 LD 443
Cdd:COG1196 479 LA 480
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
199-427 |
1.59e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 199 EAYINALRKQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDaaymnkvELEAKVDALNDE 278
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 279 I-NFLRVLYaaelsQMQTQVSDTSVVLSMDN-----NRNLDLDSIIAEVRAQYEEI--AQRSKAEAEALYQIKVQQLQTS 350
Cdd:COG3883 88 LgERARALY-----RSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148356276 351 VDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELAR 427
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-435 |
2.02e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 175 LETKWKLLQQQttttSVKNLEpfFEAYINALR-KQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVV 253
Cdd:TIGR02168 198 LERQLKSLERQ----AEKAER--YKELKAELReLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 254 LKKDVDAAYMNKVELEAKVDALNDEINFLRV---LYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQ 330
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQqkqILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 331 RSKAEAEAL----------------YQIKVQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVA 394
Cdd:TIGR02168 352 ELESLEAELeeleaeleelesrleeLEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 148356276 395 DA---EQRGEVA-----LKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:TIGR02168 432 EAelkELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDAA 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-454 |
2.32e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 267 ELEAKVDALNDEINFLRVLYA---AELSQMQTQVSDTSVVLSMDNNRnLDLDSIIAEVRAQYEEIAQRSKAEAEalyqik 343
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEaleAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 344 VQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVAL------------------- 404
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdavere 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148356276 405 --KDAYSKRTELEAALQKAKEELARVLREYQEL-MSVKLALDIEIAT---YRKLLE 454
Cdd:COG4913 767 lrENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-443 |
2.38e-06 |
|
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: 50.50 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 140 IQKVRTEEREQIKLLNNKFASFIDKVRFL--EQQNKVletkwKLLQQQTTTtSVKNLEPFFEAYINALRKQVDSLANDKG 217
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALksESQNKI-----ELLLQQHQD-RIEQLISEHEVEITGLTEKASSARSQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 218 RLQSELKIMQDSVEDYKTKYEDEINKraaAENDFVVLKKDVDAAymnKVELEAKVDALNDEInflrVLYAAELSQMQTQV 297
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSD---LESTVSQLRSELREA---KRMYEDKIEELEKQL----VLANSELTEARTER 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 298 SDTSvvlsmDNNRNLD--LDSIIAEVRAQYEEIAqrskAEAEALYQIKVQQLQTSVdqhgdSLRNTKNEISELNRLIQRL 375
Cdd:pfam15921 366 DQFS-----QESGNLDdqLQKLLADLHKREKELS----LEKEQNKRLWDRDTGNSI-----TIDHLRRELDDRNMEVQRL 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148356276 376 RAEIENVKKQCQ-TLQGSVADAEQRGEvalkdAYSKRTELEAALQKAKEELARVLreyQELMSVKLALD 443
Cdd:pfam15921 432 EALLKAMKSECQgQMERQMAAIQGKNE-----SLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLE 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
202-431 |
3.18e-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: 49.38 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 202 INALRKQVDSLANDKGRLQSELKimqdsvedyktKYEDEINKRAAAENDfvvLKKDVDAAYMNKVELEAKVDALNDEINF 281
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLA-----------ALERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 282 LRVLYAAELSQMQT--QVSDTSVVLSMDnnrnldlDSIIAEVRAQY-EEIAQRSKAEAEALyqikvQQLQTSVDQHGDSL 358
Cdd:COG4942 102 QKEELAELLRALYRlgRQPPLALLLSPE-------DFLDAVRRLQYlKYLAPARREQAEEL-----RADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148356276 359 RNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLRE 431
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
242-454 |
9.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 242 NKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRVLYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEV 321
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 322 RAQYEEIAQRSKAEAEALYQIkvQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGE 401
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148356276 402 VA---LKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLE 454
Cdd:TIGR02168 842 DLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-454 |
9.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 313 DLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQ----------QLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENV 382
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148356276 383 KKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLE 454
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
144-436 |
1.18e-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: 47.97 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 144 RTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTTTSVKNLEPffEAYINALRKQVDSLANDKGRLQSEL 223
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH--EARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 224 KIMQDSVE-------DYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRVLYA------AEL 290
Cdd:pfam07888 153 ERMKERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeAEN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 291 SQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVraqyeeIAQRSKAEAEaLYQIKVQQLQTSVD----------------QH 354
Cdd:pfam07888 233 EALLEELRSLQERLNASERKVEGLGEELSSM------AAQRDRTQAE-LHQARLQAAQLTLQladaslalregrarwaQE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 355 GDSLRNT----KNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLR 430
Cdd:pfam07888 306 RETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
....*.
gi 148356276 431 EYQELM 436
Cdd:pfam07888 386 EKQELL 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-454 |
1.19e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 268 LEAKVDALNDEINFLR---VLYAAELSQMQTQVSD---TSVVLSMDNNRNLDLDSIiAEVRAQYEEiAQRSKAEAEALYQ 341
Cdd:COG3206 166 LELRREEARKALEFLEeqlPELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 342 IKVQQLQTSVDQHGDSLRNT-----KNEISELNR--------------LIQRLRAEIENVKKQcqtLQGSVADAEQRGEV 402
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviqqlRAQLAELEAelaelsarytpnhpDVIALRAQIAALRAQ---LQQEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148356276 403 ALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLE 454
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-457 |
1.34e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 313 DLDSIIAEVRAQYEEIAQRSKAEAEAL----YQIKVQQLQTSVDQHGD---SLRNTKNEISELNRLIQRLRAEIENVKKQ 385
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAeyswDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148356276 386 CQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLRE-YQELM------SVKLALDIEIATYRKLLEGEE 457
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALgdaverELRENLEERIDALRARLNRAE 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
310-454 |
1.46e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 310 RNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQIK-----VQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKK 384
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELEeltaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 385 QCQTLQGSVADAEQRgevaLKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLE 454
Cdd:TIGR02168 303 QKQILRERLANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-461 |
2.00e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 318 IAEVRAQYEEIAQR---SKAEAEALYQiKVQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVA 394
Cdd:TIGR02168 679 IEELEEKIEELEEKiaeLEKALAELRK-ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148356276 395 DAEQRGEV----------ALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLEGEECRMS 461
Cdd:TIGR02168 758 ELEAEIEEleerleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
289-427 |
2.34e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 289 ELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEiAQRSKAEAEALYQIK---VQQLQTSVDQHGDSLRNTKNEI 365
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELagaGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148356276 366 SELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELAR 427
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-451 |
2.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 204 ALRKQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLR 283
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 284 vlyaAELSQMQTQVSDTSVVLSMdNNRNLDLDSIIAevraqyeeiaQRSKAEAEALYQIkVQQLQTSVDQHGDSLRNTKN 363
Cdd:COG4942 97 ----AELEAQKEELAELLRALYR-LGRQPPLALLLS----------PEDFLDAVRRLQY-LKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 364 EIselnrliQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALD 443
Cdd:COG4942 161 EL-------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*...
gi 148356276 444 IEIATYRK 451
Cdd:COG4942 234 AEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-451 |
3.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 314 LDSIIAEVRAQYEEIAQRSKAEAEALYQIK--VQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQG 391
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148356276 392 SVADAEQRGEVALKDAYS---KRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRK 451
Cdd:TIGR02168 324 QLEELESKLDELAEELAEleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-448 |
3.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 274 ALNDEINFLRV-LYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAL--YQIKVQQLQTS 350
Cdd:COG1196 217 ELKEELKELEAeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 351 VDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRgevaLKDAYSKRTELEAALQKAKEELARVLR 430
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEA 372
|
170
....*....|....*...
gi 148356276 431 EYQELMSVKLALDIEIAT 448
Cdd:COG1196 373 ELAEAEEELEELAEELLE 390
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
163-415 |
3.90e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 163 DKVRFLEQQNKVLETKWKLLQQQTTTtsvknlepfFEAYINALRKQVDslaNDKGRLQSELKIMQDSVEDYKTkyedEIN 242
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKA----EIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 243 KRAAAENDFVVLKKDVDAAY----MNKVELEAKVDALNDEINFLRvlYAAELSQMQTQVSDTsvvlsmdnnrnldlDSII 318
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEG--------------PDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 319 AEVRAQYEEIAQRSKAEAEAlyQIKVQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEq 398
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTA--IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA- 378
|
250 260
....*....|....*....|..
gi 148356276 399 rGEVA-----LKDAYSKRTELE 415
Cdd:PHA02562 379 -EELAklqdeLDKIVKTKSELV 399
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
146-459 |
1.12e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 146 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQ-QTTTTSVKNLEPFFEAYINALRKQVDSLANDKGRLQSELK 224
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 225 IMQdsVEdyKTKYEDEINKRAAAENDFVVLKKDVDAAYMnkvELEAKVDALNDEINFL------RVLYAAELSQMQTQVS 298
Cdd:pfam15921 587 AMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLvnagseRLRAVKDIKQERDQLL 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 299 DtsvvlSMDNNRNlDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQ--QLQTSVDQHGDSLRNTKNEISE-------LN 369
Cdd:pfam15921 660 N-----EVKTSRN-ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQlkSAQSELEQTRNTLKSMEGSDGHamkvamgMQ 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 370 RLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVaLKDAYSKRTELEAALQKAKEELA---RVLREYQELMSVKLAlDIEI 446
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVA-NMEV 811
|
330
....*....|...
gi 148356276 447 ATYRKLLEGEECR 459
Cdd:pfam15921 812 ALDKASLQFAECQ 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
211-433 |
1.25e-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: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 211 SLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRvlyaAEL 290
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK----ERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 291 SQMQTQVSDTSVVLsmdnnrnLDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQLQTSVDQHGDSLRNTKNEISELNR 370
Cdd:TIGR02169 740 EELEEDLSSLEQEI-------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148356276 371 LIQRLRAEIENVKKQCQTLQGSVADAEQRGEvALKDAYSKRTELEAALQKAKEELARVLREYQ 433
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
217-412 |
1.88e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 217 GRLQSELKIMQDSVEDYKTKYEDEINKRAaaENDFVVLKKDVDAaYMNKV-ELEAKVDALNDEINFLRVLYA--AELSQM 293
Cdd:PRK05771 63 RSYLPKLNPLREEKKKVSVKSLEELIKDV--EEELEKIEKEIKE-LEEEIsELENEIKELEQEIERLEPWGNfdLDLSLL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 294 QTQvSDTSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQIK---VQQLQTSVDQH-GDSLR 359
Cdd:PRK05771 140 LGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgFERLELEEEGTpSELIR 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148356276 360 NTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADA----EQRGEVALKDAYSKRT 412
Cdd:PRK05771 219 EIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-435 |
2.19e-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: 44.24 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 145 TEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTttSVKNLEPFFEAYINALRKQVDSLANDkgrlQSELK 224
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKK--ENKKNIDKFLTEIKKKEKELEKLNNK----YNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 225 IMQDSVEDYKTKYEDEINKRAAAEND------------FVVLKKDVDAAYMNK--VELEAKVDALNDEINFLRVLYA--- 287
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKiknkllklelllSNLKKKIQKNKSLESqiSELKKQNNQLKDNIEKKQQEINekt 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 288 AELSQMQTQVSDTSVVLSMDNNR----NLDLDSI---IAEVRAQYEEIaqrsKAEAEALYQIKVQ----QLQTSVDQHGD 356
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQlsekQKELEQNnkkIKELEKQLNQL----KSEISDLNNQKEQdwnkELKSELKNQEK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 357 SLRNTKNEISELNRLIQRLRAEIENVKKQC-------QTLQGSVADAEQRGEVALKDAYSKRTELEaALQKAKEELARVL 429
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKI 400
|
....*.
gi 148356276 430 REYQEL 435
Cdd:TIGR04523 401 QNQEKL 406
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
180-385 |
2.97e-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: 42.63 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 180 KLLQQQTT-TTSVKNLEpffeaYINalrkqvdslandkgrlQSELKIMQDSVEDYKTKYEDEINKraaaendfvvLKKDV 258
Cdd:pfam15397 42 KLLQQYEKfGTIISILE-----YSN----------------KKQLQQAKAELQEWEEKEESKLNK----------LEQQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 259 DaaymnkvELEAKVDALNDEINFLRV-------LYAAELSQMQTQVSDTSvvlsmDNNRN--LDLDSIIAEVRAQYEEIA 329
Cdd:pfam15397 91 E-------QLNAKIQKTQEELNFLSTykdkeypVKAVQIANLVRQLQQLK-----DSQQDelDELEEMRRMVLESLSRKI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148356276 330 QRSKAE-------------AEALYQ--IKVQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQ 385
Cdd:pfam15397 159 QKKKEKilsslaektlspyQESLLQktRDNQVMLKEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREV 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-385 |
4.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 139 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQttttsvknlepffeayINALRKQVDSLANDKGR 218
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 219 LQSELKIMQDSVED-----YKTKYEDEINkraaaendFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRVLyAAELSQM 293
Cdd:COG4942 95 LRAELEAQKEELAEllralYRLGRQPPLA--------LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-LAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 294 QTQVsdtsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqikvQQLQTSVDQHGDSLRNTKNEISELNRLIQ 373
Cdd:COG4942 166 RAEL----------EAERAELEALLAELEEERAALEALKAERQKLL-----ARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|..
gi 148356276 374 RLRAEIENVKKQ 385
Cdd:COG4942 231 RLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-385 |
5.64e-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: 42.70 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 140 IQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQ------------TTTTSVKNLEPFFEAYINALRK 207
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEkellekeierlkETIIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 208 QVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKdvdaaymNKVELEAKVDALNDEINFLRV--- 284
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE-------EKKELEEKVKDLTKKISSLKEkie 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 285 LYAAELSQMQTQVSD-TSVVLSMDNNrnLDLDSIIAEVRAQYEEIAQrSKAEAEALyQIKVQQLQTSVDQHGDSLRNTKN 363
Cdd:TIGR04523 528 KLESEKKEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELIDQKEKEKKDLIK 603
|
250 260
....*....|....*....|..
gi 148356276 364 EISELNRLIQRLRAEIENVKKQ 385
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-410 |
5.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 139 EIQKVRTEEREQIKLLNNKFASFIDkvRFLEQQNKVLETKWKLLQQQTTTTSVknlepffEAYINALRKQVDSLANDKGR 218
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESL-------ERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 219 LQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFLRvlyaAELSQMQTQVS 298
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR----RELEELREKLA 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 299 DTSVVLSMDNNRnldLDSIIAEVRAQY----EEIAQRSKA--EAEALYQIKVQQLQTSVDQHGDSLRNTKNEISELNRLI 372
Cdd:TIGR02168 926 QLELRLEGLEVR---IDNLQERLSEEYsltlEEAEALENKieDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
|
250 260 270
....*....|....*....|....*....|....*...
gi 148356276 373 QRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSK 410
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQ 1040
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
313-435 |
6.13e-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: 41.45 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 313 DLDSIIAEVRAQYEEI-AQRSKAEAE-ALYQIKVQQLQTSVDQHGDSLRNTKN---------EISELNRLIQRLRAEIEN 381
Cdd:COG1579 35 ELEDELAALEARLEAAkTELEDLEKEiKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkEIESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 148356276 382 VKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
139-439 |
8.19e-04 |
|
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: 42.40 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 139 EIQKVRTEEREQIKLLNNKFASfidkvrfLEQQNKVLETKWKLL----QQQTTTTSVKNLEPFFEAYINALRKQVDSLAN 214
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLdekkQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 215 DKGRLQSELKIMQDSVEDYKTKYEDE--INKRAAAENDFVVLKKDVDAAYMNKVELEAK---VDALNDEINFLRVLYAAE 289
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKEklKNIELTAHCDKLLLENKELTQEASDMTLELKkhqEDIINCKKQEERMLKQIE 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 290 -LSQMQTQVSDtsvvlsmdnnrnlDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQLQTSVDQH--GDSLRNTKNEIS 366
Cdd:pfam05483 538 nLEEKEMNLRD-------------ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIE 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148356276 367 ELNRLIQRLRAEIENVKKQcqtlqgSVADAEQRgevalkDAYS-KRTELEAALQKAKEELARVLREYQELMSVK 439
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK------GSAENKQL------NAYEiKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-455 |
8.27e-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: 42.36 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 198 FEAYINALRKQVDSLANDKGRLQsELKIMQDSVEDYKtkYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALND 277
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 278 EINFLRVLyaaelsqmqtqvsdtsvvlsmdnnrnldLDSIIAEVRAQYEEIAQRSKAEAEALyQIKVQQLQTSVDQHGDS 357
Cdd:TIGR02169 266 RLEEIEQL----------------------------LEELNKKIKDLGEEEQLRVKEKIGEL-EAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 358 LRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGsvadaeqrgevalkdaysKRTELEAALQKAKEELARVLREYQELMS 437
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERK------------------RRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250
....*....|....*...
gi 148356276 438 VKLALDIEIATYRKLLEG 455
Cdd:TIGR02169 379 EFAETRDELKDYREKLEK 396
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
265-457 |
9.81e-04 |
|
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: 42.04 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 265 KVELEAKVDALNDEINFLRVLYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQI-- 342
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 343 -------KVQQLQTSVDQHGDSLRNTKNEISELNRLIQR-------LRAEIENVKKQCQTLQGSVADAEQRGEV------ 402
Cdd:pfam05557 84 ylealnkKLNEKESQLADAREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQNlekqqs 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148356276 403 ALKDAYSKRTELEAALQK----------AKEELARV---------LRE----YQELMSVKLALDIEIATYRKLLEGEE 457
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREhnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
316-428 |
1.10e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 316 SIIAEVRAQYEEIAQRSKAEAEALYQIKVQQLQTSVD----QHGDSLRNTKNEISEL-NRLIQR---LRAEIENVKKQCQ 387
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHklrnEFEKELRERRNELQKLeKRLLQKeenLDRKLELLEKREE 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148356276 388 TLQGSVADAEQRgevaLKDAYSKRTELEAALQKAKEELARV 428
Cdd:PRK12704 111 ELEKKEKELEQK----QQELEKKEEELEELIEEQLQELERI 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-457 |
1.12e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 313 DLDSIIAEVRAQYEEIAQRSKAEAEALyqikvQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGS 392
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL-----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148356276 393 VADAEQRgevaLKDAYSKRTELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRKLLEGEE 457
Cdd:COG1196 311 RRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
307-426 |
1.43e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 307 DNNRNlDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQlqTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQC 386
Cdd:PRK11637 43 SDNRD-QLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQE--EAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQ 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148356276 387 QTLQGSVA---DA------------------EQRGEVALkdAY-----SKRTELEAALQKAKEELA 426
Cdd:PRK11637 120 AAQERLLAaqlDAafrqgehtglqlilsgeeSQRGERIL--AYfgylnQARQETIAELKQTREELA 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
267-435 |
1.59e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 267 ELEAKVDALNDEINFLRvlyaAELSQMQTQVSDtsvvlsmdnnrnldLDSIIAEVRAQYEEIAQRSKAEAEALYQIK--- 343
Cdd:COG1579 28 ELPAELAELEDELAALE----ARLEAAKTELED--------------LEKEIKRLELEIEEVEARIKKYEEQLGNVRnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 344 -VQQLQTSVDQHGDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAK 422
Cdd:COG1579 90 eYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
170
....*....|....
gi 148356276 423 EEL-ARVLREYQEL 435
Cdd:COG1579 170 AKIpPELLALYERI 183
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
261-430 |
1.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 261 AYMNKVELEAKVDALNDEINflRVLYAAE---------LSQMQTQVSDTSVVLSmdnnrnlDLDS-------IIAEVRAQ 324
Cdd:COG3096 971 SYEDAVGLLGENSDLNEKLR--ARLEQAEearreareqLRQAQAQYSQYNQVLA-------SLKSsrdakqqTLQELEQE 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 325 YEEIAQRSKAEAEALYQIKVQQLQtsvdqhgDSLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQgsvadaeqrgeval 404
Cdd:COG3096 1042 LEELGVQADAEAEERARIRRDELH-------EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE-------------- 1100
|
170 180
....*....|....*....|....*.
gi 148356276 405 KDAYSKRTELEAalqkAKEELARVLR 430
Cdd:COG3096 1101 RDYKQEREQVVQ----AKAGWCAVLR 1122
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
314-451 |
2.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 314 LDSIIAEVRAQYEEIAQRSKAEAEAlyQIKVQQLQTSVDQHGDSLRN--TKNEISELNRLIQRLRAEIENVKKQCQTLQG 391
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148356276 392 SVADAEQRGEVALKD-AYSkrtELEAALQKAKEELARVLREYQELMSVKLALDIEIATYRK 451
Cdd:COG4717 454 ELAELEAELEQLEEDgELA---ELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
145-436 |
3.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 145 TEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKwkllqQQTTTTSVKNLEPFfEAYINALRKQVDSLANDKGRLQSELK 224
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-----EERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 225 IMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAayMNKV-ELEAKVDALNDEINFLRVLYAAeLSQMQTQVSDTsvv 303
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIrTLLAAIADAEDEIERLREKREA-LAELNDERRER--- 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 304 LSMDNNRNLDLDSIIAEVRAqyeEIAQRSKAEAEAlYQIKVQQLQTSVDQHGDSLRNT----KNEISELNrliqRLRAEI 379
Cdd:PRK02224 629 LAEKRERKRELEAEFDEARI---EEAREDKERAEE-YLEQVEEKLDELREERDDLQAEigavENELEELE----ELRERR 700
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148356276 380 ENVKKQCQTLQGSVADAEQrgevaLKDAYSK-RTELEaalQKAKEELARVLREYQELM 436
Cdd:PRK02224 701 EALENRVEALEALYDEAEE-----LESMYGDlRAELR---QRNVETLERMLNETFDLV 750
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
197-402 |
4.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 197 FFEAYINALRKQVDSL---------ANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVE 267
Cdd:COG3206 179 FLEEQLPELRKELEEAeaaleefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 268 LEAkvdalNDEINFLRvlyaAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQI---KV 344
Cdd:COG3206 259 LLQ-----SPVIQQLR----AQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAlqaRE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148356276 345 QQLQTSVDQhgdsLRNTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQRGEV 402
Cdd:COG3206 330 ASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-444 |
5.24e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 203 NALRKQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDFVVLKKDVDAAYMNKVELEAKVDALNDEINFL 282
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 283 RvlyaAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAE---VRAQYEEiaQRSKAEAEAlyqikvQQLQTSVDQHGDSLR 359
Cdd:pfam01576 579 Q----QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAE--ERDRAEAEA------REKETRALSLARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 360 NTKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQrgevalkdaySKRTeLEAALQKAKEELARVLREYQELMSVK 439
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER----------SKRA-LEQQVEEMKTQLEELEDELQATEDAK 715
|
....*
gi 148356276 440 LALDI 444
Cdd:pfam01576 716 LRLEV 720
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
214-434 |
5.48e-03 |
|
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: 38.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 214 NDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAE-NDFV-VLKKDVDaaymnkvELEAKVDALNDEINFLRVLYAAELS 291
Cdd:cd22656 84 NAGGTIDSYYAEILELIDDLADATDDEELEEAKKTiKALLdDLLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 292 QMQTQVSDTSVVLSMDNNRNL--DLDSIIAEVRAQYEEIAQRSKAEAEAL------YQIKVQ---QLQTSVDQHGDSLRN 360
Cdd:cd22656 157 ALETLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAKIDELkaliadDEAKLAaalRLIADLTAADTDLDN 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148356276 361 TKNEISELNRLIQRLRAEIENVKKQCQTLQGSVADAEQrgevALKDAYSKRTELEAALQKAKeELARVLREYQE 434
Cdd:cd22656 237 LLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDIS----KIPAAILAKLELEKAIEKWN-ELAEKADKFRQ 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-454 |
5.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 139 EIQKVRTEEREQIKLLNNKFASF---IDKVRFLEQQNKVLETKWKLLQQQTTTTSVKNLEPFFEAYiNALRKQVDSLAND 215
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 216 KGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDF--------VVLKKDVDAAYMNKVEL------------------- 268
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIagvlflvlgllallfllla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 269 --EAKVDALNDEINFLRVLYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQIKVQQ 346
Cdd:COG4717 295 reKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 347 LQTSVD-----------QHGDSLRNTKNEISELNRLIQRLRAEI---------ENVKKQCQTLQGSVADAEQRgevaLKD 406
Cdd:COG4717 375 LLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEE----LEE 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 148356276 407 AYSKRTELEAALQKAKE--ELARVLREYQELMSVKLALDIEIATYRKLLE 454
Cdd:COG4717 451 LREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
267-447 |
6.48e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 267 ELEAKVDALNDEINFLRVLYAAELSQMQTQVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRskaEAEALYQIKVQQ 346
Cdd:pfam12128 726 ALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR---RQEVLRYFDWYQ 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 347 lqtsvdqHGDSLRNtkneiselnrliQRLRAEIENVKKQCQTLQGSVADAEQRGEVALKDAYSKRTELEAALQKAKEELA 426
Cdd:pfam12128 803 -------ETWLQRR------------PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
170 180
....*....|....*....|.
gi 148356276 427 RVLREYQELMSVKLALDIEIA 447
Cdd:pfam12128 864 GLRCEMSKLATLKEDANSEQA 884
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
123-420 |
6.66e-03 |
|
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: 39.65 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 123 TINQSLLTPLHVEIDPEIQKVRTEEREQIKL-LNNkfasfidkvrFLEQQNKVLETKWKLLQQQTTTTSvKNLEPFFEAY 201
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATVELhLSN----------IENKKNELLDIIVEIKKHIHGEIN-KDLNKILEDF 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 202 INAlRKQVDSLANDKGRLQSELKIMQDSVEDYKTKYEDEINKRAAAENDfvvLKKDVDAAYMNKVELEAKVDALNDEINf 281
Cdd:TIGR01612 761 KNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIIN- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 282 lrvlyaaELSQMQTQV-SDTSVVLSMDNNRNLDLDSiiaeVRAQYEEIAQRSKAEaealyqIKVQQLQTSVDQHGDSlrn 360
Cdd:TIGR01612 836 -------EMKFMKDDFlNKVDKFINFENNCKEKIDS----EHEQFAELTNKIKAE------ISDDKLNDYEKKFNDS--- 895
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 361 tKNEISELNRLIQRLRAEIENVKKqcqtLQGSVADAEQRGEvALKDAYSKRTELEAALQK 420
Cdd:TIGR01612 896 -KSLINEINKSIEEEYQNINTLKK----VDEYIKICENTKE-SIEKFHNKQNILKEILNK 949
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-454 |
7.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 144 RTEE-REQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQttttsVKNLEPFFEAyINALRKQVDSLANDKGRLQSE 222
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 223 LKIMQDSVEDYKTKYEDEINKRAAAENdfvvLKKDVDAAymnkVELEAKVDALNDEINFLRVL---YAAELSQMQTQVSD 299
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKE----LKEKAEEY----IKLSEFYEEYLDELREIEKRlsrLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 300 tsvvLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALYQIK--------------VQQLQTSVDQHGDSLR 359
Cdd:PRK03918 333 ----LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKkrltgltpeklekeLEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 360 NTKNEISELNRLIQRLRAEIENVKK---QCQTLqGSVADAEQRGEvaLKDAYSKR-TELEAALQKAKEELARVLREYQEL 435
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKakgKCPVC-GRELTEEHRKE--LLEEYTAElKRIEKELKEIEEKERKLRKELREL 485
|
330
....*....|....*....
gi 148356276 436 MSVkLALDIEIATYRKLLE 454
Cdd:PRK03918 486 EKV-LKKESELIKLKELAE 503
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
310-457 |
8.13e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 310 RNLDLDSIIAEVRAQY--EEIAQRSKAEAEALYQIKVQQLQTSVDQHGDSLRNtknEISELNRLIQRLRAEIEnvkkqcq 387
Cdd:COG2433 361 PDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVE------- 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 388 TLQGSVADAEQRGEvalkdayskrtELEAALQKAKEELARVLREYQELMsvklALDIEIATYRKLLEGEE 457
Cdd:COG2433 431 ELEAELEEKDERIE-----------RLERELSEARSEERREIRKDREIS----RLDREIERLERELEEER 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
314-435 |
8.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 314 LDSIIAEVRAQYEEIAQRSKA-----EAEALYQiKVQQLQTSVDQHGDSLRNTKNEISELNRL---IQRLRAEIENVKKQ 385
Cdd:COG4717 100 LEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEE 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 148356276 386 CQTLQGSVADAEQRgevALKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:COG4717 179 LEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-435 |
9.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 138 PEIQKVRTEEREQIKLLNNkfasFIDKVRFLEQQNKVLETKWKLLQQQTTTTSVKnlepffEAYINALRKQVDSLANDKG 217
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEE----YLDELREIEKRLSRLEEEINGIEERIKELEEK------EERLEELKKKLKELEKRLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 218 RLQSELKIMQD--SVEDYKTKYEDEINKRAAAEndfvvLKKDVDAAYMNKVELEAKVDALNDEINFLRVLYAA------E 289
Cdd:PRK03918 356 ELEERHELYEEakAKKEELERLKKRLTGLTPEK-----LEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148356276 290 LSQMQTQVSDTSVVLSMDNNRNL---------DLDSIIAEVRAQYEEIAQR-SKAEAEALYQIKVQQLQTSVDQhgdsLR 359
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEHRKELleeytaelkRIEKELKEIEEKERKLRKElRELEKVLKKESELIKLKELAEQ----LK 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148356276 360 NTKNEISELN-RLIQRLRAEIENVKKQCQTLQGSVADAEQRGEvALKDAYSKRTELEAALQKAKEELARVLREYQEL 435
Cdd:PRK03918 507 ELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| |
