|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
136-449 |
2.27e-151 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 435.12 E-value: 2.27e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 136 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTSTSSkNLEPLFETYLSVLRKQLDTLVNDKGRLQSELKT 215
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 216 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVLS 295
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 296 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845070 376 CQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEECR 449
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-133 |
4.61e-36 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 131.32 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 14 GFSCGSAIVGSGKRGAFSSVSVS------GGAGRCSSGGFGSRSLYNLGGNKSISMSVAGSRQGACFGGAGGFGTGGFGG 87
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845070 88 GFGGSFSGKGGPG------------------------------FPVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 133
Cdd:pfam16208 81 GGFGGGGGGGFGGgggfgggfggggyggggfggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-425 |
1.01e-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: 61.23 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 197 KQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFL---K 273
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 274 VLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNT 351
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 352 KSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRI--------ELETALQQAKEELARMLREYQ 423
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaeleELEEELEELQEELERLEEALE 464
|
..
gi 1622845070 424 EL 425
Cdd:TIGR02168 465 EL 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-433 |
4.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 192 LSVLRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINF 271
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 272 LKVLYDAELSQmqthvsdmsvvLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQhgdnlKNT 351
Cdd:COG1196 335 LEEELEELEEE-----------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 352 KSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLA 431
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
..
gi 1622845070 432 LD 433
Cdd:COG1196 479 LA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-447 |
3.23e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 301 NLD-LDSIIAEVRAQYEEIA-QRSKAE-----AEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIK 373
Cdd:COG1196 187 NLErLEDILGELERQLEPLErQAEKAEryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 374 KQCQTLQASVADAEQRGENALKD---AHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-425 |
4.97e-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: 52.75 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 158 LEQQNKV--LETKWKLLQQQTTSTSSKnleplfetyLSVLRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRT 235
Cdd:TIGR02168 673 LERRREIeeLEEKIEELEEKIAELEKA---------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 236 AAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKvlydAELSQMQTHVSDMsvvlsmdNNRNLDLDSIIAEVRAQY 315
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE----AEIEELEAQIEQL-------KEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 316 EE--IAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENA 393
Cdd:TIGR02168 813 TLlnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622845070 394 ----------LKDAHSKRIELETALQQAKEELARMLREYQEL 425
Cdd:TIGR02168 893 rseleelseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-447 |
6.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 308 IAEVRAQYEEIAQRSKAEAEALYQ--TKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD 385
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845070 386 AEQR---GENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 349 AEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-444 |
7.73e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 257 ELEAKVDSLNDEINFLKVLY---DAELSQMQTHVSDMSVVLSMDNNRnLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtk 333
Cdd:COG4913 614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 334 VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRG------------ENALKDAHSKR 401
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralleerfAAALGDAVERE 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845070 402 I---------ELETALQQAKEELARMLREYQEL-MSVKLALDIEIAT---YRKLLE 444
Cdd:COG4913 767 LrenleeridALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-444 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 303 DLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISvdqhGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTL--- 379
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNG----GDRLEQLEREIERLERELEERERRRARLEALLAALglp 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845070 380 -----------QASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG4913 375 lpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
277-417 |
1.26e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.35 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 277 DAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEiAQRSKAEAEALY---QTKVQQLQISVDQHGDNLKNTKS 353
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845070 354 EIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELAR 417
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-441 |
1.32e-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: 51.21 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 304 LDSIIAEVRAQYEEIAQRSKAEAEALYQTK--VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 381
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845070 382 SVADAEQRGENALKDAHSKRIELETA---LQQAKEELARMLREYQELMSVKLALDIEIATYRK 441
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-444 |
2.10e-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: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 232 NKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEV 311
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 312 RAQYEEIAQRSKAEAEALyqTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGE 391
Cdd:TIGR02168 764 EELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845070 392 NA---LKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR02168 842 DLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-423 |
2.27e-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: 49.76 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 331 QTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRgenaLKDAHSKRIELETALQQ 410
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101
|
90
....*....|...
gi 1622845070 411 AKEELARMLREYQ 423
Cdd:COG4942 102 QKEELAELLRALY 114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
129-415 |
2.75e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 129 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKwklLQQQTTSTSSKNLE-PLFETYLSVLRKQLDTLVNDKG 207
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLK---------------------KDVDAAYMNKVELEAKVDSLN 266
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskeKELKKLNEEKKELEEKVKDLT 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 267 DEINFLKVLYD---AELSQMQTHVSDM-SVVLSMDNNrnLDLDSIIAEVRAQYEEIAQrSKAEAEALyQTKVQQLQISVD 342
Cdd:TIGR04523 517 KKISSLKEKIEkleSEKKEKESKISDLeDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELID 592
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845070 343 QHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLqasvadaeqrgENALKDAHSKRIELETALQQAKEEL 415
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL-----------SSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
189-417 |
2.93e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 189 ETYLSVLRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDaaymnkvELEAKVDSLNDE 268
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 269 I-NFLKVLYDAELSqmqthVSDMSVVLSMDN-----NRNLDLDSIIAEVRAQYEEI--AQRSKAEAEALYQTKVQQLQIS 340
Cdd:COG3883 88 LgERARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 341 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELAR 417
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-441 |
4.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 304 LDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 381
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845070 382 SVADAEQRGENA---LKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRK 441
Cdd:COG1196 324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
113-410 |
4.25e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 113 TINQSLLTPLHVEIDPEIQKVRTEEREQIKL-LNNkfasfidkvrFLEQQNKVLETKWKLlQQQTTSTSSKNLEPLFETY 191
Cdd:TIGR01612 692 TEDKAKLDDLKSKIDKEYDKIQNMETATVELhLSN----------IENKKNELLDIIVEI-KKHIHGEINKDLNKILEDF 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 192 LSVlRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYMNKVELEAKVDSLNDEINF 271
Cdd:TIGR01612 761 KNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINE 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 272 LKVLYDAELSQMQTHVsdmsvvlSMDNNRNLDLDSiiaeVRAQYEEIAQRSKAEaealyqtkvqqlqISVDQHGD---NL 348
Cdd:TIGR01612 837 MKFMKDDFLNKVDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAE-------------ISDDKLNDyekKF 892
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845070 349 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEqrgenALKDAHSKRIELETALQQ 410
Cdd:TIGR01612 893 NDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-438 |
4.48e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 308 IAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD 385
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622845070 386 AEQRgenaLKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIAT 438
Cdd:COG1196 342 LEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-431 |
4.83e-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: 49.67 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 133 VRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTSTssKNLEPLFETYLSVLRKQLDTLVNDKGRLQSE 212
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 213 LKTMQDSVEDF---KTKYEEEINK----RTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVlydaELSQMQT 285
Cdd:TIGR02168 749 IAQLSKELTELeaeIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE----EAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 286 HVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQ----------RSKAEAEALYQTKvQQLQISVDQHGDNLKNTKSEI 355
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleelieELESELEALLNER-ASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 356 AELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGEN-----------ALKDAHSKRIELETALQQAKEELARMLREYQE 424
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 1622845070 425 LMSVKLA 431
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
258-444 |
6.30e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 258 LEAKVDSLNDEINFLK---VLYDAELSQMQTHVSDM---SVVLSMDNNRNLDLDSIiAEVRAQYEEiAQRSKAEAEALYQ 331
Cdd:COG3206 166 LELRREEARKALEFLEeqlPELRKELEEAEAALEEFrqkNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 332 TKVQQLQISVDQHGDNLKNT-----KSEIAELNRM--------------IQRLRAEIENIKKQcqtLQASVADAEQRGEN 392
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviqqlRAQLAELEAElaelsarytpnhpdVIALRAQIAALRAQ---LQQEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622845070 393 ALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
300-444 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 300 RNLDLDSIIAEVRAQYEEIAQRSKAEAEAL-----YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKK 374
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEeeleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 375 QCQTLQASVADAEQRgenaLKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR02168 303 QKQILRERLANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
303-444 |
1.47e-05 |
|
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: 46.46 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 303 DLDSIIAEVRAQYEEI-AQRSKAEAE-ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIK--KQCQT 378
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845070 379 LQASVADAEQR---GENALKDAHSKRIELETALQQAKEELARMLREYQELmsvKLALDIEIATYRKLLE 444
Cdd:COG1579 94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-441 |
1.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 197 KQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKvly 276
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 277 dAELSQMQTHVSDMSVVLSMDNNRNLDL------DSIIAEVRAQY-EEIAQRSKAEAEALYQTKVQqlqisvdqhgdnlk 349
Cdd:COG4942 97 -AELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYlKYLAPARREQAEELRADLAE-------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 350 ntkseiaelnrmIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVK 429
Cdd:COG4942 162 ------------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 1622845070 430 LALDIEIATYRK 441
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-434 |
2.99e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 195 LRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflkv 274
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN---- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 275 lydaelsQMQTHVSDMSVVLsmDNNRNL---------DLDSIIAE---VRAQYEEiaQRSKAEAEAL-YQTKVqqlqISV 341
Cdd:pfam01576 577 -------RLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEAReKETRA----LSL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 342 DQHGDNLKNTKSEIAELNRMiqrLRAEIENIkkqcqtlqasVADAEQRGENALKDAHSKRIeLETALQQAKEELARMLRE 421
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQ---LRAEMEDL----------VSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELEDE 707
|
250
....*....|...
gi 1622845070 422 YQELMSVKLALDI 434
Cdd:pfam01576 708 LQATEDAKLRLEV 720
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
125-447 |
4.42e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 125 EIDPE-IQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQT------TSTSSKNLEPLFETY---LSV 194
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 195 LRKQLDTLVNDKGRLQSE---LKTMQDSVEdfktkyEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINF 271
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLE------SEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNR 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 272 LKVLYDAELSQMQTHVSDMSVVLSmdnnrNLDLDSIiaevRAQYEEIAQRSKAEAEALYQTKVQQLQIS---------VD 342
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksireIE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 343 QHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQaSVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREY 422
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
330 340
....*....|....*....|....*
gi 1622845070 423 QELMSVKLALDIEIATYRKLLEGEE 447
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-447 |
5.96e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 188 FETYLSVLRKQLDTLVNDKGRLQsELKTMQDSVEDFKtkYEEEINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLND 267
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 268 EINFLKVLydaeLSQMQTHVSDMSvvlsmdNNRNLDLDSIIAEVRAqyeEIAQRSKAEAEalYQTKVQQLQisvdqhgDN 347
Cdd:TIGR02169 266 RLEEIEQL----LEELNKKIKDLG------EEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDAE-------ER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 348 LKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGE-------------NALKDAHSKRielETALQQAKEE 414
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefAETRDELKDY---REKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|...
gi 1622845070 415 LARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
136-449 |
6.59e-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: 45.88 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 136 EEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQTTSTSSKNLEPL-FETYLSVLRKQLDTLVNDKGRLQSELK 214
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 215 TMQdsVEdfKTKYEEEINKRTAAENDFVVLKKDVDAAYMnkvELEAKVDSLNDEinflKVLYDAELSQMQTHVSDM---- 290
Cdd:pfam15921 587 AMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELE----KVKLVNAGSERLRAVKDIkqer 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 291 -SVVLSMDNNRNlDLDSIIAEvraqYEEIAQRSKAEAEALYQT------KVQQLQISVDQHGDNLKNTKSEIAELNRMIQ 363
Cdd:pfam15921 656 dQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEEMETTtnklkmQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 364 RLRAEIENIKKQCQTLQASVADAEQRGENALKDAH---SKRIELETALQQAKEELARMLREYQELMSVKLAL-----DIE 435
Cdd:pfam15921 731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLkekvaNME 810
|
330
....*....|....
gi 1622845070 436 IATYRKLLEGEECR 449
Cdd:pfam15921 811 VALDKASLQFAECQ 824
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
255-447 |
6.61e-05 |
|
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: 45.50 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 255 KVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKV 334
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 335 QQLQIS---------VDQHGDNLKNTKSEIAELNRMIQR-------LRAEIENIKKQCQTLQASVADAEQRGEN------ 392
Cdd:pfam05557 84 YLEALNkklnekesqLADAREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQNlekqqs 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845070 393 ALKDAHSKRIELETALQQ----------AKEELARM---------LRE----YQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREhnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
191-402 |
7.15e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 191 YLSVLRKQLDTLvndkGRLQSELKTMQDSVEDFKTKYEEEINKRtaAENDFVVLKKDVDAaYMNKV-ELEAKVDSLNDEI 269
Cdd:PRK05771 51 LLTKLSEALDKL----RSYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEKIEKEIKE-LEEEIsELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 270 NFLKVL--YDAELSQMQTHvSDMSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQTK---V 334
Cdd:PRK05771 124 ERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgF 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845070 335 QQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADA----EQRGENALKDAHSKRI 402
Cdd:PRK05771 203 ERLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
153-385 |
8.13e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 153 DKVRFLEQQNKVLETKWKLLQQQTTstssknlepLFETYLSVLRKQLDtlvNDKGRLQSELKTMQDSVEDFKTkyeeEIN 232
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK---------TYNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKA----EIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 233 KRTAAENDFVVLKKDVDAAY----MNKVELEAKVDSLNDEINFLKvlydaELSQMQTHVSDMSvvlsmdnnrnlDLDSII 308
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDRI 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 309 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVAD 385
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTA--IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
204-424 |
1.79e-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: 43.51 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 204 NDKGRLQSELKTMQDSVEDFK--TKYEEEINKRTAAENDFVVLKKDVDaaymnkvELEAKVDSLNDEINFLKVLYDAELS 281
Cdd:cd22656 84 NAGGTIDSYYAEILELIDDLAdaTDDEELEEAKKTIKALLDDLLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 282 QMQTHVSDMSVVLSMDNNRNL--DLDSIIAEVRAQYEEIAQRSKAEAEAL------YQTKVQ---QLQISVDQHGDNLKN 350
Cdd:cd22656 157 ALETLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAKIDELkaliadDEAKLAaalRLIADLTAADTDLDN 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622845070 351 TKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQrgenALKDAHSKRIELETAlQQAKEELARMLREYQE 424
Cdd:cd22656 237 LLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDIS----KIPAAILAKLELEKA-IEKWNELAEKADKFRQ 305
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
309-416 |
1.91e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 309 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHgDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQAS-VADAE 387
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETR 115
|
90 100 110
....*....|....*....|....*....|
gi 1622845070 388 QRGENA-LKDAHSKRIELETALQQAKEELA 416
Cdd:PRK11281 116 ETLSTLsLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
276-441 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 276 YDAELSQMQTHVSDMSVVLSMDNNRNLdLDSIIAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGD--------- 346
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQEL--KEELEELEEQLEELLGeleelleal 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 347 NLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENAlkdahskriELETALQQAKEELARMLREYQELM 426
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA---------ELLQELEELKAELRELAEEWAALK 496
|
170
....*....|....*
gi 1622845070 427 SVKLALDIEIATYRK 441
Cdd:COG4717 497 LALELLEEAREEYRE 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
303-425 |
2.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 303 DLDSIIAEVRAQYEEI------AQRSKAEAEALYQTKVQQLQISVDQHGdNLKNTK------SEIAELNRMIQRLRAEIE 370
Cdd:COG1579 35 ELEDELAALEARLEAAkteledLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKeyealqKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622845070 371 NIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQEL 425
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
237-441 |
2.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 237 AENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVlsmdnnrNLDLDSIIAEVRAQYE 316
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-------QAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 317 EIAQRskaeAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRM----------IQRLRAEIENIKKQCQTLQASVADA 386
Cdd:COG3883 87 ELGER----ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIadadadlleeLKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622845070 387 EQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRK 441
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
129-429 |
2.68e-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: 43.94 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 129 EIQKVRTEEREQIKLLNNKFASfidkvrfLEQQNKVLETKWKLLQQQttstssKNLEPLFETylsvLRKQLDTLVndkGR 208
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEK------KQFEKIAEE----LKGKEQELI---FL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 209 LQSELKTMQD-SVEDFKTKYEEEINKRTAAEndfvvLKKDVDAAYMNKVELEAKVDSLndeinflkVLYDAELSQmqtHV 287
Cdd:pfam05483 445 LQAREKEIHDlEIQLTAIKTSEEHYLKEVED-----LKTELEKEKLKNIELTAHCDKL--------LLENKELTQ---EA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 288 SDMSVVLSM---DNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ---LQISVDQHGDNLKNTKSEIAELNRM 361
Cdd:pfam05483 509 SDMTLELKKhqeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845070 362 IQRLRAEIENIKKQCQTLQASVADAEQRGEnALK---DAHSKRI--------ELETALQQAKEELARMLREYQELMSVK 429
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENK-ALKkkgSAENKQLnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
309-424 |
3.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 309 AEVRAQYEEIAQRSKAEAE--------ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ 380
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKElrerrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622845070 381 ASvadAEQRGEN--ALKDAHSKRIELETALQQAKEELARMLREYQE 424
Cdd:PRK12704 138 EE---QLQELERisGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
129-444 |
3.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 129 EIQKVRTEEREQIKLLNNKFASF---IDKVRFLEQQNKVLETKWKLLQQQTTSTSSKNLEPLFETYlSVLRKQLDTLVND 205
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 206 KGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDF--------VVLKKDVDAAYMNKVEL------------------- 258
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIagvlflvlgllallfllla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 259 --EAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ 336
Cdd:COG4717 295 reKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 337 LQISVD-----------QHGDNLKNTKSEIAELNRMIQRLRAEI---------ENIKKQCQTLQASVADAEQRgenaLKD 396
Cdd:COG4717 375 LLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEELEEE----LEE 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622845070 397 AHSKRIELETALQQAKE--ELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG4717 451 LREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-444 |
3.43e-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: 43.51 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 195 LRKQLDTLvndkgRLQSELktmqdsVEDFKTKYEEEIN-KRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflk 273
Cdd:TIGR02168 198 LERQLKSL-----ERQAEK------AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQ--- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 274 vLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRskaeaEALYQTKVQQLQISVDQHGDNLKNTKS 353
Cdd:TIGR02168 264 -ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-----LANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 354 EIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRG---ENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKL 430
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250
....*....|....
gi 1622845070 431 ALDIEIATYRKLLE 444
Cdd:TIGR02168 418 RLQQEIEELLKKLE 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-447 |
3.49e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 257 ELEAKVDSLNDEINflkvLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqtkvQQ 336
Cdd:COG1196 250 ELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-----EE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 337 LQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELA 416
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190
....*....|....*....|....*....|.
gi 1622845070 417 RmLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 401 Q-LEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
129-389 |
3.90e-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: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 129 EIQKVRTEEREQIKLLNNKFASFIDKVRFLEQQNKVLETKWKLLQQQttstssknleplfetyLSVLRKQLDTLVNDKGR 208
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------------LAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 209 LQSELKTMQDsvedfktkyeeeinkrtaaendfvVLKKDVDAAYMNkveleakvdSLNDEINFLkvLYDAELSQMQTHVS 288
Cdd:COG4942 95 LRAELEAQKE------------------------ELAELLRALYRL---------GRQPPLALL--LSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 289 DMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQ--LQISVDQHGDNLKNTKSEIAELNRMIQRLR 366
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERaaLEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|...
gi 1622845070 367 AEIENIKKQCQTLQASVADAEQR 389
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
312-447 |
5.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 312 RAQYEEIAQRSKAEAEALyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRge 391
Cdd:COG1196 241 LEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-- 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845070 392 naLKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196 318 --LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
302-419 |
6.52e-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: 40.97 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 302 LDLDSIIAEVRAqyeeiAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQA 381
Cdd:pfam02321 69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622845070 382 SVADAEQrGENALKDAHSKRIELETALQQAKEELARML 419
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
187-415 |
6.65e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 187 LFETYLSVLRKQLDTLVNDKGRLQSELKTMQdsvedfktKYEEEINKRTAAENDfvvlkkdvdaaymnkvELEAKVDSLN 266
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYN--------KNIEEQRKKNGENIA----------------RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 267 DEINFLKvlydAELSQMQTHVSDmsVVLSMDNNRNL--DLDSIIAEVRAQYEEIAQRSK---------------AEAEAL 329
Cdd:PHA02562 227 EEAKTIK----AEIEELTDELLN--LVMDIEDPSAAlnKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 330 Y---QTKVQQLQISVDQ---HGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRIE 403
Cdd:PHA02562 301 ItkiKDKLKELQHSLEKldtAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE 380
|
250
....*....|..
gi 1622845070 404 LETaLQQAKEEL 415
Cdd:PHA02562 381 LAK-LQDELDKI 391
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
142-342 |
1.34e-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: 41.58 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 142 KLLNNKFASFIDKVRFLEQQNKVLETKWKLlqqqttstssKNLEPLFETYLSVLRKQL---DTLVND--KGRLQSELKTM 216
Cdd:TIGR01612 2085 KFENNYKHSEKDNHDFSEEKDNIIQSKKKL----------KELTEAFNTEIKIIEDKIiekNDLIDKliEMRKECLLFSY 2154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 217 QDSVEDFKTK---YEEEINKRTAAENDFVvlkkdvdaAYMNKVEleakvDSLNDEINFLKVLYDaeLSQMQTHVSDMSVV 293
Cdd:TIGR01612 2155 ATLVETLKSKvinHSEFITSAAKFSKDFF--------EFIEDIS-----DSLNDDIDALQIKYN--LNQTKKHMISILAD 2219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 294 LSMDNNRNLDLDSIIAEVRAQYEEI--AQRSKAEAEALYQTKVQ------QLQISVD 342
Cdd:TIGR01612 2220 ATKDHNNLIEKEKEATKIINNLTELftIDFNNADADILHNNKIQiiyfnsELHKSIE 2276
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
297-424 |
1.54e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 297 DNNRNlDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISvdQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQC 376
Cdd:PRK11637 43 SDNRD-QLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAIS--QASRKLRETQNTLNQLNKQIDELNASIAKLEQQQ 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622845070 377 QTLQASVA---DA------------------EQRGE------NALKDAHSKRIEletALQQAKEELARMLREYQE 424
Cdd:PRK11637 120 AAQERLLAaqlDAafrqgehtglqlilsgeeSQRGErilayfGYLNQARQETIA---ELKQTREELAAQKAELEE 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
128-425 |
1.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 128 PEIQKVRTEEREQIKLLNNkfasFIDKVRFLEQQNKVLETKWKLLQQQTTSTSSKNLEplfetyLSVLRKQLDTLVNDKG 207
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEE----YLDELREIEKRLSRLEEEINGIEERIKELEEKEER------LEELKKKLKELEKRLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 208 RLQSELKTMQD--SVEDFKTKYEEEINKRTAAEndfvvLKKDVDAAYMNKVELEAKVDSLNDEINFLKvlydAELSQMQT 285
Cdd:PRK03918 356 ELEERHELYEEakAKKEELERLKKRLTGLTPEK-----LEKELEELEKAKEEIEEEISKITARIGELK----KEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 286 HVSDMSVVLSMDN--NRNLDLD---SIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQ-----------ISVDQHGDNLK 349
Cdd:PRK03918 427 AIEELKKAKGKCPvcGRELTEEhrkELLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeselIKLKELAEQLK 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 350 NTKSEIAELN-RMIQRLRAEIENIKKQCQTLQASVADAEQRGENaLKDAHSKRIELETALQQAKEELARMLREYQEL 425
Cdd:PRK03918 507 ELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
126-444 |
2.25e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 126 IDPEIQKVRTEEREQIKLLNNKFAsfiDKVRFLEQQNKVLETKwkLLQQQTTSTSSKN-LEPLFETYLSVLRKQLDTLVN 204
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQ---DRIEQLISEHEVEITG--LTEKASSARSQANsIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 205 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINflKVLydAELSQMQ 284
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQ--KLL--ADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 285 THVS------------DMSVVLSMDNNRNlDLDSIIAEVRaQYEEIAQRSKAEAealyQTKVQQLQISVDQHGDNLKNTK 352
Cdd:pfam15921 391 KELSlekeqnkrlwdrDTGNSITIDHLRR-ELDDRNMEVQ-RLEALLKAMKSEC----QGQMERQMAAIQGKNESLEKVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 353 SEIAELNRMIQRLRAEIENIKKQCQTLQAS---VAD---AEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELM 426
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR 544
|
330 340
....*....|....*....|.
gi 1622845070 427 SVKL---ALDIEIATYRKLLE 444
Cdd:pfam15921 545 NVQTeceALKLQMAEKDKVIE 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-447 |
2.25e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 350 NTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSKRI---ELETALQQAKEELARMLREYQELM 426
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEAEVEQLEERIAQLS 753
|
90 100
....*....|....*....|.
gi 1622845070 427 SVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAE 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-445 |
2.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 232 NKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLkvlyDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEV 311
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 312 RAQYEEIAQRSKAEAEALYQTKvQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAE---Q 388
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaerA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845070 389 RGENALKDAHSKRIELETALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG 445
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-415 |
3.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 195 LRKQLDTLVndkgRLQSELKTMQDSVE---DFKTKYEE-EINKRTAAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEIN 270
Cdd:COG4913 230 LVEHFDDLE----RAHEALEDAREQIEllePIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 271 FLKVLYD---AELSQMQTHVSDMSVvlSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalYQTKVQQLQISVDQHGDN 347
Cdd:COG4913 306 RLEAELErleARLDALREELDELEA--QIRGNGGDRLEQLEREIERLERELEERERRRAR--LEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845070 348 LKNTKSEIAELNRMIQRLRAEIEN-----------IKKQCQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEEL 415
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEalaeaeaalrdLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-425 |
4.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 195 LRKQLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEeinkrtaAENDFVVLKKDVDAAYMNKVELEAKVDSLNDEInflkv 274
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 275 lydAELSQMQTHVsdmsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRskaEAEALYQTKVQQLQISVDQHGDNLKNTKSE 354
Cdd:TIGR02169 754 ---ENVKSELKEL----------EARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 355 IAELNRMIQR---LRAEIENIKKQCQTLQASVADAEQRGEN-----------------ALKDAHSKRIELETALQQAKEE 414
Cdd:TIGR02169 818 EQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeeleeeleeleaALRDLESRLGDLKKERDELEAQ 897
|
250
....*....|.
gi 1622845070 415 LARMLREYQEL 425
Cdd:TIGR02169 898 LRELERKIEEL 908
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
300-447 |
4.24e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 300 RNLDLDSIIAEVRAQY--EEIAQRSKAEAEALYQTKVQQLQISVDQhgdNLKNTKSEIAELNRMIQRLRAEIEnikkqcq 377
Cdd:COG2433 361 PDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEER---ELTEEEEEIRRLEEQVERLEAEVE------- 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 378 TLQASVADAEQRGEnalkdahskriELETALQQAKEELARMLREYQELMsvklALDIEIATYRKLLEGEE 447
Cdd:COG2433 431 ELEAELEEKDERIE-----------RLERELSEARSEERREIRKDREIS----RLDREIERLERELEEER 485
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
251-447 |
4.37e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 251 AYMNKVeLEAKVDSLNDEINFLKVLYDAELSQMQTHVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIaqrsKAEAEALy 330
Cdd:PHA02562 166 SEMDKL-NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI----KAEIEEL- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 331 QTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKK--QCQTLQASVADAEQRgenaLKDAHSKRIELETAL 408
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggVCPTCTQQISEGPDR----ITKIKDKLKELQHSL 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622845070 409 QQ---AKEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:PHA02562 316 EKldtAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
304-425 |
5.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 304 LDSIIAEVRAQYEEIAQRSKA-----EAEALYQtKVQQLQISVDQHGDNLKNTKSEIAElnrmIQRLRAEIENIKKQCQT 378
Cdd:COG4717 100 LEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAE 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622845070 379 LQASVADAEQRG----ENALKDAHSKRIELETALQQAKEELARMLREYQEL 425
Cdd:COG4717 175 LQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-433 |
6.23e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 130 IQKVRTEEREQIKLLNNKFASFIDKVRFL--EQQNKVletkwKLLQQQttstSSKNLEPLF---ETYLSVLRKQLDTLVN 204
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALksESQNKI-----ELLLQQ----HQDRIEQLIsehEVEITGLTEKASSARS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 205 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAymnKVELEAKVDSLNDEInflkVLYDAELSQMQ 284
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNSMYMRQLSD---LESTVSQLRSELREA---KRMYEDKIEELEKQL----VLANSELTEAR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 285 THVSDMSvvlsmDNNRNLD--LDSIIAEVRAQYEEIAQRsKAEAEALYQTKVQQlQISVDqhgdnlkNTKSEIAELNRMI 362
Cdd:pfam15921 363 TERDQFS-----QESGNLDdqLQKLLADLHKREKELSLE-KEQNKRLWDRDTGN-SITID-------HLRRELDDRNMEV 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845070 363 QRLRAEIENIKKQCQTLQASVADAEQRGENALKDAHSkrieLETALQQAKEELARMLreyQELMSVKLALD 433
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS----LTAQLESTKEMLRKVV---EELTAKKMTLE 492
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
210-375 |
6.33e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 38.39 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 210 QSELKTMQDSVEDFKTKYEEEINKrtaaendfvvLKKDVDaaymnkvELEAKVDSLNDEINFLKVLYDAE-------LSQ 282
Cdd:pfam15397 62 KKQLQQAKAELQEWEEKEESKLNK----------LEQQLE-------QLNAKIQKTQEELNFLSTYKDKEypvkavqIAN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 283 MQTHVSDMSvvlsmDNNRN--LDLDSIIAEVRAQYEEIAQRSK--------AEAEALYQTKVQQLQIS-------VDQHG 345
Cdd:pfam15397 125 LVRQLQQLK-----DSQQDelDELEEMRRMVLESLSRKIQKKKekilsslaEKTLSPYQESLLQKTRDnqvmlkeIEQFR 199
|
170 180 190
....*....|....*....|....*....|
gi 1622845070 346 DNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam15397 200 EFIDELEEEIPKLKAEVQQLQAQRQEPREV 229
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
352-414 |
8.87e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 37.05 E-value: 8.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845070 352 KSEIAELNRMIQRLRAEIENIKKQcqtlqasvadAEQRGENALKDAHSKRIE--------LETALQQAKEE 414
Cdd:COG0576 5 EAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLAEdllpvldnLERALAAAEED 65
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
130-444 |
8.90e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.85 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 130 IQKVRTEEREQIKLLNNKFasfidkvRFLEQQNKVLETKWKLLQQQTTSTSS------------KNLEPLFETYLSVLRK 197
Cdd:TIGR04523 59 LDKNLNKDEEKINNSNNKI-------KILEQQIKDLNDKLKKNKDKINKLNSdlskinseikndKEQKNKLEVELNKLEK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 198 QLDTLVNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDvdaaymnKVELEAKVDSLNDEINFLKVL-- 275
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNKLLKLELLls 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 276 ----YDAELSQMQTHVSDMsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQIsVDQHGDN---L 348
Cdd:TIGR04523 205 nlkkKIQKNKSLESQISEL-------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI-KKQLSEKqkeL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 349 KNTKSEIAELNRMIQRLRAEIENIKKQ-CQTLQASVADAEQRGENALKDAHSKRIELETALQQAKEELARMLREYQELMS 427
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330
....*....|....*..
gi 1622845070 428 VKLALDIEIATYRKLLE 444
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIE 373
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-417 |
9.73e-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: 38.62 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 209 LQSELKTMQDSVEDFKTKYEEEINKRTAAEndfvvlkkdvdaayMNKVELEAKVDSLNDEINFLKVLYDA---ELSQMQT 285
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--------------LEKVTTEAKIKKLEEDILLLEDQNSKlskERKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 286 HVSDMSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyqtkvQQLQISVDQHGDNLKNTKSEIAELNRMIQRL 365
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGR-----QELEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622845070 366 RAEIENIKKQCQTLQASVADAEQRGENALKdahsKRIELETALQQAKEELAR 417
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALK----KIRELEAQISELQEDLES 282
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
208-421 |
9.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAE----------NDFVVLKKDVDAAYMNKVELEAKVDSLNDEINFLKvlyd 277
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLR---- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 278 AELSQMQTHVSDMSVVLSMDN-------NRNLDLDSIIAEVRAQYEEI---AQRSKAEAEALYQtKVQQLQISVDQHGDN 347
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECrvaAQAHNEEAESLRE-DADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845070 348 LKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQASVADAEQRGENA----------LKDAHSKRIELETALQQAKEEL-- 415
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAedfleelreeRDELREREAELEATLRTARERVee 444
|
....*.
gi 1622845070 416 ARMLRE 421
Cdd:PRK02224 445 AEALLE 450
|
|
| |
