|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
919-1238 |
4.85e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 919 EREKDDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSEE-----NALLKNDLGRVRQELEAAESTHNAQRKEIEV 990
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAekaERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 991 LKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKV 1070
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1071 ELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQRLLSLQGEQAGR 1150
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1151 --RLDAQREEHEKQLKATEERVEEAemilknmEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRG 1228
Cdd:COG1196 416 leRLEEELEELEEALAELEEEEEEE-------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330
....*....|
gi 1622839299 1229 AEKQSRILEE 1238
Cdd:COG1196 489 AAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
919-1251 |
1.42e-15 |
|
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: 82.41 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 919 EREKDDMETKLLHLEDVVRALEKHVD-LRENDRL--EFHRLSEE-----NALLKNDLGRVRQELEAAESTHNAQRKEIEV 990
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKsLERQAEKaeRYKELKAElreleLALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 991 LKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKV 1070
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1071 ELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQH---SQEVRQLQEQMSRLVPQDRVAE--LQRLLSLQG 1145
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLNNEIERLEarLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1146 EQAGRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHL---VRALQAT 1222
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERL 497
|
330 340
....*....|....*....|....*....
gi 1622839299 1223 EEKQRGAEKQSRILEEKVRALNKLVGRIA 1251
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
218-279 |
8.22e-11 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 58.80 E-value: 8.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839299 218 ESQIRGMWEELGVGSRGHLSEQELAVVCQSVGLRG-LEKEELEDLFNKLDQDGDGKVSLEEFQ 279
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
983-1250 |
9.76e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 983 AQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQS 1062
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1063 DQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQgahlrlrQAQAQHSQEVRQLQEQmsrlvpQDRVAELQRLLs 1142
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-------QLKEELKALREALDEL------RAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1143 LQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKNMEML---LQEKVDELKEQFEKNTKsdlLLKELYVENAHLVRAL 1219
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLN---ERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|.
gi 1622839299 1220 QATEEKQRGAEKQSRILEEKVRALNKLVGRI 1250
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
913-1239 |
1.13e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 913 ETKTALEREKDDMETKLLHLEDVVRALEKHVDlrendrlefhrlseenallkndlgRVRQELEAAESTHNAQRKEIEVLK 992
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELE------------------------ELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 993 KDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEhrvtiqlltqsleevacsgqqQSDQIQKLKVEL 1072
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---------------------LEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1073 ECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQRLLSLQGEQAGRRL 1152
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE--EALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1153 DAQREEHEKQLKATEERVEEAEMILKNMEmlLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQ 1232
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEA--LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
....*..
gi 1622839299 1233 SRILEEK 1239
Cdd:COG1196 510 VKAALLL 516
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
985-1251 |
1.48e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 985 RKEIEVLKKDKEKAcsemevltRQNQNYKDQLSQLndRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQ 1064
Cdd:COG1196 199 ERQLEPLERQAEKA--------ERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1065 IQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQRLLSLQ 1144
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL--EELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1145 GEQAGRR--LDAQREEHEKQLKATEERVEEAEMILKNmemLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQAT 1222
Cdd:COG1196 347 EEAEEELeeAEAELAEAEEALLEAEAELAEAEEELEE---LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260
....*....|....*....|....*....
gi 1622839299 1223 EEKQRGAEKQSRILEEKVRALNKLVGRIA 1251
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1196 |
4.64e-10 |
|
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: 64.31 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 902 RQEQLAAPEEGETktaLEREKDDMETKLLHLEDVVRALEKHVdlrENDRLEFHRLSEENALLKNDLGRVRQELEAAESTH 981
Cdd:TIGR02168 704 RKELEELEEELEQ---LRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 982 NAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQA--------------QSEEHRVTIQLL 1047
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERriaaterrledleeQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1048 TQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQE-QMS 1126
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVR 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1127 RLVPQDRVAELQRLLSLQGEQAGRRLDAQREEHEKQLKATEERVEEaemiLKNMEMLLQEKVDELKEQFE 1196
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE----LGPVNLAAIEEYEELKERYD 1003
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
833-1245 |
1.39e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 833 ASCRGQAEKPQSIQEERARSWsrgtqgqasEEQARAEGALESACQehgvevarrgSLPSHLQLAEPGASRQEQLaapeeg 912
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMAREL---------AELNEAESDLEQDYQ----------AASDHLNLVQTALRQQEKI------ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 913 etktalEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLk 992
Cdd:PRK04863 351 ------ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 993 kDKEKACSEMEVLTRQN-----QNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQiqk 1067
Cdd:PRK04863 424 -ERAKQLCGLPDLTADNaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAR--- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1068 lkvELeclnqeyqslqLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRL-VPQDRVAELQRLLSlqge 1146
Cdd:PRK04863 500 ---EL-----------LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgKNLDDEDELEQLQE---- 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1147 qagrRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDELKEQFEKNTKSDLLLKELY------VENAHLVRAL- 1219
Cdd:PRK04863 562 ----ELEARLESLSESVSEARERRMALRQQLEQ----LQARIQRLAARAPAWLAAQDALARLReqsgeeFEDSQDVTEYm 633
|
410 420
....*....|....*....|....*.
gi 1622839299 1220 QATEEKQRGAEKQSRILEEKVRALNK 1245
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDE 659
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
925-1244 |
3.05e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 925 METKLLHLEDVVRALEKHVDLrENDRL------------EFHRLSEENALLKNDLGRVRQELEAAE---STHNAQRK--- 986
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEK-KQQEInektteisntqtQLNQLKDEQNKIKKQLSEKQKELEQNNkkiKELEKQLNqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 987 -EIEVLKKDKE-----KACSEMEVLTRQNQNYKDQL-------SQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEE 1053
Cdd:TIGR04523 295 sEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQIsqnnkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1054 VACSGQQQSDQIQKLKVELECLNQEYQslqlSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDR 1133
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1134 VAELQRllslqgeqagRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENA 1213
Cdd:TIGR04523 451 VKELII----------KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
330 340 350
....*....|....*....|....*....|.
gi 1622839299 1214 HLVRALQATEEKQRGAEKQSRILEEKVRALN 1244
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
234-279 |
1.02e-08 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 52.55 E-value: 1.02e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622839299 234 GHLSEQELAVVCQSVGlRGLEKEELEDLFNKLDQDGDGKVSLEEFQ 279
Cdd:cd00051 15 GTISADELKAALKSLG-EGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
964-1245 |
1.28e-08 |
|
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: 59.70 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 964 KNDLGRVRQELEAAESTHNAQRKEIEVLKKDKEKACS-----------EMEVLTRQNQNYKDQLSQLNDRVLQLGQEAST 1032
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1033 HQAQSEEHRVTIQLLTQSLEEVACS-GQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQ 1111
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1112 AQHSQEVRQLQEQMSRLVP-QDRVAELQ---RLLSLQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEK 1187
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKlTEEYAELKeelEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839299 1188 VD----------ELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRALNK 1245
Cdd:TIGR02169 416 QRlseeladlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
917-1178 |
8.29e-08 |
|
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: 57.00 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 917 ALEREKDDMETKLLHLEDVVRALEKhvdLRENDRLEFHRLSEENAL-LKNDLGRVRQELEAAESTHNAQRKEIEVLKKDK 995
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 996 EKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEAsthqaqsEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECL 1075
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY-------AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1076 NQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQ----------EVRQLQEQMSRLVpQDRVAELQRLLSLQG 1145
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekedkalEIKKQEWKLEQLA-ADLSKYEQELYDLKE 476
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622839299 1146 EQA---GRRLDAQRE--EHEKQLKATEERVEE---AEMILK 1178
Cdd:TIGR02169 477 EYDrveKELSKLQRElaEAEAQARASEERVRGgraVEEVLK 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
900-1165 |
1.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 900 ASRQEQLAApEEGETKTALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAES 979
Cdd:COG1196 252 EAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 980 THNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVAcsgq 1059
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1060 qqsDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQR 1139
Cdd:COG1196 407 ---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA--ALLEAALAE 481
|
250 260
....*....|....*....|....*.
gi 1622839299 1140 LLSLQGEQAGRRLDAQREEHEKQLKA 1165
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
966-1246 |
1.20e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.60 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 966 DLGRVRQELEAAESTHNAQRKEI-EVLK----------------KDKEKACSEMEVLTRqnqNYKDQLSQLNDRVLQLGQ 1028
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIvEALQsalnwleerkgsleraKQYQQVIDNFPKLSA---ELRQQLNNERDEPRSVPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1029 EASTHQAQSEEHRVTIQLLTQSLEEvacsgQQQSDQIQKLKVELECLNQEyqslqlsQSELTQTLEESQGQVQG------ 1102
Cdd:PRK10929 101 NMSTDALEQEILQVSSQLLEKSRQA-----QQEQDRAREISDSLSQLPQQ-------QTEARRQLNEIERRLQTlgtpnt 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1103 ----AHLRLRQAQ-AQHSQEVRQLqeQMSRLVPQDRvAELQRLLSLQGEQAGRRLDAQREEHEKQLKAteERVEEAEMIL 1177
Cdd:PRK10929 169 plaqAQLTALQAEsAALKALVDEL--ELAQLSANNR-QELARLRSELAKKRSQQLDAYLQALRNQLNS--QRQREAERAL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839299 1178 KNMEMLLQEKVD---ELKEQFEKNtksdlllKELYVENAHLVRALQATEEKQRGAEKQSrileEKVR-ALNKL 1246
Cdd:PRK10929 244 ESTELLAEQSGDlpkSIVAQFKIN-------RELSQALNQQAQRMDLIASQQRQAASQT----LQVRqALNTL 305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
900-1251 |
1.60e-07 |
|
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: 55.84 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 900 ASRQEQLAAPEEGETKTALEREKDDMETKLLHLEDVVRALEKHVD----LRENDRLEFHRLSEENALLKNDLGRVRQELE 975
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDelsqELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 976 AAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQS-EEHRVTIQLLTQSLEEV 1054
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1055 ACSGQQQSDQIQKLKVELECLNQEyqsLQLSQSELTQTLEESQGQVQGAHLRLRQAQAqhsqEVRQLQEQMSRLvpqdrv 1134
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEELEELEA----ALRDLESRLGDL------ 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1135 aelqrllslqgeqagrrlDAQREEHEKQLKATEERVEEAE-------MILKNMEMLLQEKVDELKEqFEKNTKSD----- 1202
Cdd:TIGR02169 888 ------------------KKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLEALEEELSE-IEDPKGEDeeipe 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622839299 1203 --LLLKELYVENAHLVRALQATEEKQRGAEKQsriLEEKVRALNKLVGRIA 1251
Cdd:TIGR02169 949 eeLSLEDVQAELQRVEEEIRALEPVNMLAIQE---YEEVLKRLDELKEKRA 996
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1023-1254 |
2.28e-07 |
|
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: 54.77 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1023 VLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQG 1102
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1103 AHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQG-EQAGRRLD------AQREEHEKQLKATEERVEEAEM 1175
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQylkylaPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839299 1176 ILKNMEMLLQEKVDELKEQFEKntksdllLKELYVENAHLVRALQATEEKQRgaeKQSRILEEKVRALNKLVGRIAPAA 1254
Cdd:COG4942 168 ELEAERAELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIARLEAEA 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
963-1250 |
3.11e-07 |
|
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: 55.03 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 963 LKNDLGRVRQELEAAESTHNAQRKEIEvlkkdkEKAcSEMEVLTRQNQNYKD-------QLSQLNDRVLQLGQEASTHQA 1035
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELE------EKQ-NEIEKLKKENQSYKQeiknlesQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1036 QSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQ---A 1112
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1113 QHSQEVRQLQEQMSRLvpQDRVAEL-QRLLSLQGEQagRRLDAQREEHEKQLKATEERVEEAEMILKNMEML-----LQE 1186
Cdd:TIGR04523 493 SKEKELKKLNEEKKEL--EEKVKDLtKKISSLKEKI--EKLESEKKEKESKISDLEDELNKDDFELKKENLEkeideKNK 568
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839299 1187 KVDELKEQFE----KNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRALNKLVGRI 1250
Cdd:TIGR04523 569 EIEELKQTQKslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
908-1221 |
6.36e-07 |
|
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: 53.98 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 908 APEEGETKTALEREKDDMETKLL-HLEDVVRALEKHVDLRENdrleFHRLSEENALLKNDLGRVRQELEAAESTHNAQRK 986
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELeHKRARIELEKKASALKRQ----LDRESDRNQELQKRIRLLEKREAEAEEALREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 987 EIEVLKKDkekacseMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVacsgQQQSDQIQ 1066
Cdd:pfam05557 77 LNRLKKKY-------LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL----QERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1067 KLKVELECLNQEYQSLQlsqseltQTLEESQGQVQGAHLRLrQAQAQHSQEVRQLQEQMSRlvpqdrVAELQRLLslqge 1146
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQ-------SSLAEAEQRIKELEFEI-QSQEQDSEIVKNSKSELAR------IPELEKEL----- 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839299 1147 qagrrldAQREEHEKQLKATEERVEeaemilknmemLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQA 1221
Cdd:pfam05557 207 -------ERLREHNKHLNENIENKL-----------LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQS 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1200 |
6.88e-07 |
|
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: 53.23 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 976 AAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVA 1055
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1056 CSGQQQSDQIQKLKVELECL-NQEYQSLQLSQSELTQTLEESQ--GQVQGAHLRLRQAQAQHSQEVRQLQEQMsrlvpQD 1132
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAEL-----EA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839299 1133 RVAELQRLLSLQGEQAgRRLDAQREEHEKQLKATEERVEEAEMILKNM---EMLLQEKVDELKEQFEKNTK 1200
Cdd:COG4942 172 ERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAE 241
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
232-278 |
8.37e-07 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 46.92 E-value: 8.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622839299 232 SRGHLSEQELAVVCQSVGLRGLEKEELEDLFNKLDQDGDGKVSLEEF 278
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
906-1148 |
8.63e-07 |
|
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: 52.84 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 906 LAAPEEGETKTALEREKDDMETKLLHLEDVVRALEKHvdlRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQR 985
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 986 KEIEVLKKDKEKACSEMEVLTRQNQnykdQLSQLNDRVLQLGQEASthqAQSEEHRVTIQLLTQSLEEVACSGQQQSDQI 1065
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALY----RLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1066 QKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQRLLSLQG 1145
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL--EALIARLEAEAAAAA 240
|
...
gi 1622839299 1146 EQA 1148
Cdd:COG4942 241 ERT 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
945-1175 |
9.89e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 945 LRENDRLEFHRLSEENALLKNDLGRVRQELEAAEsthnaqrKEIEVLKKDkekacSEMEVLTRQNQNYKDQLSQLNDRVL 1024
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-------AALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1025 QLGQEASTHQAQSEEHRVTIQLLTQSLEEVacsgqQQSDQIQKLKVELECLNQEYQSLQLS-----------QSELTQTL 1093
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPEL-----LQSPVIQQLRAQLAELEAELAELSARytpnhpdvialRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1094 EESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQDRVAELQRLlslqgEQAGRRLDAQREEHEKQLKATEERVEEA 1173
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQL--EARLAELPEL-----EAELRRLEREVEVARELYESLLQRLEEA 377
|
..
gi 1622839299 1174 EM 1175
Cdd:COG3206 378 RL 379
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
855-1209 |
1.12e-06 |
|
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: 53.42 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 855 RGTQGQASEEQARaegaLESACQEHGVEVARRGSLPSHLQLAEPGASR-QEQLAAPEegetktALEREKDDMETKLLHLE 933
Cdd:COG3096 295 FGARRQLAEEQYR----LVEMARELEELSARESDLEQDYQAASDHLNLvQTALRQQE------KIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 934 DVVRALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLkkDKEKACSEMEVLTRQN---- 1009
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALCGLPDLTPENaedy 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1010 -QNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEV---------------ACSGQQQSDQIQKLKVELE 1073
Cdd:COG3096 443 lAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVersqawqtarellrrYRSQQALAQRLQQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1074 CLNQEYQSLQ--------LSQS---------ELTQTLEESQGQVQGAHLRLRQAQA------QHSQEVRQLQEQMSRLVP 1130
Cdd:COG3096 523 ELEQRLRQQQnaerlleeFCQRigqqldaaeELEELLAELEAQLEELEEQAAEAVEqrselrQQLEQLRARIKELAARAP 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1131 QDRVAE--LQRLLSLQGEQ--AGRRLDAQRE---EHEKQLKATEERVEEA-EMILKNMEMLLQEKVDE------LKEQFe 1196
Cdd:COG3096 603 AWLAAQdaLERLREQSGEAlaDSQEVTAAMQqllEREREATVERDELAARkQALESQIERLSQPGGAEdprllaLAERL- 681
|
410
....*....|...
gi 1622839299 1197 kntkSDLLLKELY 1209
Cdd:COG3096 682 ----GGVLLSEIY 690
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1211 |
2.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 862 SEEQARAEGALESACQEHGVEVARRGSlpSHLQLAEPGASRQEQLAAPEEGETKTALEREKDDMETKLLHL----EDVVR 937
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKK 1504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 938 ALEKHVDLRENDRLEFHRLSEEnaLLKNDLGRVRQELEAAESTHNAQR-KEIEVLKKDKEKACSEMEVLTRQNQNYKDQL 1016
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1017 SQL--------NDRVLQLGQEASTHQAQ----SEEHRVTIQLLTQSlEEVACSGQQQSDQIQKLKVELECLNQEYQSLQL 1084
Cdd:PTZ00121 1583 AEEakkaeearIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1085 SQSELTQTLEESQGQVQGA------------HLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQgeqagrrl 1152
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-------- 1733
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622839299 1153 DAQREEHEKQLKATEERVEEAEmilknmemllQEKVDELKEQFEKNTKSDLLLKELYVE 1211
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEE----------KKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1197 |
2.38e-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: 51.30 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 971 RQELEAAESTHNAQRKEIEVLKKDKEKAcsemevltrqnqnyKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQS 1050
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKAL--------------LKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1051 LEEVACSGQQQSDQIQKLKVELECL-NQEYQSLQLSQSELTQTLEESQ--GQVQGAHLRLRQAQAQHSQEVRQLQEQMsr 1127
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAEL-- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1128 lvpQDRVAELQRLLSLQGEQAgRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDELKEQFEK 1197
Cdd:COG4942 170 ---EAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIAR 231
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
832-1209 |
7.24e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 832 AASCRGQAEKPQSIQEERARswsrgtqgQASEEQARaegalesacqehgvEVARRGSLPSHLQLAEPGASRQEQLAAPEE 911
Cdd:pfam17380 283 AVSERQQQEKFEKMEQERLR--------QEKEEKAR--------------EVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 912 getKTALEREKddmETKLLHLEDVVRALEK---------HVDLRENDRLEFHRLSeenallKNDlgRVRQELEAAesthn 982
Cdd:pfam17380 341 ---RMAMERER---ELERIRQEERKRELERirqeeiameISRMRELERLQMERQQ------KNE--RVRQELEAA----- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 983 aqrKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEhrvtiQLLTQSLEEVacsgQQQS 1062
Cdd:pfam17380 402 ---RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE-----QERQQQVERL----RQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1063 DQIQKLKVELEclnQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRlVPQDRVAELQRLLS 1142
Cdd:pfam17380 470 EERKRKKLELE---KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE-EERRREAEEERRKQ 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839299 1143 LQGEQagrrldaQREEHEKQLKATEERvEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELY 1209
Cdd:pfam17380 546 QEMEE-------RRRIQEQMRKATEER-SRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIY 604
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
222-282 |
7.53e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.71 E-value: 7.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839299 222 RGMWEELGVGSRGHLSEQELAVVCQSVGLRGLEkEELEDLFNKLDQDGDGKVSLEEFQLGL 282
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
234-278 |
7.60e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.71 E-value: 7.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622839299 234 GHLSEQELAVVCQSVGLRgleKEELEDLFNKLDQDGDGKVSLEEF 278
Cdd:COG5126 84 GKISADEFRRLLTALGVS---EEEADELFARLDTDGDGKISFEEF 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
830-1242 |
7.98e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 830 SPAASCRGQAEKPQSIQEERARSWSRGTQGQASEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPG--ASRQEQLA 907
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAeeVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 908 APEEG----------ETKTALEREKDDMETKllhLEDVVRALEKHVDLRENDRLEFHRLSEEnaLLKNDLGRVRQELEAA 977
Cdd:PTZ00121 1195 KAEDArkaeaarkaeEERKAEEARKAEDAKK---AEAVKKAEEAKKDAEEAKKAEEERNNEE--IRKFEEARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 978 ESTHNAQRKEIEVLKKDKEKACSEmEVLTRQNQNYKDQLSQLNDRvlqlGQEASTHQAQSEEHRVTIQLLTQSLEEVACS 1057
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1058 GQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQG---QVQGAHLRLRQAQ--AQHSQEVRQLQEQMSRLVPQD 1132
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEedKKKADELKKAAAAKKKADEAK 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1133 RVAELQRllslQGEQAGRRLDAQREEHEKQLKATEERveEAEMILKNMEMllQEKVDELKEQFEKNTKSDLLLKELYVEN 1212
Cdd:PTZ00121 1425 KKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
410 420 430
....*....|....*....|....*....|
gi 1622839299 1213 AHLVRALQATEEKQRGAEkqSRILEEKVRA 1242
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADE--AKKAEEAKKA 1524
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
865-1240 |
1.28e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 865 QARAEGALESACQEHGVEVA-RRGSLPSHLQlaepgaSRQEQLAAPEEGETKTALEREKDDMETKLLHLEDVVRALEkHV 943
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIApKQRSSNSKLQ------SNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDE-AI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 944 DLRENDRLEfhRLSEENALLKNDLGRVRQELEAAEsthnaqrKEIEVLKK-------DKEKACSEMEVLTRQNQNYKDQL 1016
Cdd:PLN02939 109 AAIDNEQQT--NSKDGEQLSDFQLEDLVGMIQNAE-------KNILLLNQarlqaleDLEKILTEKEALQGKINILEMRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1017 SQLNDRvLQLGQEASTHQAQSEEHrvtiqlLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQlsqsELTQTLEES 1096
Cdd:PLN02939 180 SETDAR-IKLAAQEKIHVEILEEQ------LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQFLKAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1097 QGQVQGAHLRLRQAQAQHS---QEVRQL-------QEQMSRLVPQ------DRVAELQRLLSL---QGEQAGRRLDaQRE 1157
Cdd:PLN02939 249 LIEVAETEERVFKLEKERSlldASLRELeskfivaQEDVSKLSPLqydcwwEKVENLQDLLDRatnQVEKAALVLD-QNQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1158 EHEKQLKATEERVEEAEMILKNMEM--LLQEKVDELKEQFEKNTKSDLLLKELYvenAHLVRALQATEEKQRgAEKQSRI 1235
Cdd:PLN02939 328 DLRDKVDKLEASLKEANVSKFSSYKveLLQQKLKLLEERLQASDHEIHSYIQLY---QESIKEFQDTLSKLK-EESKKRS 403
|
....*
gi 1622839299 1236 LEEKV 1240
Cdd:PLN02939 404 LEHPA 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
982-1173 |
1.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 982 NAQRKeIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRvlqlgQEASTHQAQSEEHRVTIQLLTQSLEEVacsgQQQ 1061
Cdd:COG4913 607 DNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQRLAEYSWDEIDVASAEREIAEL----EAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1062 SDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHsQEVRQLQEQMSRLVPQDRVAELQRLL 1141
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622839299 1142 SLQG-----EQAGRRLDAQREEHEKQLKATEERVEEA 1173
Cdd:COG4913 756 AAALgdaveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
956-1251 |
1.52e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 956 LSEENALLKNDLGRVRQELEAAEsthnAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQ-------------LSQLNDR 1022
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1023 V------LQLGQEA--------STHQAQSEEHRVTI-------QLLTQSLEEVACSGQQQS-DQIQKLKVELECLNQ--E 1078
Cdd:PRK11281 130 LaqtldqLQNAQNDlaeynsqlVSLQTQPERAQAALyansqrlQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNAqnD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1079 YQSLQLSQSELTQTLeesqGQVQGAHLRLRQAQAQHsqevrqlqeqmsrlvpqdRVAELQRLLSlqgeqagrrldaqree 1158
Cdd:PRK11281 210 LQRKSLEGNTQLQDL----LQKQRDYLTARIQRLEH------------------QLQLLQEAIN---------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1159 hEKQLKATEERVEEAEmilkNMEMLLQEKVDEL-KEQFEKNTK-SDLLLK-----------ELYVENAhLVRALQAteek 1225
Cdd:PRK11281 252 -SKRLTLSEKTVQEAQ----SQDEAARIQANPLvAQELEINLQlSQRLLKateklntltqqNLRVKNW-LDRLTQS---- 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622839299 1226 QRGAEKQ----------SRILEEKVRAL------NKLVGRIA 1251
Cdd:PRK11281 322 ERNIKEQisvlkgslllSRILYQQQQALpsadliEGLADRIA 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1044-1242 |
1.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1044 IQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQE 1123
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1124 QMSRLVPQDRVAE-------LQRLLSLQ--GEQAGRRLDAQREEhEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQ 1194
Cdd:COG3883 98 SGGSVSYLDVLLGsesfsdfLDRLSALSkiADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622839299 1195 FEKNTKsdlLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRA 1242
Cdd:COG3883 177 QAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
952-1253 |
3.07e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 952 EFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLkkdkEKACSEMEVltrqnqnykdQLSQLNDRvLQLGQEAS 1031
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQ----------DYQAASDH-LNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1032 THQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSL--QLS--QSEL-------------TQTLE 1094
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksQLAdyQQALdvqqtraiqyqqaVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1095 ESQGQVQGAHLRLRQAQAQHSQEVRQLQEQmsrlvpQDRVAELQRLLSL------QGEQAGR----------RLDAQR-- 1156
Cdd:PRK04863 425 RAKQLCGLPDLTADNAEDWLEEFQAKEQEA------TEELLSLEQKLSVaqaahsQFEQAYQlvrkiagevsRSEAWDva 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1157 ----EEHEKQlKATEERVEEAEMILKNMEMLL--QEKVDELKEQFEKNTKSDL----LLKELYVENAHLVRALQATEEKQ 1226
Cdd:PRK04863 499 rellRRLREQ-RHLAEQLQQLRMRLSELEQRLrqQQRAERLLAEFCKRLGKNLddedELEQLQEELEARLESLSESVSEA 577
|
330 340
....*....|....*....|....*..
gi 1622839299 1227 RGAEKQSRILEEKVRALNKLVGRIAPA 1253
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
357-1252 |
4.46e-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: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 357 QNGREILQENSRLQKEIVEVAEKLSDSERLALKLQKDLEfvlkdKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDE 436
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELA-----ELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 437 LQAELEGLWARLpknqhspswspggcrrqlsglgpagisflgnsvpvsIETELMMEQVKEHYEDLRTQLEtkvnHYEREI 516
Cdd:TIGR02168 377 LEEQLETLRSKV------------------------------------AQLELQIASLNNEIERLEARLE----RLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 517 AALKRNFEKERKDMEQARRREVSvleGQKADLEELHKKSQEVIWGLQEQLqdtahdpepermglapcctqalcglalrhq 596
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQ---AELEELEEELEELQEELERLEEAL------------------------------ 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 597 SHLRQIRREAQAELSGELLGLRALPARRDLTLELEEPLQGpLPRGSRRSEQLNLESALNLECASEKgaqmcasLALKEEL 676
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGY 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 677 ELAggkrvdrlfreaeMLGALpkeglvagsgregargllplspgyGERPLAWLTpgdggESEEAAgagsrcRQAQDTEAT 756
Cdd:TIGR02168 536 EAA-------------IEAAL------------------------GGRLQAVVV-----ENLNAA------KKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 757 KRPAPAPAPashgPSERWSHVQPCGVDGGTVPEELELFGVPVGLEQPGSRELPLLGTegdasqtqprmWESPLSPAAScr 836
Cdd:TIGR02168 568 NELGRVTFL----PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY-----------LLGGVLVVDD-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 837 gqaekpqsiqeerarswsrgtqGQASEEQARAEGALESACQEHGVEVARRGSLpshlqlaePGASRQEQLAApeegetkT 916
Cdd:TIGR02168 631 ----------------------LDNALELAKKLRPGYRIVTLDGDLVRPGGVI--------TGGSAKTNSSI-------L 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 917 ALEREKDDMETKLLHLEDVVRALEKHVDlrendrlefhRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLKKDKE 996
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALA----------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 997 KACSEMEVLTRQNQNYKDQLSQLNDRVlqlgQEASTHQAQSEEHRvtiqlltQSLEEVAcsgQQQSDQIQKLKVELECLN 1076
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERL----EEAEEELAEAEAEI-------EELEAQI---EQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1077 QEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHsqevRQLQEQMSRLVPQdrVAELQRLLSLQGEQAgRRLDAQR 1156
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----EELSEDIESLAAE--IEELEELIEELESEL-EALLNER 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1157 EEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVE--------NAHLVRALQATEEKQRG 1228
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlSEEYSLTLEEAEALENK 962
|
890 900
....*....|....*....|....
gi 1622839299 1229 AEKQSRILEEKVRALNKLVGRIAP 1252
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELGP 986
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
932-1178 |
5.19e-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: 47.20 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 932 LEDVVRALEKHVDLRENDRLEFHRLSEEnalLKNDLGRVRQELEAAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQN 1011
Cdd:pfam07888 50 QEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1012 YKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQ 1091
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1092 TLEESQGQVQGAHLRLRQAQaQHSQEVRQLQEQMSRLvpQDRVAELQRLLSLQGEQ----AGRRLDAQREEHEKQLKATE 1167
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAH-RKEAENEALLEELRSL--QERLNASERKVEGLGEElssmAAQRDRTQAELHQARLQAAQ 283
|
250
....*....|.
gi 1622839299 1168 ERVEEAEMILK 1178
Cdd:pfam07888 284 LTLQLADASLA 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
972-1170 |
5.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 972 QELEAAESTHNAQRKEIEVLKKDKEKAcsEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSL 1051
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1052 EEvacSGQQQSDQIQK----LKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSR 1127
Cdd:COG4913 333 RG---NGGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622839299 1128 LVpqDRVAELQRLL-SLQGEQAG---------RRLDAQREEHEKQLKATEERV 1170
Cdd:COG4913 410 AE--AALRDLRRELrELEAEIASlerrksnipARLLALRDALAEALGLDEAEL 460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1239 |
5.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 860 QASEEQARAEGALESACQEHGVEVARRGSlpSHLQLAEPGASRQEQLAAPEEGETKTALEREKDDMETKLLHLEDVVRAL 939
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 940 EKHVDLRENDrlEFHRLSEENALLKNDLGRVRQELEAAESTHNAQ-RKEIEVLKKDKEKACSEmEVLTRQNQNYKDQLSQ 1018
Cdd:PTZ00121 1477 KKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKK 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1019 LnDRVLQLGQEASTHQAQSEEHRVTIQLltQSLEEVACSGQQQSDQIQKLKVELECLNQEyqslqlsqseltQTLEESQG 1098
Cdd:PTZ00121 1554 A-EELKKAEEKKKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYEEEKKMKAE------------EAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1099 QVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRllSLQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILK 1178
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN--KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839299 1179 NMEMllQEKVDELKEQF-EKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEK 1239
Cdd:PTZ00121 1697 EAEE--AKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
955-1235 |
6.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 955 RLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQ 1034
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1035 AQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQH 1114
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1115 SQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQ 1194
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622839299 1195 FEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRI 1235
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
258-279 |
6.46e-05 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 40.77 E-value: 6.46e-05
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
919-1245 |
8.98e-05 |
|
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: 46.94 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 919 EREKDDMETKLLhLEDVVRALEKhvDLRENDRLEFHRLSEenallkndLGRVRQELEAAESTHNAQRKEIEVLKKDKEKa 998
Cdd:TIGR04523 110 SEIKNDKEQKNK-LEVELNKLEK--QKKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELENELNL- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 999 csemevLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRvtiqLLTQSLEEVACSGQQQSDQIQKLKVELECLNQE 1078
Cdd:TIGR04523 178 ------LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1079 YQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLV------PQDRVAELQRLLSLQGEQAgRRL 1152
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqkEQDWNKELKSELKNQEKKL-EEI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1153 DAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKeqfEKNTKSDLLLKE---LYVENAHLVRALQATEEKQRGA 1229
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQNEIEKLKKEnqsYKQEIKNLESQINDLESKIQNQ 403
|
330
....*....|....*.
gi 1622839299 1230 EKQSRILEEKVRALNK 1245
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQ 419
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
832-1196 |
9.32e-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: 47.04 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 832 AASCRGQAEKPQS---IQEERARSWSRGTQGQASE-----EQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGASRQ 903
Cdd:pfam15921 287 ASSARSQANSIQSqleIIQEQARNQNSMYMRQLSDlestvSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 904 EqlAAPEEGETKTALEREKDDmetklLHLEDVVRALEKHVDLRENDR-----LEFHRLSEENALLKNDLGRVRQELEAAE 978
Cdd:pfam15921 367 Q--FSQESGNLDDQLQKLLAD-----LHKREKELSLEKEQNKRLWDRdtgnsITIDHLRRELDDRNMEVQRLEALLKAMK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 979 STHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNdrvlqlgQEASTHQAQSEEHRVTIQLLTQSLEEVACSG 1058
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV-------EELTAKKMTLESSERTVSDLTASLQEKERAI 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1059 QQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGqvqgahLRLRQAQAQHSQEV-RQLQEQMSRLVPQ------ 1131
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA------LKLQMAEKDKVIEIlRQQIENMTQLVGQhgrtag 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1132 --------------DRVAELQRLLSLQGEQAG--RRLDAQREEHE----KQLKATEERVEEAEMILKNMEMLLQE----- 1186
Cdd:pfam15921 587 amqvekaqlekeinDRRLELQEFKILKDKKDAkiRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNEvktsr 666
|
410
....*....|.
gi 1622839299 1187 -KVDELKEQFE 1196
Cdd:pfam15921 667 nELNSLSEDYE 677
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1058-1245 |
1.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1058 GQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQ----------------VQGAHLRLRQAQAQH------S 1115
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELerldasS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1116 QEVRQLQEQMSRLvpQDRVAELQRLLSLQGEQAGRrLDAQREEHEKQLKATEERVEEAEMILKnmemllQEKVDELKEQF 1195
Cdd:COG4913 685 DDLAALEEQLEEL--EAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLAR------LELRALLEERF 755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1196 EKNTKSDLLLKELyvenAHLVRALQATEEKQRGAEKQsriLEEKVRALNK 1245
Cdd:COG4913 756 AAALGDAVERELR----ENLEERIDALRARLNRAEEE---LERAMRAFNR 798
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
257-282 |
1.27e-04 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 40.08 E-value: 1.27e-04
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
972-1254 |
1.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 972 QELEAAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSL 1051
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1052 EEVacsgqqqSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQgahlRLRQAQAQHSQEVRQLQEQMSRLVPQ 1131
Cdd:COG4372 111 EEL-------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1132 DRVAELQRLLSLQGEQA---GRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKEL 1208
Cdd:COG4372 180 EAEQALDELLKEANRNAekeEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622839299 1209 YVENAHLVRALQATEEKQRGAEKQSRILEEKVRALNKLVGRIAPAA 1254
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1255 |
1.95e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 843 QSIQEERARSWSRGTQGQASEEQARAEGA-----LESACQEHGVEVARRGSLPSHLQLAEPGASRQEQLAAPEEGETKTA 917
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAaqleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 918 LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRK-----EIEVLK 992
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagAVAVLI 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 993 KDKEKACSEMEVLTRQnqnykdQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVEL 1072
Cdd:COG1196 531 GVEAAYEAALEAALAA------ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1073 ECLNQEYQSLQLSQSELTQ-----TLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQ 1147
Cdd:COG1196 605 ASDLREADARYYVLGDTLLgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1148 AgRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQR 1227
Cdd:COG1196 685 A-ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
410 420
....*....|....*....|....*...
gi 1622839299 1228 GAEKQSRILEEKVRALnklvGRIAPAAL 1255
Cdd:COG1196 764 ELERELERLEREIEAL----GPVNLLAI 787
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
913-1239 |
1.96e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 913 ETKTALEREKDDMETKLLHLEDVVRALEKHVdLRENDRLEFHRLSEENallkndlgrvrqeleaaesthnaQRKEIEVLK 992
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLK-EQAKKALEYYQLKEKL-----------------------ELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 993 KDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEasthqaqseehrvTIQLLTQSLEEVACSGQQQSDQIQKLKVEL 1072
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-------------KLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1073 ECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGRRL 1152
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1153 DAQREEHEKQLKATEERVEEAEM--------------ILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRA 1218
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELElkseeekeaqllleLARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340
....*....|....*....|.
gi 1622839299 1219 LQATEEKQRGAEKQSRILEEK 1239
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKE 476
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
257-278 |
2.04e-04 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 39.67 E-value: 2.04e-04
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
846-1128 |
2.10e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 846 QEERARSWSRGTQGQASEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGASRQEQLAAPEEGETKTALEREKDDM 925
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 926 ETKLLHledvvralEKHVDLRENDRlEFHRLSEENALLKndlgrvrQELEAAESTHNAQRKEIEVLKKDKEKAcsemevL 1005
Cdd:TIGR00618 702 CQTLLR--------ELETHIEEYDR-EFNEIENASSSLG-------SDLAAREDALNQSLKELMHQARTVLKA------R 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1006 TRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVacsGQQQSDQIQKLKVELECLNQEYQSLQLS 1085
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622839299 1086 QSELTQTLEESQGQvQGAHLRLRQAQAQHSQEVRQLQEQMSRL 1128
Cdd:TIGR00618 837 LEEKSATLGEITHQ-LLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1007-1194 |
2.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1007 RQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEhrvtIQLLTQSLEEVACSGQQQSDQIQKLKVELECLN--QEYQSLQL 1084
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1085 SQSELTQTLEESQGQVQgAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQagRRLDAQREEHEKQLK 1164
Cdd:COG4717 140 ELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|..
gi 1622839299 1165 ATEERVEEAEMILKNME--MLLQEKVDELKEQ 1194
Cdd:COG4717 217 EAQEELEELEEELEQLEneLEAAALEERLKEA 248
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
848-1246 |
2.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 848 ERARSWSRGTQGQASEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGASRQEQLAAPEEGETKTALEREKDDmET 927
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 928 KLLHLEDVVRALE-KHVDLRENDRLEFHRLSEEnallkndlgrVRQELEAAESTHNAQRKEiEVLKKDKEKACSEMEVLT 1006
Cdd:PTZ00121 1397 KKKAEEDKKKADElKKAAAAKKKADEAKKKAEE----------KKKADEAKKKAEEAKKAD-EAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1007 RQNQNYKDQLSQLNDRvlqlGQEASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQ 1086
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEE----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1087 SELTQTLEESQG--QVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGRRLDAQREEHEKQLK 1164
Cdd:PTZ00121 1542 AEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1165 ATEERVEEAE----MILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKV 1240
Cdd:PTZ00121 1622 AEELKKAEEEkkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
....*.
gi 1622839299 1241 RALNKL 1246
Cdd:PTZ00121 1702 KKAEEL 1707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
910-1251 |
2.83e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 910 EEGETKTALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIE 989
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 990 VLK------KDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQ---SEEHRVTIQLLTQSLEEVAC---- 1056
Cdd:PRK03918 277 ELEekvkelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKrlee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1057 ---------SGQQQSDQIQKLKVELECLNQEyqslqlSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSR 1127
Cdd:PRK03918 357 leerhelyeEAKAKKEELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1128 LVPQDRVAELQRLLSLQGEQAG--RRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEK---------VDELKEQFE 1196
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseliklkelAEQLKELEE 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622839299 1197 KNTKSDllLKELYVENahlvRALQATEEKQRGAEKQSRILEEKVRALNKLVGRIA 1251
Cdd:PRK03918 511 KLKKYN--LEELEKKA----EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
257-282 |
2.88e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 39.08 E-value: 2.88e-04
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
902-1113 |
2.91e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 902 RQEQLAAPEEGETKTALEREKDDMETKLLHLEDVVRALEKHVDLREND---RLEFHRLSEENALLKNDLGRVRQELEAAE 978
Cdd:COG5185 304 SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESlteNLEAIKEEIENIVGEVELSKSSEELDSFK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 979 STHNAQRKEIEVLKKDKEKacSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVACSG 1058
Cdd:COG5185 384 DTIESTKESLDEIPQNQRG--YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1059 QQQSDQ-----IQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQ 1113
Cdd:COG5185 462 QSRLEEaydeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
857-1253 |
3.07e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 857 TQGQASEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGASRQEqlAAPEEGETKtALEREKDDMETKLLHLEDVV 936
Cdd:pfam10174 173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQ--LQPDPAKTK-ALQTVIEMKDTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 937 RALEK-----------HVDLRENDRLEFHRLSEENALLKNDLGRVRQELeaaesthnaQRKEIEVLKKDkekacSEMEVL 1005
Cdd:pfam10174 250 RDLEDevqmlktngllHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL---------SKKESELLALQ-----TKLETL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1006 TRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVtiqlltqSLEEVACSGQQQSDQIQKLKVELECLNQEYqslqls 1085
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRL-------RLEEKESFLNKKTKQLQDLTEEKSTLAGEI------ 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1086 qSELTQTLEESQGQVQGAHLRLRQAQAQhsqeVRQLQEQMSRLvpQDRVAELQR--------LLSLQGEQAG--RRLDAQ 1155
Cdd:pfam10174 383 -RDLKDMLDVKERKINVLQKKIENLQEQ----LRDKDKQLAGL--KERVKSLQTdssntdtaLTTLEEALSEkeRIIERL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1156 REEHEKQLKATEERVEEAEMILKNmemlLQEKVDELKEQFEKNTKSDLLLKElyvenahlvralQATEEKQRGAEKQSRI 1235
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKD----LKEKVSALQPELTEKESSLIDLKE------------HASSLASSGLKKDSKL 519
|
410 420
....*....|....*....|....
gi 1622839299 1236 ------LEEKVRALNKLVGRIAPA 1253
Cdd:pfam10174 520 ksleiaVEQKKEECSKLENQLKKA 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1064-1257 |
3.79e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1064 QIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSL 1143
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1144 QGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDELKEQFEKNTKS-DLLLKELYVENAHLVRALQAT 1222
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREAlDELRAELTLLNEEAANLRERL 826
|
170 180 190
....*....|....*....|....*....|....*
gi 1622839299 1223 EEKQRGAEKQSRILEEKVRALNKLVGRIAPAALSV 1257
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
909-1014 |
4.10e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 909 PEEGETKTALEREKDDMETKLLHLEDVVRALEKHV-DLREndrlEFHRLSEENALLKNDLGRVRQE--LEAAESTH-NAQ 984
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeELEA----ELEEKDERIERLERELSEARSEerREIRKDREiSRL 470
|
90 100 110
....*....|....*....|....*....|
gi 1622839299 985 RKEIEVLKKDKEKACSEMEVLTRQNQNYKD 1014
Cdd:COG2433 471 DREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1242 |
4.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 854 SRGTQGQASEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGA-SRQEQLAAPEEGETKTALEREKDDMEtkllHL 932
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARKAEDAK----KA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 933 EDVVRALE--KHVDLREND---RLEFHRLSEENALLKnDLGRVRQE--LEAAESTHNAQRKEIEVLKKDKEKACSE---- 1001
Cdd:PTZ00121 1179 EAARKAEEvrKAEELRKAEdarKAEAARKAEEERKAE-EARKAEDAkkAEAVKKAEEAKKDAEEAKKAEEERNNEEirkf 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1002 ----MEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEvacsgqqqSDQIQKLKVELECLNQ 1077
Cdd:PTZ00121 1258 eearMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AKKADEAKKKAEEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1078 EYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRllslQGEQAGRRLDAQRE 1157
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----KADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1158 EHEKQLKATEERVEEAEMILKNMEmllQEKVDELKEQFEKNTKSDLLLKElyVENAHLVRALQATEEKQRGAEKQSRILE 1237
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEE---KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
....*
gi 1622839299 1238 EKVRA 1242
Cdd:PTZ00121 1481 EAKKA 1485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1208 |
4.45e-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: 44.71 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 903 QEQLAAPEEGETKTALEREkddmETKLLH------LEDVVRALEKHVDLRENDRLEFHrlseenALLKNDLGRVRQELEA 976
Cdd:pfam05483 161 KETCARSAEKTKKYEYERE----ETRQVYmdlnnnIEKMILAFEELRVQAENARLEMH------FKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 977 AESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVlQLGQEASTHQAQSEEHrvtiqlLTQSLEEVAC 1056
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT-KLQDENLKELIEKKDH------LTKELEDIKM 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1057 SGQQQSDQIQKLKveleclnqeyQSLQLSQSELTQTLEESQGQVQgahlRLRQAQAQHSQEVRQLQEQMSRLvpqdrvae 1136
Cdd:pfam05483 304 SLQRSMSTQKALE----------EDLQIATKTICQLTEEKEAQME----ELNKAKAAHSFVVTEFEATTCSL-------- 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622839299 1137 lqrllslqgeqagrrldaqreehEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTKSDLLLKEL 1208
Cdd:pfam05483 362 -----------------------EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
862-1161 |
4.60e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 862 SEEQARAEGALESACQEHGVEVARRGSLPSHLQLAEPGASRQEQLAAPEEGETK---TALEREKDDMETKLLHLEDVVRA 938
Cdd:pfam07111 351 SQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKfvvNAMSSTQIWLETTMTRVEQAVAR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 939 LEKHvdlreNDRLEF--HRLSEENALL--KNDLGRVRQEL----EAAESTHNAQRKEIEVLKKDKEKACSEMEV------ 1004
Cdd:pfam07111 431 IPSL-----SNRLSYavRKVHTIKGLMarKVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDAELQLsahliq 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1005 --LTRQNQNYKDQLSQLNDRVLQLGQEasTHQAQSEEHRVTIQLltqsleEVACSGQQQS-DQIQKLKVELECLNQEY-Q 1080
Cdd:pfam07111 506 qeVGRAREQGEAERQQLSEVAQQLEQE--LQRAQESLASVGQQL------EVARQGQQEStEEAASLRQELTQQQEIYgQ 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1081 SLQLSQSELTQTLEEsqgQVQGAHLRLRQAQAQHSQEV---RQLQEQMSRlvPQDRVAELQRLLSLQGEQAGRRLDAQRE 1157
Cdd:pfam07111 578 ALQEKVAEVETRLRE---QLSDTKRRLNEARREQAKAVvslRQIQHRATQ--EKERNQELRRLQDEARKEEGQRLARRVQ 652
|
....
gi 1622839299 1158 EHEK 1161
Cdd:pfam07111 653 ELER 656
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
840-1203 |
8.47e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 840 EKPQSIQEERARSWSRGTQGQASEEQARAEGALESAC----QEHGVEVARRGSLPSHLQLAEPGASRQEQLAAPEEGETK 915
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEihirDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 916 TALEREKDDMETKLLHLEDVVRALEKH--VDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIE---- 989
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqt 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 990 ---VLKKDKEKACSEMEVLTRQNQN---YKDQLSQLNDRVLQLGQ-EASTHQAQSEEHRVtiQLLTQSLEEVACSGQQQS 1062
Cdd:TIGR00618 478 keqIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDIDNpGPLTRRMQRGEQTY--AQLETSEEDVYHQLTSER 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1063 DQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQgahLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLS 1142
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV---RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622839299 1143 LQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVdELKEQFEKNTKSDL 1203
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQL 692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
902-1245 |
1.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 902 RQEQLAAPEEG-----ETKTALEREKDDmetkllhLEDVVRalekhvDLREndRLEfhRLSEENALLKNDLGRVRQELEA 976
Cdd:PRK02224 249 RREELETLEAEiedlrETIAETEREREE-------LAEEVR------DLRE--RLE--ELEEERDDLLAEAGLDDADAEA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 977 AESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVAC 1056
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1057 SGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQA--------------QHSQEVRQLQ 1122
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1123 EQmsrlvpQDRVAELQ-RLLSLQGEQAGRrldAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKntks 1201
Cdd:PRK02224 472 ED------RERVEELEaELEDLEEEVEEV---EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER---- 538
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622839299 1202 dllLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRALNK 1245
Cdd:PRK02224 539 ---AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
963-1246 |
1.60e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 963 LKNDLGRVRQELEAAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRV 1042
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1043 TIQLLTQSLEEVACSGQqqsdQIQKLKVELECLNQEYQSLQLSQSELTQTLEESqgQVQGAHLRLRQAQAQHSQEVRQLQ 1122
Cdd:COG1340 93 ELDELRKELAELNKAGG----SIDKLRKEIERLEWRQQTEVLSPEEEKELVEKI--KELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1123 EQMSRLvpQDRVAELQRLLSLQGEQAGRRLDAQREEHEKQLKATEERVEEAEMILKnmemlLQEKVDELKEQFEKntksd 1202
Cdd:COG1340 167 AELKEL--RKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE-----AQEKADELHEEIIE----- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622839299 1203 llLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRALNKL 1246
Cdd:COG1340 235 --LQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
977-1174 |
1.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 977 AESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVAC 1056
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1057 SGQQQSDQIQKLKVELEclNQEYQSLqLSQSELTQTLEESQG----QVQGAHLRLRQAQAQHSQEVRQLQEQMSRLvpQD 1132
Cdd:COG3883 94 ALYRSGGSVSYLDVLLG--SESFSDF-LDRLSALSKIADADAdlleELKADKAELEAKKAELEAKLAELEALKAEL--EA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622839299 1133 RVAELQRLLSlQGEQAGRRLDAQREEHEKQLKATEERVEEAE 1174
Cdd:COG3883 169 AKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
218-279 |
2.13e-03 |
|
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319994 [Multi-domain] Cd Length: 101 Bit Score: 39.05 E-value: 2.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839299 218 ESQIRGMWEELGVGSRGHLSEQELAVVCQSVGL--RGLEKEELEDLFNKLDQDGDGKVSLEEFQ 279
Cdd:cd16251 33 EDQIKKVFQILDKDKSGFIEEEELKYILKGFSIagRDLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
257-292 |
2.65e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.53 E-value: 2.65e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1622839299 257 ELEDLFNKLDQDGDGKVSLEEFQLGLFSHEPALLLE 292
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE 36
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1030-1224 |
2.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1030 ASTHQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVE--LECLNQEYQSLQLSQSELTQTLEESQGQVQGAHLRL 1107
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1108 RQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGR---------RLDAQREEHEKQLKATEERVEEAemiLK 1178
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdviALRAQIAALRAQLQQEAQRILAS---LE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622839299 1179 NMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEE 1224
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1024-1243 |
3.69e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1024 LQLGQEASTHQAQSEEHRVTIQLLTQsLEEVACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGA 1103
Cdd:TIGR00618 149 LPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1104 HLRLRQAQAQHSQEVRQLQEQMSRLVPQDR--------VAELQRLLSLQGEQAGRRLDAQREEHEKQLKATEERVEEAEM 1175
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKkqqllkqlRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622839299 1176 ILKNMEMLLQEKVDELKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRILEEKVRAL 1243
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-559 |
3.88e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 360 REILQENSRLQKEIVEVAEKLSDSERLALKLQKDLEFVL--KDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDEL 437
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 438 QAELEGLwarlpknqhspswspggcRRQLSGLGPAGISFLGNsvpVSIETELMMEQVKEHY---EDLRTQLETKVNHYER 514
Cdd:TIGR02168 921 REKLAQL------------------ELRLEGLEVRIDNLQER---LSEEYSLTLEEAEALEnkiEDDEEEARRRLKRLEN 979
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622839299 515 EIAALKR-NFEKERKDMEQARRREVsvLEGQKADLEELHKKSQEVI 559
Cdd:TIGR02168 980 KIKELGPvNLAAIEEYEELKERYDF--LTAQKEDLTEAKETLEEAI 1023
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1131-1254 |
4.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1131 QDRVAELQRLLSLQGEQAgRRLDAQREEHEKQLKATEERVEEAEMILKNMEmlLQEKVDELKEQFEKNTKSDLLLKELYV 1210
Cdd:COG4913 616 EAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDDLAALEE 692
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622839299 1211 ENAHLVRALQATEEKQRGAEKQSRILEEKVRALNKLVGRIAPAA 1254
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1079-1236 |
4.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1079 YQSLQLSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGR--RLDAQR 1156
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARaeKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1157 EEHEKQLKATEERVEEAEMILKNMEMLLQEkVDELKEQFEKNTKSDLLLKELYVENAHLVRALqaTEEKQRGAEKQSRIL 1236
Cdd:PRK12705 105 NQLEEREKALSARELELEELEKQLDNELYR-VAGLTPEQARKLLLKLLDAELEEEKAQRVKKI--EEEADLEAERKAQNI 181
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
970-1200 |
4.90e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 970 VRQELEAAESTHNAQRKEIEVLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRV---LQLGQEASTHQAQSEEHRVTIQL 1046
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLaeaLEKLEEAEKAADESERGRKVLEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1047 LTQSLEEvacSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEesqgqvqgahlRLRQAQAQHSQEVRQLQEQMS 1126
Cdd:pfam00261 86 RALKDEE---KMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLE-----------RAEERAELAESKIVELEEELK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622839299 1127 rlvpqdRVAELQRLLSLQGEQAGRRLDAQREEHE---KQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEKNTK 1200
Cdd:pfam00261 152 ------VVGNNLKSLEASEEKASEREDKYEEQIRfltEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
956-1155 |
5.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 956 LSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVLKKDKEKACSEmevLTRQNQNYKDQLSQLNDRVlqlgqeASTHQA 1035
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERA------RALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1036 QSEEHRVTIQLLTQSLEE----------VACSGQQQSDQIQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAHL 1105
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1106 RLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAGRRLDAQ 1155
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1061-1231 |
5.64e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1061 QSDQIQKLKVELECLNQE---YQSLQLSQSELT-QTLEESQGQVQgahlRLRQAQAQHSQEVRQLQEQMSRLVPQ--DRV 1134
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQiktYNKNIEEQRKKNgENIARKQNKYD----ELVEEAKTIKAEIEELTDELLNLVMDieDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1135 AELQRLLSLQGEQAGRRLDAQREEH-----------EKQLKATEERVEEAEMILKNMEM---LLQEKVDELKEQFEKNTK 1200
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptcTQQISEGPDRITKIKDKLKELQHsleKLDTAIDELEEIMDEFNE 334
|
170 180 190
....*....|....*....|....*....|.
gi 1622839299 1201 SDLLLKELYVENAHLVRALQATEEKQRGAEK 1231
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKA 365
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
916-1240 |
6.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 916 TALEREKDDMETKLLHLEDVVR----ALEKHVDLRENDRLEFHRLSEENALLKNDLGRVRQELEAAESTHNAQRKEIEVL 991
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 992 KKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTIQLLTQSLEEVAC-------SGQQQSDQ 1064
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGSPHVET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1065 IQKLKVELECLNQEYQSLQLSQSELTQTLEESQGQVQGAhlrlrqAQAQHSQEVRQLQEQMsRLVPQDRVAELQRLLSLQ 1144
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE------DRIERLEERREDLEEL-IAERRETIEEKRERAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1145 GEQAGrRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEkVDELKEQFEKNTKSDLLLKELYVENAHLVRALQA--- 1221
Cdd:PRK02224 543 RERAA-ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLREKREAlae 620
|
330 340
....*....|....*....|...
gi 1622839299 1222 --TEEKQRGAEKQSRI--LEEKV 1240
Cdd:PRK02224 621 lnDERRERLAEKRERKreLEAEF 643
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
904-1194 |
6.40e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 904 EQLAAPEEGETKTAlerEKDDMETKLLHLEDVVRAL-EKHVDLRENDRLEFHRLSEENALlkNDLGRVRQELEAAESTHN 982
Cdd:TIGR00618 206 LTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTqQSHAYLTQKREAQEEQLKKQQLL--KQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 983 AQRKEIEvLKKDKEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQE---ASTHQAQSEEHRVTIQLLTQSLE------- 1052
Cdd:TIGR00618 281 ETQERIN-RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSqeihird 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1053 --EVACSGQQQSDQ-------IQKLKVELECLNQEYQSLqlsqSELTQTLEESQGQVQGAHLRLRQAQAQ----HSQEVR 1119
Cdd:TIGR00618 360 ahEVATSIREISCQqhtltqhIHTLQQQKTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQlahaKKQQEL 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622839299 1120 QLQEQMSRLVPQDRVAELQRLLSLQGEQAGRRLDAqREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQ 1194
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
899-1078 |
7.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 899 GASRQEQLAAPEE-----GETKTALEREKDDMETKLLHLEDVVRALEKHVDLREND------RLEFHRLSEENALLKN-- 965
Cdd:COG4913 605 GFDNRAKLAALEAelaelEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAELERLDAss 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 966 -DLGRVRQELEAAESTHNAQRKEIEVLKKDKEKacsemevLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQSEEHRVTI 1044
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGR-------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180 190
....*....|....*....|....*....|....
gi 1622839299 1045 QLLTQSLEEVAcsgQQQSDQIQKLKVELECLNQE 1078
Cdd:COG4913 758 ALGDAVERELR---ENLEERIDALRARLNRAEEE 788
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
913-1240 |
7.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 913 ETKTALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENAllkNDLGRVRQELEAAESTHNAQRKEIEVLK 992
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 993 KDKEKACSEMEVLTRQNQNYKDQLSQLNdrVLQLGQEasthQAQSEEHRVTIQLLTQSLEEVACSGQQQSDQIQKLKVEL 1072
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVT--IMERFQM----ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1073 ECLNQEYQSLQ---LSQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQEQMSRLVPQDRVAELQRLLSLQGEQAg 1149
Cdd:TIGR00606 839 DTVVSKIELNRkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF- 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1150 rrLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDELKEQFEK-NTKSDLLLKELYVENAHLVRALQATEEKQRG 1228
Cdd:TIGR00606 918 --LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
|
330
....*....|..
gi 1622839299 1229 AEKQSRILEEKV 1240
Cdd:TIGR00606 996 INEDMRLMRQDI 1007
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
220-285 |
7.43e-03 |
|
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.03 E-value: 7.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839299 220 QIRGMWEELGVGSRGHLSEQELAVVCQSVGLRgLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFSH 285
Cdd:cd15898 1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIR-VSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL 65
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1160-1245 |
9.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1160 EKQLKATEERVEEAEMILKNMEML---LQEKVDELKEQFEKnTKSDL------LLKELYVENAHLVRALQATEEKQRGAE 1230
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEEDK-LLEEAekeaqqAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90
....*....|....*
gi 1622839299 1231 KqSRILEEKVRALNK 1245
Cdd:PRK00409 605 K-AHELIEARKRLNK 618
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
918-1213 |
9.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 918 LEREKDDMETKLLHLEDVVRALEKHVDLREndRLefhrLSEENALLKNDLGrvrQELEAAEsthnAQRKEIEVLKKD--- 994
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALN--RL----LPRLNLLADETLA---DRVEEIR----EQLDEAEEAKRFvqq 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 995 KEKACSEMEVLTRQNQNYKDQLSQLNDRVLQLGQEASTHQAQseehrvtIQLLTQSLEEVACSGQQQSDQIqklkvelec 1074
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQ-------AFALTEVVQRRAHFSYEDAAEM--------- 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839299 1075 LNQEYQSlqlsQSELTQTLEESQGQVQGAHLRLRQAQAQHSQEVRQLQE-QMSRLVPQDRVAELQRLLSLQG----EQAG 1149
Cdd:PRK04863 980 LAKNSDL----NEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASlKSSYDAKRQMLQELKQELQDLGvpadSGAE 1055
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839299 1150 RRLDAQREEHEKQLKATEERVEEAEMILKnmemLLQEKVDELKEQFEKNTKSDLLLKELyVENA 1213
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNQLEKQLT----FCEAEMDNLTKKLRKLERDYHEMREQ-VVNA 1114
|
|
| |
