|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1020-1353 |
1.56e-13 |
|
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: 75.86 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1020 AREAERQLV-LRLKERCEQQTRQLGVAQGELKRAicgfdaLAVATQHFFRKN-ESALVKEKELSIELANIRDEVAFHTAK 1097
Cdd:TIGR02168 195 LNELERQLKsLERQAEKAERYKELKAELRELELA------LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1098 CEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQ---EEHGDQLLSIRCQHQEQVEDLTAShDAA 1174
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELY-ALANEISRLEQQKQIL-RERLANLErqlEELEAQLEELESKLDELAEELAEL-EEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1175 LLEMENNHTVaitiLQDDHD--HKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1252
Cdd:TIGR02168 346 LEELKEELES----LEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1253 EQLEIALAPYQH-LEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDqntvVTRQL 1331
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD----SLERL 497
|
330 340
....*....|....*....|..
gi 2462536697 1332 SEENANLQEYVEKETQEKKRLS 1353
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1076-1359 |
8.18e-12 |
|
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: 70.09 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1076 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLS 1155
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1156 I----RCQHQEQVEDLTASHDAALLEMENNHTvAITILQDDHD------HKVQELMSTHELEKKELEENFEKLRLSLQDQ 1225
Cdd:TIGR02168 772 EaeeeLAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1226 VDTLTFQSQSLRDrarrfEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEE 1305
Cdd:TIGR02168 851 SEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE---LRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1306 KIQVLQQQNEDLKARIDQNtvvTRQLSEEN-------ANLQEYVEKETQE-KKRLSRTNEEL 1359
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNL---QERLSEEYsltleeaEALENKIEDDEEEaRRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1359 |
1.31e-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: 69.70 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1098
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1099 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1178
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALD-ELRAELTLLNEEAA-NLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1179 ENnHTVAITILQDDHDHKVQELMSThelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1258
Cdd:TIGR02168 862 EE-LEELIEELESELEALLNERASL------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1259 LApyqhleedmkslKQVLEMKNQQIHEQ--EKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVT-------R 1329
Cdd:TIGR02168 929 LR------------LEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyE 996
|
330 340 350
....*....|....*....|....*....|
gi 2462536697 1330 QLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1093-1358 |
3.21e-10 |
|
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: 64.76 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1093 FHTAKCEKLQKEKEELERRFE--------DEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSiRCQHQEQV 1164
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVErrrkleeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE-RIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1165 EDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRlslQDQVDTLTFQSQSLRD-RARRF 1243
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEeRAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1244 EEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQ-IHEQEKKILELEKLAEKNIILEE--KIQVLQQQNEDLKA- 1319
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKa 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462536697 1320 -------RIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 1358
Cdd:pfam17380 529 iyeeerrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1100-1360 |
1.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1100 KLQKEKEELERR---FEDEVKRlgwQQQAELQELEERLQLQFEAEMARLQEEHGdQLLSIRCQHQEQVEDLTAshdaaLL 1176
Cdd:COG1196 217 ELKEELKELEAElllLKLRELE---AELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEE-----AQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1177 EMENNHTVAITILQDDHDHKVQELmsthelekKELEENFEKlrlsLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLE 1256
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERR--------RELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1257 IAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNtvvTRQLSEENA 1336
Cdd:COG1196 356 AE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL---EEELEELEE 428
|
250 260
....*....|....*....|....
gi 2462536697 1337 NLQEYVEKETQEKKRLSRTNEELL 1360
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1079-1359 |
1.67e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1079 ELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEdEVKRLGWQQQAELQELEERLQLQfEAEMARLQEEhgdqllsirc 1158
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISAL-RKDLARLEAE---------- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1159 qhQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRD 1238
Cdd:TIGR02168 742 --VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA----------------EAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1239 RARRFEEALRkNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLK 1318
Cdd:TIGR02168 804 ALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462536697 1319 ARIDQNTVVTR-QLSEENANLQEyVEKETQEKKR-LSRTNEEL 1359
Cdd:TIGR02168 883 ASLEEALALLRsELEELSEELRE-LESKRSELRReLEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1019-1343 |
3.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLVLRLKERcEQQTRQLGVAQGELKRAIcgfdalavatqhffRKNESALVKEKELSIELANIRDEVafhtakc 1098
Cdd:COG1196 219 KEELKELEAELLLLKL-RELEAELEELEAELEELE--------------AELEELEAELAELEAELEELRLEL------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1099 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1178
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA-RLEQDIARLEERRR-ELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1179 EnnhtvaitILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1258
Cdd:COG1196 354 E--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1259 LApyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1338
Cdd:COG1196 426 LE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
....*
gi 2462536697 1339 QEYVE 1343
Cdd:COG1196 504 EGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1021-1323 |
1.25e-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: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1021 REAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKElsiELANIRDEVAFHTAKCEK 1100
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1101 LQKEKEELERRFEDEvkrlGWQQ-QAELQELEE---RLQLQFEAEMARLQEEHGD-QLLSIRCQH-QEQVEDLTASHDAA 1174
Cdd:TIGR02169 777 LEEALNDLEARLSHS----RIPEiQAELSKLEEevsRIEARLREIEQKLNRLTLEkEYLEKEIQElQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1175 LLEMENNHTVAITILQ--DDHDHKVQELMSTHELEKKELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1252
Cdd:TIGR02169 853 EKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1253 EQLEIALAPYQHLEE-----DMKSLKQVLEMKNQQIHEQE----KKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQ 1323
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIpeeelSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1076-1359 |
5.21e-08 |
|
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: 57.72 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1076 KEKElsIELANIRDEVAFHTAKCEKLQKEKEELERRFEdevkrlgwQQQAELQELEERLQlQFEAEMARLQEEHgDQLLS 1155
Cdd:TIGR04523 366 EEKQ--NEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIK-KLQQEKELLEKEI-ERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1156 IRCQHQEQVEDLTaSHDAALLEMENNH--------------TVAITILQDDHDHKVQELMSTHELEKKELEENFEklrls 1221
Cdd:TIGR04523 434 TIIKNNSEIKDLT-NQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1222 LQDQVDTLTFQSQSLRDRARRFE-EALRKNTEeqleialapYQHLEEDMKSLKQVLEMKN--QQIHEQEKKILEL----E 1294
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLEsEKKEKESK---------ISDLEDELNKDDFELKKENleKEIDEKNKEIEELkqtqK 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462536697 1295 KLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1017-1376 |
6.13e-08 |
|
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: 57.44 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1017 DPQAREAER--QLVLRLKERCE-QQTRQLGVAQG--ELKRAICGFDALAVATQHFFRKNESALVKEKelsIELANIRDEV 1091
Cdd:pfam15921 422 DDRNMEVQRleALLKAMKSECQgQMERQMAAIQGknESLEKVSSLTAQLESTKEMLRKVVEELTAKK---MTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1092 AFHTAKCEklqkEKEELERRFEDEVKRLGWQQQAELQEL------EERLQ-LQFEAEMARLQEEHGDQLLSIRCQHQEQV 1164
Cdd:pfam15921 499 SDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELqhlkneGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1165 EDLTASH---------DAALLEMENN----HTVAITILQDDHDHKVQEL-------------MSTHELEKKELEENFEKL 1218
Cdd:pfam15921 575 TQLVGQHgrtagamqvEKAQLEKEINdrrlELQEFKILKDKKDAKIRELearvsdlelekvkLVNAGSERLRAVKDIKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1219 RLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEE----------QLEIALAPYQHLEEDMKSL--------KQVLEMKN 1280
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmetttnklkmQLKSAQSELEQTRNTLKSMegsdghamKVAMGMQK 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1281 Q------QIHEQEKKILELEKL-----AEKNIILEEK--------------------IQVLQQQNEDLKARIDQNTVVTR 1329
Cdd:pfam15921 735 QitakrgQIDALQSKIQFLEEAmtnanKEKHFLKEEKnklsqelstvateknkmageLEVLRSQERRLKEKVANMEVALD 814
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462536697 1330 QLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSPIKLSP 1376
Cdd:pfam15921 815 KASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKP 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1072-1323 |
9.72e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1072 SALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFE--DEVKRLGWQQ------QAELQELEERL--------- 1134
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1135 --QLQF-----EAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMsthele 1207
Cdd:COG4913 687 laALEEqleelEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL------ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1208 kkeLEENFEKLRLSLQDQVDTltfqsqsLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM----KNQQI 1283
Cdd:COG4913 760 ---GDAVERELRENLEERIDA-------LRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALldrlEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462536697 1284 HEQEKKILELEKLAEKNIIlEEKIQVLQQQNEDLKARIDQ 1323
Cdd:COG4913 830 PEYEERFKELLNENSIEFV-ADLLSKLRRAIREIKERIDP 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1031-1359 |
1.16e-07 |
|
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: 56.65 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1031 LKERCEQQ---TRQLGVAQGELKRAICGFDAL----AVATQHFFRknesaLVKEKELSIELANIRDE------VAFHTAK 1097
Cdd:pfam05483 284 LKELIEKKdhlTKELEDIKMSLQRSMSTQKALeedlQIATKTICQ-----LTEEKEAQMEELNKAKAahsfvvTEFEATT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1098 C---EKLQKEKEELERRfEDEVKRLGWQQQAELQELEERLQLQF--EAEMARLQEEHGDQ--LLSIRCQHQEQVEDLTAS 1170
Cdd:pfam05483 359 CsleELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFKNnkEVELEELKKILAEDekLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1171 HD--AALLEMENNHT----VAITILQDDHDHKVQELMSTHELEKKELEENFEklrlsLQDQVDTLTFQSQSLRDRARRFE 1244
Cdd:pfam05483 438 EQelIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1245 EALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKI-LELEKLAEKNIILEEKIQVLQQQNEDL 1317
Cdd:pfam05483 513 LELKKhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462536697 1318 KARIDQntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:pfam05483 593 ENKCNN---LKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1019-1359 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAE-RQLVLRLKErCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEK--ELSIELANIRDEVAFHT 1095
Cdd:COG4717 84 EEKEEEyAELQEELEE-LEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 ---AKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQ------LQFEAEMARLQEEHGDqllsIRCQHQEQVED 1166
Cdd:COG4717 160 eleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEelqqrlAELEEELEEAQEELEE----LEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1167 LTASHDAALLEMENNHTVAITIlqddhdhkVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEA 1246
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAA--------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1247 LRKNTEEQLEIA-----LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQN----EDL 1317
Cdd:COG4717 308 QALPALEELEEEeleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2462536697 1318 KARIDQN----------TVVTRQLSEENANLQEYVEKETQE--KKRLSRTNEEL 1359
Cdd:COG4717 388 RAALEQAeeyqelkeelEELEEQLEELLGELEELLEALDEEelEEELEELEEEL 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1122-1365 |
3.08e-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: 55.46 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1122 QQQAELQELEERLQlQFEAEMARLQEE--HGDQLLSircQHQEQVEDLTASHDAALLEMEnnhtvaitILQDDHDHKVQE 1199
Cdd:TIGR02169 671 SEPAELQRLRERLE-GLKRELSSLQSElrRIENRLD---ELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1200 LmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlAPYQHL-EEDMKSLKQVLEM 1278
Cdd:TIGR02169 739 L---------------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLsHSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1279 KNQQIHEQEKKILELE----KLAEKNIILEEKIQVLQQQNEDLKARIDQN---------------------TVVTRQLSE 1333
Cdd:TIGR02169 803 LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienlngkkeeleeeleelEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|..
gi 2462536697 1334 ENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1365
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1080-1365 |
3.28e-07 |
|
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: 54.97 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1080 LSIELANIRDEVAFHTAKCEKLQKEKEELErrfedevKRLGWQQQA-ELQELEERLQLQfEAEMARLQEEhgdqlLSIRC 1158
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQE-------EQLKKQQLLkQLRARIEELRAQ-EAVLEETQER-----INRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1159 QHQEQVEdltasHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeLEENFEKLRLSLQDQVDTL-TFQSQSLR 1237
Cdd:TIGR00618 291 KAAPLAA-----HIKAVTQIEQQAQRIHTELQSKMRSRAKLLM---------KRAAHVKQQSSIEEQRRLLqTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1238 DRARRFEEALRKnteEQLEIALAPYQHLeedmKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDL 1317
Cdd:TIGR00618 357 IRDAHEVATSIR---EISCQQHTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462536697 1318 KARIdqntvvtrQLSEENANLQE-YVEKETQEKK-------RLSRTNEELLWKLQT 1365
Cdd:TIGR00618 430 KKQQ--------ELQQRYAELCAaAITCTAQCEKlekihlqESAQSLKEREQQLQT 477
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1015-1359 |
5.04e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1015 KPDPQAREAERQLVlRLKERCEQQTRQLGVAQGELKraicgfDALAVATQHFFRKNEsALVKEKELSIELANIRDEVAFH 1094
Cdd:pfam01576 212 KLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQ------AALARLEEETAQKNN-ALKKIRELEAQISELQEDLESE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1095 TAKCEKLQKEK----EELE---RRFEDEVKRLGWQQQaelqeleerLQLQFEAEMARLQ----EE---HGDQLLSIRCQH 1160
Cdd:pfam01576 284 RAARNKAEKQRrdlgEELEalkTELEDTLDTTAAQQE---------LRSKREQEVTELKkaleEEtrsHEAQLQEMRQKH 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1161 QEQVEDLTASHDAA------------LLEMENNHTVA-ITILQD---DHDHK-------VQELMSTHELEkkeleenfEK 1217
Cdd:pfam01576 355 TQALEELTEQLEQAkrnkanlekakqALESENAELQAeLRTLQQakqDSEHKrkklegqLQELQARLSES--------ER 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1218 LRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEE--QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILE-LE 1294
Cdd:pfam01576 427 QRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDvsSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEqLE 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1295 KLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKKRLSRTNEEL 1359
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRL 578
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1036-1312 |
5.30e-07 |
|
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: 54.57 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1036 EQQTR--QLGVAQGELKRA--ICGFDAL----AVATQHFFRKNESA-----LVKEKELSIE-------------LANIRD 1089
Cdd:COG3096 407 VQQTRaiQYQQAVQALEKAraLCGLPDLtpenAEDYLAAFRAKEQQateevLELEQKLSVAdaarrqfekayelVCKIAG 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1090 EV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQFEAEmaRLQEEHGdQLLSIRCQHQEQ 1163
Cdd:COG3096 487 EVersqAWQTAR---------ELLRRYRSQQALAQRLQQlrAQLAELEQRLRQQQNAE--RLLEEFC-QRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1164 VEDLTASHDAallemennhtvaitiLQDDHDHKVQElmsthelekkeleenFEKLRLSLQDQVDTLTFQSQSLRDRA--- 1240
Cdd:COG3096 555 LEELLAELEA---------------QLEELEEQAAE---------------AVEQRSELRQQLEQLRARIKELAARApaw 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1241 RRFEEALRKnTEEQLEIALAPYQHLEEDMkslKQVLEmknqqiHEQEKKILElEKLAEKNIILEEKIQVLQQ 1312
Cdd:COG3096 605 LAAQDALER-LREQSGEALADSQEVTAAM---QQLLE------REREATVER-DELAARKQALESQIERLSQ 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1234-1364 |
1.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1234 QSLRDRARRFEEALRKNtEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ 1313
Cdd:COG1196 235 RELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEER 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462536697 1314 NEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1364
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1066-1365 |
1.22e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1066 FFRKNESAL-------VKEKELSIELANIRDEVafhtakcEKLQKEKEELERrFEDEVKRL----GWQQQAELQELEERL 1134
Cdd:TIGR02169 168 FDRKKEKALeeleeveENIERLDLIIDEKRQQL-------ERLRREREKAER-YQALLKEKreyeGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1135 QlQFEAEMARLQEEhgdqllsircqhqeqVEDLTASHDAALLEMEnnhtvAITILQDDHDHKVQELMSTHELEKKELEEN 1214
Cdd:TIGR02169 240 E-AIERQLASLEEE---------------LEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1215 FEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE--EQLEIALAPYQ----HLEEDMKSLKQVLEMKNQqiheqek 1288
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERkrrdKLTEEYAELKEELEDLRA------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1289 kilELEKLAEKNIILEEKIQVLQQQNEDLKARI-------DQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELL- 1360
Cdd:TIGR02169 372 ---ELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAl 448
|
330
....*....|.
gi 2462536697 1361 ------WKLQT 1365
Cdd:TIGR02169 449 eikkqeWKLEQ 459
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1078-1357 |
1.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAE-LQELEERLqlqfeaemarlqEEHGDQLLSI 1156
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKL------------KKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1157 RCQHQEQVEDLtashdaaLLEMENNhtvaITILQDDHDhKVQELMStHELEKKELEENFEKLRLSLQDQVDTLTFQS-QS 1235
Cdd:PRK03918 523 KAEEYEKLKEK-------LIKLKGE----IKSLKKELE-KLEELKK-KLAELEKKLDELEEELAELLKELEELGFESvEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1236 LRDRARRFEEALR-----KNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILEL---------EKLAEKNI 1301
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyEELREEYL 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462536697 1302 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 1357
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1078-1323 |
1.77e-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: 52.07 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQEehgdQLLSIR 1157
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAAL-EAELAELEK----EIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1158 CQHQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLR 1237
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1238 DrarrfeealrknTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 1317
Cdd:COG4942 164 A------------LRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAE---LAAELAELQQEAEEL 225
|
....*.
gi 2462536697 1318 KARIDQ 1323
Cdd:COG4942 226 EALIAR 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1028-1349 |
3.22e-06 |
|
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: 51.65 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1028 VLRLKERCEQQTRQLGVAQG-------ELKRAICGFDALAVATQHFFRKNESALvkeKELSIELANIRDEVAFHTAKCEK 1100
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQL---KIITMELQKKSSELEEMTKFKNN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1101 LQKEKEELERRFEDEVKRLGWQQQAElqELEERLQLQfEAEM-----ARLQEEHG--DQLLSIRCQHQ---EQVED---- 1166
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFE--KIAEELKGK-EQELifllqAREKEIHDleIQLTAIKTSEEhylKEVEDlkte 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1167 ----------LTASHDAALLEME------NNHTVAITILQDD--HDHKVQELMSTHELEKKELEENF----EKLRLSLQD 1224
Cdd:pfam05483 480 lekeklknieLTAHCDKLLLENKeltqeaSDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLrdelESVREEFIQ 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1225 QVDTLTFQSQSLRDRARRFEEALRK-------------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL 1291
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKkekqmkilenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462536697 1292 ELE-KLAEKNIILEEKIQVLQQQNEDLKarIDQNTVV-----TRQLSEENANLQEYVEKETQEK 1349
Cdd:pfam05483 640 KLElELASAKQKFEEIIDNYQKEIEDKK--ISEEKLLeevekAKAIADEAVKLQKEIDKRCQHK 701
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1222-1356 |
3.50e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1222 LQDQVDTLTFQSQSLRDRARRFEEALRKN------TEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKkilELEK 1295
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQArseleqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE---ELEE 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462536697 1296 LAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1356
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1097-1354 |
4.47e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1097 KCEKLQKEKEELERRFEDEVKRLGWQ---QQAELQEL-------EERLQL--------------------QFEAEMARLQ 1146
Cdd:pfam01576 198 KEEKGRQELEKAKRKLEGESTDLQEQiaeLQAQIAELraqlakkEEELQAalarleeetaqknnalkkirELEAQISELQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1147 E----------------------------EHGDQLLSIRCQHQ-----EQ--------VEDLTASHDAALLEMENNHTVA 1185
Cdd:pfam01576 278 EdleseraarnkaekqrrdlgeelealktELEDTLDTTAAQQElrskrEQevtelkkaLEEETRSHEAQLQEMRQKHTQA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1186 ITILQDDHDHkvqelmstheleKKELEENFEKLRLSLQDQVDTLTFQSQSLRdRARRFEEALRKNTEEQLEIALAPY--- 1262
Cdd:pfam01576 358 LEELTEQLEQ------------AKRNKANLEKAKQALESENAELQAELRTLQ-QAKQDSEHKRKKLEGQLQELQARLses 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1263 ----QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ-NEDLKARIDQNTVVtRQLSEENAN 1337
Cdd:pfam01576 425 erqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS---LESQLQDTQELlQEETRQKLNLSTRL-RQLEDERNS 500
|
330
....*....|....*..
gi 2462536697 1338 LQEYVEKETQEKKRLSR 1354
Cdd:pfam01576 501 LQEQLEEEEEAKRNVER 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1016-1367 |
4.96e-06 |
|
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: 51.12 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1016 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1095
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 AKCEKLQKEKEELERR-----------------------FEDEVKRLGWQQQ---AELQELEERLQlQFEAEMARLQEEH 1149
Cdd:TIGR00618 494 ARLLELQEEPCPLCGScihpnparqdidnpgpltrrmqrGEQTYAQLETSEEdvyHQLTSERKQRA-SLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1150 gDQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEK----LRLSLQDQ 1225
Cdd:TIGR00618 573 -SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQelalKLTALHAL 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1226 VDTLTFQSQSLRDRARRFEEALRKnteEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniilee 1305
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELL---ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------ 722
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1306 kiqvLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKrlSRTNEELLWKLQTGD 1367
Cdd:TIGR00618 723 ----IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH--FNNNEEVTAALQTGA 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1099-1341 |
7.42e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1099 EKLQKEKEELERRFedevKRLGWQQQAELQELEERLQlQFEAEMARLQEEHgDQLLSIRcqhqEQVEDLTAshdaallem 1178
Cdd:COG4717 49 ERLEKEADELFKPQ----GRKPELNLKELKELEEELK-EAEEKEEEYAELQ-EELEELE----EELEELEA--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1179 ennhtvAITILQDDHDhkvqelmsthelekkeleenfeklRLSLQDQVDTLTFQSQSLRDRARRFEEALrknteEQLEIA 1258
Cdd:COG4717 110 ------ELEELREELE------------------------KLEKLLQLLPLYQELEALEAELAELPERL-----EELEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1259 LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKK------------ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTV 1326
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LE 233
|
250
....*....|....*
gi 2462536697 1327 VTRQLSEENANLQEY 1341
Cdd:COG4717 234 NELEAAALEERLKEA 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1078-1359 |
7.54e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIELANIRDEVafhtakcEKLQKEKEELERRFE--DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlls 1155
Cdd:PRK03918 210 NEISSELPELREEL-------EKLEKEVKELEELKEeiEELEKELESLEGSKRKLEEKIR-ELEERIEELKKE------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1156 IRcQHQEQVEDLTAshdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTFQSQS 1235
Cdd:PRK03918 275 IE-ELEEKVKELKE------LKEKAEEYIKLSEFYEEYLDELREI---------------EKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1236 LRDRARRFEEALRKNTEEQLEIA-LAPYQHLEEDMKSLKQVLE-----MKNQQIHEQEKKILELEK----LAEKNIILEE 1305
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEeLEERHELYEEAKAKKEELErlkkrLTGLTPEKLEKELEELEKakeeIEEEISKITA 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462536697 1306 KIQVLQQQNEDLKARIDQ-------NTVVTRQLSEENAnlQEYVEKETQEKKRLSRTNEEL 1359
Cdd:PRK03918 413 RIGELKKEIKELKKAIEElkkakgkCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEI 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1016-1357 |
8.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1016 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1095
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 AKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQE--EHGDQLLSI-RCQHQEQ-VE 1165
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEdfleelREERDELREREA-ELEATLRTARErvEEAEALLEAgKCPECGQpVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1166 DltASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRARR 1242
Cdd:PRK02224 463 G--SPHVETI---------------EEDRERVEEL---------------EAELEDLEEEVEEVEErleRAEDLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1243 FEEAL--RKNTEEQLEIALAPYQHLEEDMKSL---KQVLEMKNQqihEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 1317
Cdd:PRK02224 511 IERLEerREDLEELIAERRETIEEKRERAEELrerAAELEAEAE---EKREAAAEAEEEAEE---AREEVAELNSKLAEL 584
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1318 KARIDQ-NTVVTR---------QLSEENANLQEYVEKETQEKKRLSRTNE 1357
Cdd:PRK02224 585 KERIESlERIRTLlaaiadaedEIERLREKREALAELNDERRERLAEKRE 634
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1002-1358 |
1.13e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1002 KQRTAAARNGFPPKPDPQAREAErqlvlrLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHffrknESALVKEKELS 1081
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALESE------LREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA-----TPELLLQLENF 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1082 IELAN-IRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG------WQQQAELQELEERLQ------LQFEAEMARLQEE 1148
Cdd:pfam12128 470 DERIErAREEQEAANAEVERLQSELRQARKRRDQASEALRqasrrlEERQSALDELELQLFpqagtlLHFLRKEAPDWEQ 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1149 HGDQLLSIRCQHQeqvEDLTASHDAALLEMENN-HTVAITILQDDHDHKVQelmsthelekkeleeNFEKLRLSLqDQVD 1227
Cdd:pfam12128 550 SIGKVISPELLHR---TDLDPEVWDGSVGGELNlYGVKLDLKRIDVPEWAA---------------SEEELRERL-DKAE 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1228 TlTFQSQslRDRARRFEEAL---RKNTEEQ---LEIALAPYQHLEEDMKSL---KQVLEMK-NQQIHE-QEKKILELEKL 1296
Cdd:pfam12128 611 E-ALQSA--REKQAAAEEQLvqaNGELEKAsreETFARTALKNARLDLRRLfdeKQSEKDKkNKALAErKDSANERLNSL 687
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462536697 1297 -AEKNIILEEKIQVLQQQNEDLK----ARIDQNTVVTRQLSEENANLQEYVEK-ETQEKKRLSRTNEE 1358
Cdd:pfam12128 688 eAQLKQLDKKHQAWLEEQKEQKReartEKQAYWQVVEGALDAQLALLKAAIAArRSGAKAELKALETW 755
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1019-1320 |
1.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAErQLVLRLKERC--------EQQTR--QLGVAQGELKRA--ICGFDALAV----ATQHFFRKNESALVK-----E 1077
Cdd:PRK04863 384 RAEAAE-EEVDELKSQLadyqqaldVQQTRaiQYQQAVQALERAkqLCGLPDLTAdnaeDWLEEFQAKEQEATEellslE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIE-------------LANIRDEV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQF 1138
Cdd:PRK04863 463 QKLSVAqaahsqfeqayqlVRKIAGEVsrseAWDVAR---------ELLRRLREQRHLAEQLQQlrMRLSELEQRLRQQQ 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1139 EAEmaRLQEEHGdQLLSIRCQHQEQVEDLTASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKL 1218
Cdd:PRK04863 534 RAE--RLLAEFC-KRLGKNLDDEDELEQLQEELEARL---------------ESLSESVSEA---------------RER 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1219 RLSLQDQVDTLTFQSQSLRDRARRFEEAlrKNTEEQLeialapYQHLEEDMKSLKQVLE-MKNQQIHEQEkkilelekLA 1297
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAA--QDALARL------REQSGEEFEDSQDVTEyMQQLLERERE--------LT 644
|
330 340
....*....|....*....|...
gi 2462536697 1298 EKNIILEEKIQVLQQQNEDLKAR 1320
Cdd:PRK04863 645 VERDELAARKQALDEEIERLSQP 667
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1078-1370 |
1.46e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQEEHG- 1150
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeleslQEEAEELQEELE-ELQKERQDLEQQRKq 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1151 -----DQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQ 1225
Cdd:COG4372 134 leaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1226 VDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM--KNQQIHEQEKKILELEKLAEKNIIL 1303
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1304 EEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTS 1370
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1067-1348 |
1.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1067 FRKNESALVKEKELSIELANIRDEVAFHTAkcEKLQKEKEELE------RRFEDEVKRLGwQQQAELQELEERLQLqFEA 1140
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEklkeklIKLKGEIKSLK-KELEKLEELKKKLAE-LEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1141 EMARLQEEHGDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleENFEKLRL 1220
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREE-------------KELKKLEE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1221 SLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN 1300
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEE-------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462536697 1301 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQE 1348
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1250-1364 |
1.90e-05 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 46.07 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKIlELEKLAEKNiiLEEKIQVLQQQNEDLKARIDQNTVVTR 1329
Cdd:pfam09744 33 NVLELLESLASRNQEHNVELEELREDNE---QLETQYEREK-ALRKRAEEE--LEEIEDQWEQETKDLLSQVESLEEENR 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462536697 1330 QLSEENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 1364
Cdd:pfam09744 107 RLEADHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1069-1359 |
2.01e-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: 49.25 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1069 KNESALVKEKELSIE--LANIRDEvafHTAKCEKLQ--KEKEELERRFEDEVKRLGwQQQAELQELEERLQLQFEAEMAR 1144
Cdd:TIGR04523 172 ENELNLLEKEKLNIQknIDKIKNK---LLKLELLLSnlKKKIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1145 LQEEHgDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVaITILQDDhdhkVQELMSthelekkeleenfEKLRLSLQD 1224
Cdd:TIGR04523 248 ISNTQ-TQLNQLKDEQNKIKKQL----SEKQKELEQNNKK-IKELEKQ----LNQLKS-------------EISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1225 QVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlapyqHLEEDMKSLKQV---LEMKNQQIHEQ-EKKILELEKLAEKN 1300
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----QLNEQISQLKKEltnSESENSEKQRElEEKQNEIEKLKKEN 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1301 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1108-1336 |
2.10e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1108 LERRFEDEVKRLGWQQQaELQELEERLQlQFEAEMARLQEEHG------------DQLLSIRCQH---QEQVEDLTASHD 1172
Cdd:COG3206 166 LELRREEARKALEFLEE-QLPELRKELE-EAEAALEEFRQKNGlvdlseeaklllQQLSELESQLaeaRAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1173 AALLEMENNHTVAITILQDDhdhKVQELMSthelekkeleeNFEKLRLSLQDQVDTLTFQS---QSLRDRARRFEEALRK 1249
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSP---VIQQLRA-----------QLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTVVTR 1329
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-ARLAE 381
|
....*..
gi 2462536697 1330 QLSEENA 1336
Cdd:COG3206 382 ALTVGNV 388
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1029-1362 |
2.29e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1029 LRLKERCEQQTRQLGVAQgelKRAI----CGFDALAVATQHFFRKNESaLVKEKELSIELANIRDEVAFHTA-KCEKLQK 1103
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQ---RKAIqelqFENEKVSLKLEEEIQENKD-LIKENNATRHLCNLLKETCARSAeKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1104 EKEELERRFEDevkrlgwqqqaeLQELEERLQLQFEAemARLQEEHgdqllsircqhqeqvedltashdaALLEMENNht 1183
Cdd:pfam05483 177 EREETRQVYMD------------LNNNIEKMILAFEE--LRVQAEN------------------------ARLEMHFK-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1184 vaitiLQDDHDhKVQELMSTHELEKKELEENFEKLRLSL---QDQVDTLTFQSQSLRDRARRFEEA-------LRKNTEE 1253
Cdd:pfam05483 217 -----LKEDHE-KIQHLEEEYKKEINDKEKQVSLLLIQItekENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1254 Q-------------LEIALAPYQHLEEDM----KSLKQVLEMKNQQIHEQEK----KILELEKLAEKNIILEEKIQVLQQ 1312
Cdd:pfam05483 291 KdhltkeledikmsLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKakaaHSFVVTEFEATTCSLEELLRTEQQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462536697 1313 QnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELLWK 1362
Cdd:pfam05483 371 R---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDE 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1017-1358 |
3.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1017 DPQAREAERQL--VLRLKERCEQQTRQLGVAQGELKRAICGFDALAVAT-QHFFRKNESALVKEKELSIELANIRDEVAF 1093
Cdd:COG4717 145 PERLEELEERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1094 HTAKCEKLQKEKE--ELERRFEDE--------------------------------------VKRLGWQQQAELQELEER 1133
Cdd:COG4717 225 LEEELEQLENELEaaALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1134 LQLQFEAEMARLQEEHGDQLLSIR----CQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELM-STHELEK 1208
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLaEAGVEDE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1209 KELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEMKNQQIHEQEK 1288
Cdd:COG4717 385 EELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL---EELEEELEELEEELEELREELAELEA 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462536697 1289 KILELEKlaekniilEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQ---EYVEKETQ--EKKRLSRTNEE 1358
Cdd:COG4717 461 ELEQLEE--------DGELAELLQELEELKAEL-------RELAEEWAALKlalELLEEAREeyREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1095-1320 |
5.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1095 TAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQL------QFEAEMARLQEEHGD---QLLSIRCQ 1159
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKkeekalLKQLAALERRIAAlarrirALEQELAALEAELAElekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1160 HQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLRDR 1239
Cdd:COG4942 99 LEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1240 ARRFEEAlRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDLKA 1319
Cdd:COG4942 166 RAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAE 241
|
.
gi 2462536697 1320 R 1320
Cdd:COG4942 242 R 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1073-1358 |
5.79e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1073 ALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLgwQQQAELQE-LEERLQLQFEAEMARLQEehGD 1151
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK--RYRQELEEqIEEREQKRQEEYEEKLQE--RE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1152 QLLSIrcQHQEQVEDltashdaaLLEMENNHtvaitilqddhdhkvqelmsthelekkeleenfeKLRLSLQDQVDtltf 1231
Cdd:pfam13868 102 QMDEI--VERIQEED--------QAEAEEKL----------------------------------EKQRQLREEID---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1232 qsqslrdrarRFEEALRKNTEEQLEialapyQHLEEDMKsLKQVLEMKNQQIHEQEKKILELEKLAEKNIileEKIQVLQ 1311
Cdd:pfam13868 134 ----------EFNEEQAEWKELEKE------EEREEDER-ILEYLKEKAEREEEREAEREEIEEEKEREI---ARLRAQQ 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1312 QQNEDLKARIDQntVVTRQLSEENANLQEYVEKETQEKKR-----LSRTNEE 1358
Cdd:pfam13868 194 EKAQDEKAERDE--LRAKLYQEEQERKERQKEREEAEKKArqrqeLQQAREE 243
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
802-1023 |
8.40e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 802 SSASAIHPPGPITTATSLYSSDPSGVHALSG---TWFNYSGSLGDLSADLKKASSSNAAKSNLPKSGLRPPGySRLPAAK 878
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVpppERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-ARPTVGS 2694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 879 LAAFG--------------FVRSSSVSSVSSTQSGDSAQPEQGRPATRSTFGNEEQPVLKASLPSKDTPKGAGRVAPPAS 944
Cdd:PHA03247 2695 LTSLAdpppppptpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA 2774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 945 SSVTAPRRSLLP--APKSTSTPAGTKKDAPKDQdtnkPAVSSPKRVAASTTKLHSPGYPKQRTAAARNGFPPKPDPQARE 1022
Cdd:PHA03247 2775 PAAGPPRRLTRPavASLSESRESLPSPWDPADP----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
|
.
gi 2462536697 1023 A 1023
Cdd:PHA03247 2851 P 2851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1232-1359 |
8.68e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1232 QSQSLRDRARRFEEALRKNTEE---QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNII---LE 1304
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEeKLEELRLEvseLE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1305 EKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQ-EYVEKETQ---EKKRLSRTNEEL 1359
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQleeLESKLDELAEEL 339
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1095-1355 |
1.13e-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: 46.67 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1095 TAKCEKLQKEKEELeRRFEDEVKRL---GWQQQAELQ----EL------EERLQLQFE--------AEMARLQEEHGDQ- 1152
Cdd:pfam07111 62 SQQAELISRQLQEL-RRLEEEVRLLretSLQQKMRLEaqamELdalavaEKAGQAEAEglraalagAEMVRKNLEEGSQr 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1153 -LLSIRCQHQEQVEDLTASHDAALLEMENNHT---VAITILQDDHDHKVQELmSTHELEKKELEENFEKLRLSLQDQVdT 1228
Cdd:pfam07111 141 eLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEgleKSLNSLETKRAGEAKQL-AEAQKEAELLRKQLSKTQEELEAQV-T 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1229 LTfqsQSLRDRA--RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLE-----------MKNQQIHEQEKKI----- 1290
Cdd:pfam07111 219 LV---ESLRKYVgeQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVEllqvrvqslthMLALQEEELTRKIqpsds 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462536697 1291 LELEKLAEKNIIL---EEKIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRT 1355
Cdd:pfam07111 296 LEPEFPKKCRSLLnrwREKVFALMVQ---LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRA 360
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1096-1359 |
1.14e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 AKCEKLQKEKE----------ELERRF---EDEVKRLGWQQQAEL-----------------QELEERLQlqfeaEM-AR 1144
Cdd:pfam01576 9 AKEEELQKVKErqqkaeselkELEKKHqqlCEEKNALQEQLQAETelcaeaeemrarlaarkQELEEILH-----ELeSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1145 LQEEH--GDQLLSIRCQHQEQVEDLTAShdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSL 1222
Cdd:pfam01576 84 LEEEEerSQQLQNEKKKMQQHIQDLEEQ-----LDEEEAARQKLQLEKVTTEAKIKKL---------------EEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1223 QDQVDTLTFQSQSLRDRARRFEEALRKntEEQLEIALAPYQHLEEDMKSLKQVlemknqQIHEQEKKILELEKLAEKnii 1302
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAE--EEEKAKSLSKLKNKHEAMISDLEE------RLKKEEKGRQELEKAKRK--- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1303 LEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1244-1373 |
1.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1244 EEALRKNTEEQLEialapyQHLEEDMKSLKQV-----------LEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQ 1312
Cdd:PHA02562 108 ESASSKDFQKYFE------QMLGMNYKSFKQIvvlgtagyvpfMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQ 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1313 QNEDLKARID--------QNTVVTRQLSEENANLQEY-------VEKETQEKKRLSRTNEELL-WKLQTGDPTSPIK 1373
Cdd:PHA02562 182 QIQTLDMKIDhiqqqiktYNKNIEEQRKKNGENIARKqnkydelVEEAKTIKAEIEELTDELLnLVMDIEDPSAALN 258
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1250-1356 |
2.25e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALAPYQHLEEDMKSLKQVL-----EMKNQQIHEQEKKILEL-EKLAEKNIILEEKiQVLQQQNEDLKARIDQ 1323
Cdd:PRK11281 198 QAEQALLNAQNDLQRKSLEGNTQLQDLlqkqrDYLTARIQRLEHQLQLLqEAINSKRLTLSEK-TVQEAQSQDEAARIQA 276
|
90 100 110
....*....|....*....|....*....|...
gi 2462536697 1324 NTVVTRQLsEENANLQEYVEKETQEKKRLSRTN 1356
Cdd:PRK11281 277 NPLVAQEL-EINLQLSQRLLKATEKLNTLTQQN 308
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1234-1358 |
2.37e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1234 QSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEmknQQIHEQEKKILELEK-LAEKNIILEEKIQVLQQ 1312
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFE---KELRERRNELQKLEKrLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462536697 1313 QNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR-TNEE 1358
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEE 154
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
534-962 |
2.48e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.68 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 534 ARADSVLNIPAPLHPET--TVNMTYQPTTPSSSFQDVSVFGMDAGSPLVVPPPtdSARLLNTSPKVPDKNTCPSGIPKPV 611
Cdd:pfam05109 440 AAPNTTTGLPSSTHVPTnlTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSP--SPRDNGTESKAPDMTSPTSAVTTPT 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 612 FTHSKDTPSSQEGMENYQVEKTEERTETKPIIMPKPKHVRPkiityirrNPQALGQVDASLVPVGLPYAPPTC-TMPLPH 690
Cdd:pfam05109 518 PNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP--------TPAVTTPTPNATIPTLGKTSPTSAvTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 691 EEKAAGGDLKPSANLYEKFKPDLQKPRVFSSglmvsgikPPGHPFSQMSEkflqevtdhpGKEEFCSPPYAHYEVPPTFY 770
Cdd:pfam05109 590 ATSPTVGETSPQANTTNHTLGGTSSTPVVTS--------PPKNATSAVTT----------GQHNITSSSTSSMSLRPSSI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 771 RSAmlLKPQLGLGAMSRLPsaksrILIASQRSSASAIHPPGPITTATSLYSSdpSGVHALSGTWFNYSGSlGDlSADLKK 850
Cdd:pfam05109 652 SET--LSPSTSDNSTSHMP-----LLTSAHPTGGENITQVTPASTSTHHVST--SSPAPRPGTTSQASGP-GN-SSTSTK 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 851 ASSSNAAKSNLPKSGLRPpgysRLPAAKLAAFGFVrSSSVSSVSSTQSGDSAQPEQGRPATRST--FGNEEQpvlkaslp 928
Cdd:pfam05109 721 PGEVNVTKGTPPKNATSP----QAPSGQKTAVPTV-TSTGGKANSTTGGKHTTGHGARTSTEPTtdYGGDST-------- 787
|
410 420 430
....*....|....*....|....*....|....
gi 2462536697 929 SKDTPKGAGRVAPPASSSVTAPRRSLLPAPKSTS 962
Cdd:pfam05109 788 TPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTA 821
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1216-1360 |
2.54e-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: 45.82 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1216 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALA------PYQHLEEDMKSLKQVLEMKNQQIHEQEKK 1289
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1290 ILEL-EKLAEkniiLEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEELL 1360
Cdd:TIGR02168 332 LDELaEELAE----LEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVAQLELQIAS 397
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1216-1359 |
2.55e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1216 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapyQHLEEDMKSLKQVLEMKNQQIH------EQEKK 1289
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------KRLELEIEEVEARIKKYEEQLGnvrnnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1290 ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQeyvEKETQEKKRLSRTNEEL 1359
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAE---LEAELAELEAELE---EKKAELDEELAELEAEL 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1076-1340 |
2.63e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1076 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG--WQQQAELQELEERLQLQFE--AEMARLQEEHGD 1151
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEAEIEDLREtiAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1152 QLLSircqHQEQVEDLtashdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDqvdtLTF 1231
Cdd:PRK02224 280 EVRD----LRERLEEL---------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----HNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1232 QSQSLRDRARRFEEALRKNTEEQLEialapyqhLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNII----LEEKI 1307
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnAEDFL 414
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462536697 1308 QVLQQQNEDLKARIDQNTVVTRQLS---EENANLQE 1340
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARervEEAEALLE 450
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1267-1364 |
3.07e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1267 EDMKSLK-QVLEMKNQQIH--------EQEKKIL--ELEKLAEKNIILEEKiqvLQQQNED------LKARIDQNTVVTR 1329
Cdd:pfam13851 26 ELIKSLKeEIAELKKKEERneklmseiQQENKRLtePLQKAQEEVEELRKQ---LENYEKDkqslknLKARLKVLEKELK 102
|
90 100 110
....*....|....*....|....*....|....*
gi 2462536697 1330 QLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1364
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQ 137
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1122-1359 |
3.14e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1122 QQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTAshdaallemennhtvAITILQDDHDHKVQELm 1201
Cdd:COG4942 24 EAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLA-ALERRIAALAR---------------RIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1202 sthelekkeleenfeklrLSLQDQVDTLTFQSQSLRDR-ARRFEEALRKNTEEQLEIALAP--YQHLEEDMKSLKQVLEM 1278
Cdd:COG4942 86 ------------------AELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1279 KNQQIHEQEKKILELEKLAEKNIILEEKIQVL----QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1354
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
....*
gi 2462536697 1355 TNEEL 1359
Cdd:COG4942 228 LIARL 232
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1275-1365 |
3.25e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1275 VLEMKNQQIHEQEKKILELEKlaeKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1354
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90
....*....|.
gi 2462536697 1355 TNEELLWKLQT 1365
Cdd:TIGR04523 282 KIKELEKQLNQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1340 |
4.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1056 FDALAVATQHF--FRKNESALVKEKElSIE-LANIRdevafhtAKCEKLQKEKEELERrFEDEVKRLG-WQQQAELQELE 1131
Cdd:COG4913 224 FEAADALVEHFddLERAHEALEDARE-QIElLEPIR-------ELAERYAAARERLAE-LEYLRAALRlWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1132 ERLQlQFEAEMARLQEehgdqllsircqhqeQVEDLTASHDAA---LLEMENnhtvaiTILQDDHDhkvqelmsthelek 1208
Cdd:COG4913 295 AELE-ELRAELARLEA---------------ELERLEARLDALreeLDELEA------QIRGNGGD-------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1209 keleenfeklRL-SLQDQVDTLTFQSQSLRDRARRFEEALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQ 1281
Cdd:COG4913 339 ----------RLeQLEREIERLERELEERERRRARLEALLAAlglplpASAEEFAALRAEAAALLEALEEELEALE---E 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1282 QIHEQEKKILELEKLAEKniiLEEKIQVLQQQnedlKARIDQNTVVTRQLSEENANLQE 1340
Cdd:COG4913 406 ALAEAEAALRDLRRELRE---LEAEIASLERR----KSNIPARLLALRDALAEALGLDE 457
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1101-1359 |
6.07e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1101 LQKEKEELERR-FEDEvkrlgwQQQAELQEleERLQLQfeAEMARLQE-----EHGDQLLSIRC----QHQEQVEDLTAS 1170
Cdd:pfam05622 5 AQEEKDELAQRcHELD------QQVSLLQE--EKNSLQ--QENKKLQErldqlESGDDSGTPGGkkylLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1171 hdaaLLEMENNhtvaitilQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRArrfeEAL 1247
Cdd:pfam05622 75 ----NFRLETA--------RDDYRIKCEEL---------------EKEVLELQHRNEELTSlaeEAQALKDEM----DIL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1248 RKNTEE--QLEIALAPYQHLEEDMKSLK-QV--LEMKNQqIHEQEKkiLELEKLAEKNIILEEKIQVLQQQNEDLKARID 1322
Cdd:pfam05622 124 RESSDKvkKLEATVETYKKKLEDLGDLRrQVklLEERNA-EYMQRT--LQLEEELKKANALRGQLETYKRQVQELHGKLS 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462536697 1323 QNTVVTRQLSEENANLQEYVEKETQEKKRLS-------RTNEEL 1359
Cdd:pfam05622 201 EESKKADKLEFEYKKLEEKLEALQKEKERLIierdtlrETNEEL 244
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
1293-1364 |
6.73e-04 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 39.56 E-value: 6.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1293 LEKLAEKNIILEEKIQVLQQQNEDLKARidqntvvTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1364
Cdd:pfam06005 6 LEQLETKIQAAVDTIALLQMENEELKEE-------NEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1100-1343 |
6.97e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1100 KLQKEKEELERRF----------EDEVKRLGW---QQQAELQELEERLQ-------------LQFEAEMARLQEEHGD-- 1151
Cdd:pfam01576 149 KLSKERKLLEERIseftsnlaeeEEKAKSLSKlknKHEAMISDLEERLKkeekgrqelekakRKLEGESTDLQEQIAElq 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1152 -QLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQ-DDHDHKVQELMSTHELEKKELEEN-------FEKLRLSL 1222
Cdd:pfam01576 229 aQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQrrdlgeeLEALKTEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1223 QDQVDTLTFQsQSLRDRARRFEEALRKNTEEQLEIALAPYQHLE--------------EDMKSLKQVLEmKNQQIHEQEK 1288
Cdd:pfam01576 309 EDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMRqkhtqaleelteqlEQAKRNKANLE-KAKQALESEN 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1289 KIL--ELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE 1343
Cdd:pfam01576 387 AELqaELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1019-1339 |
7.44e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLvlrlKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALV----KEKELSIELANIRDEVAFH 1094
Cdd:pfam15921 332 ELREAKRMY----EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1095 TAKCEKLQKEKEELERRfEDEVKRLgwqqQAELQELEERLQLQFEAEMARLQEEHgdqllsircQHQEQVEDLTAshdaa 1174
Cdd:pfam15921 408 TGNSITIDHLRRELDDR-NMEVQRL----EALLKAMKSECQGQMERQMAAIQGKN---------ESLEKVSSLTA----- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1175 llEMENNHTVAitilqddhdHKVQELMSTHELEKKELEENFEKLRLSLQDQ---VDTLTFQSQSLRDRARRFEEALR--K 1249
Cdd:pfam15921 469 --QLESTKEML---------RKVVEELTAKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLRSRVDLKLQELQhlK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQI---------HEQEKKILELEKLAekniiLEEKIQVLQQQNEDLKAR 1320
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIenmtqlvgqHGRTAGAMQVEKAQ-----LEKEINDRRLELQEFKIL 612
|
330
....*....|....*....
gi 2462536697 1321 IDQNTVVTRQLSEENANLQ 1339
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLE 631
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1239-1359 |
7.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1239 RARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDL 1317
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEeELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462536697 1318 KARIDQNTVVTRQL---SEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:COG4372 90 QAAQAELAQAQEELeslQEEAEELQEELEELQKERQDLEQQRKQL 134
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1097-1352 |
7.92e-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: 44.04 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1097 KCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQF-------EAEMARLQEEHGdqllsiRCQhqEQVEDLTA 1169
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIndrirllEQEVARYKEESG------KAQ--AEVERLLG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1170 shdaALLEMENNhtvaitilQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALRK 1249
Cdd:pfam10174 587 ----ILREVENE--------KNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK---GAQLLEEARRREDNLADN 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEklAEKNIILEEkiqVLQQQNEDLKARI---DQNTV 1326
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR--AERRKQLEE---ILEMKQEALLAAIsekDANIA 726
|
250 260
....*....|....*....|....*.
gi 2462536697 1327 VTRQLSEENANLQEYVEKETQEKKRL 1352
Cdd:pfam10174 727 LLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1241-1365 |
8.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1241 RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL----ELEKLAEKNIILEEKIQVLQQQNED 1316
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEqarsELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462536697 1317 LKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1365
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1216-1360 |
8.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1216 EKLRLSLQDQVDTLTFQSQSLRDRARRFE------EALRKNTEEQLEIALAP--YQHLEEDMKSLKQvlemknqQIHEQE 1287
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLEleieevEARIKKYEEQLGNVRNNkeYEALQKEIESLKR-------RISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462536697 1288 KKILEL-EKLAEKNIILEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRT-NEELL 1360
Cdd:COG1579 110 DEILELmERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEELEAEREELAAKiPPELL 177
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1069-1319 |
9.48e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1069 KNESALVKEKE-LSIELANIRDEVAFHTAKCEKLQKEKEELERRFED---EVKRLGWQQQAELQ---------------- 1128
Cdd:TIGR02169 230 KEKEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGEEEQLRVKekigeleaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1129 --ELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQddhdhKVQELMSTHEL 1206
Cdd:TIGR02169 310 iaEKERELE-DAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRA-----ELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1207 EKKELEENFEKL------RLSLQDQVDTLTFQSQSLRDRARRFEEAL-----RKN------TEEQLEIALAPYQ--HLEE 1267
Cdd:TIGR02169 383 TRDELKDYREKLeklkreINELKRELDRLQEELQRLSEELADLNAAIagieaKINeleeekEDKALEIKKQEWKleQLAA 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462536697 1268 DMKSLKQVLEMKNQQIHEQEKkilELEKLAEKNIILEEKIQVLQQQNEDLKA 1319
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
865-1101 |
9.59e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.52 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 865 GLRPPGYSRLPAAKLAAFGFVRSSSVSSVSSTQSGDSAQPEQGRPATRSTfgnEEQPvlKASLPSKDTPKGAGRVAPPAS 944
Cdd:PRK14959 377 GASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAP--SPRVPWDDAPPAPPRSGIPPR 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 945 SSVTAPRRSLLP-APKSTSTPAGTkkdapkdqdtnkpavsSPKRVAASTTKLHSPGYPKQ-----RTAAARNGFPPKPDP 1018
Cdd:PRK14959 452 PAPRMPEASPVPgAPDSVASASDA----------------PPTLGDPSDTAEHTPSGPRTwdgflEFCQGRNGQGGRLAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQL---VLRLKERCEQQTRQLGVAQGE-----LKRAICGFDA-LAVATQHFFRKNESALVKEKELSIELANIRD 1089
Cdd:PRK14959 516 VLRQATPEHadgRLRLATMSSVQYERLTDAATEttlagLVRDYFGDACrVEVLPPTRVRRTEAELRKEAEAHPAVQLLKE 595
|
250
....*....|..
gi 2462536697 1090 EVAFHTAKCEKL 1101
Cdd:PRK14959 596 EMGACILKCTPL 607
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1078-1154 |
1.02e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 39.47 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1078 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQfEAEMARLQEEHgDQLL 1154
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDLEEELKEKNKANEI--------LNDELIALQIENNLL-EEKLRKLQEEN-DELV 73
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1019-1285 |
1.04e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLVLRLKERCEQQTR----QLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 1094
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLYEKEIEdlrrQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1095 T-------AKCEKLQKEKEELERRFEDEVKrlgwqqqaELQELEERLQLQFEAEMARLQEEhgDQLLS-IRCQHQEQVED 1166
Cdd:pfam00038 116 TlarvdleAKIESLKEELAFLKKNHEEEVR--------ELQAQVSDTQVNVEMDAARKLDL--TSALAeIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1167 LTAshdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKeleenfeklrlsLQDQVDTLTFQSQSLRDRARRFEEA 1246
Cdd:pfam00038 186 NRE-------EAEEWYQSKLEELQQAAARNGDALRSAKEEITE------------LRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462536697 1247 LRKnTEEQLEIALAPYQ----HLEEDMKSLKQVLEMKNQQIHE 1285
Cdd:pfam00038 247 LAE-TEERYELQLADYQelisELEAELQETRQEMARQLREYQE 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1023-1341 |
1.09e-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: 43.50 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1023 AERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQ 1102
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1103 KEKEELERRFEDEVKRlgwqQQAELQELEERLqlqfeaemarlqeehgDQLLSIRCQHQEQVEDltaSHDAALLEMENNH 1182
Cdd:TIGR00606 923 QEKEELISSKETSNKK----AQDKVNDIKEKV----------------KNIHGYMKDIENKIQD---GKDDYLKQKETEL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1183 TVAITILQDDHDHKvqelmsthelekkeleENFEK-LRLSLQDqvdtltFQSQSLRDRARRFEEALRKNTEEQLEIALAP 1261
Cdd:TIGR00606 980 NTVNAQLEECEKHQ----------------EKINEdMRLMRQD------IDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1262 YQHLEE-------DMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKiQVLQQQNEDLKARIDQNTVVTRQLSEE 1334
Cdd:TIGR00606 1038 KQHLKEmgqmqvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK-ELREPQFRDAEEKYREMMIVMRTTELV 1116
|
....*..
gi 2462536697 1335 NANLQEY 1341
Cdd:TIGR00606 1117 NKDLDIY 1123
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1166-1338 |
1.14e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1166 DLTASHDAALLEMENNHTvAITilqddhdHKVQELMSTHELEKKELEENFEKLRLSLQDqvdtLTFQSQSLRD---RARR 1242
Cdd:pfam13851 1 ELMKNHEKAFNEIKNYYN-DIT-------RNNLELIKSLKEEIAELKKKEERNEKLMSE----IQQENKRLTEplqKAQE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1243 FEEALRKNTEEQ------LEIALAPYQHLEEDMKSLK---QVLEMKNQQIHE--------QEKKILEL-EKLAEKNIILE 1304
Cdd:pfam13851 69 EVEELRKQLENYekdkqsLKNLKARLKVLEKELKDLKwehEVLEQRFEKVERerdelydkFEAAIQDVqQKTGLKNLLLE 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462536697 1305 EKIQVLQqqnEDLKARidqntvvTRQLSE--ENANL 1338
Cdd:pfam13851 149 KKLQALG---ETLEKK-------EAQLNEvlAAANL 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1071-1367 |
1.31e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1071 ESALVKEKELSIELANIRDEVAFHTAK-CEKLQKEKEELERRFEDEVKRLGW------QQQAELQEL-----EERLQLQF 1138
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEdHEKIQHLEEEYKKEINDKEKQVSLlliqitEKENKMKDLtflleESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1139 EAEMARLQEEHGDQLLSIRCQHQEQVEDL------TASHDAALLEMENNHTVAITILQDDHDHKVQEL---MSTHE---L 1206
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnkaKAAHSfvvT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1207 EKKELEENFEKL----RLSLQDQVDTLTFQSQSLRDRARRFEE--ALRKNTE---EQLEIALAP----------YQHLEE 1267
Cdd:pfam05483 353 EFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEvelEELKKILAEdeklldekkqFEKIAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1268 DMKSLKQ----VLEMKNQQIHEQEKKIL------------------ELEKLAEKNI---------ILEEKIQVLQQQNED 1316
Cdd:pfam05483 433 ELKGKEQelifLLQAREKEIHDLEIQLTaiktseehylkevedlktELEKEKLKNIeltahcdklLLENKELTQEASDMT 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462536697 1317 LKARIDQNTVVTRQLSEEN--ANLQEYVEKETQEKKRLSRTNEELlwkLQTGD 1367
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRDELESVREEF---IQKGD 562
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1258 |
1.42e-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: 43.12 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLVLRLKERCEQQtrqLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1098
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1099 EKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSIRCQHQEQVEDLTASHDAALLEM 1178
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1179 E-NNHTVAITILQDDHDHKVQELMSTHELEKKEleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFE---EALRKNTEEQ 1254
Cdd:TIGR02168 441 ElEELEEELEELQEELERLEEALEELREELEEA-----EQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQ 515
|
....
gi 2462536697 1255 LEIA 1258
Cdd:TIGR02168 516 SGLS 519
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1221-1320 |
1.57e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1221 SLQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKn 1300
Cdd:pfam04012 54 QLERRLEQQTEQAKKLEEKAQ---AALTKGNEELAREALAEKKSLEKQAEALETQLA-------QQRSAVEQLRKQLAA- 122
|
90 100
....*....|....*....|
gi 2462536697 1301 iiLEEKIQVLQQQNEDLKAR 1320
Cdd:pfam04012 123 --LETKIQQLKAKKNLLKAR 140
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
1250-1367 |
1.69e-03 |
|
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.
Pssm-ID: 464594 Cd Length: 857 Bit Score: 42.86 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1250 NTEEQLEIALApYQHLEEDMKSLKQVLEMKNQQIHEQEKKI---------LELEKLAEKNIILEEKIQVLQQQNEDLKAR 1320
Cdd:pfam15254 378 NTNIQAEIALA-LQPLRSENAQLRRQLRILNQQLREQEKTEktsgsgdcnLELFSLQSLNMSLQNQLQESLKSQELLQSK 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462536697 1321 idqntvvtrqlseeNANLQEYVEKETQEKKRLSRT----NEELLWKLQTGD 1367
Cdd:pfam15254 457 --------------NEELLKVIENQKEENKKLTKIfkekEQTLLENKQQFD 493
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1279-1356 |
1.70e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 39.09 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1279 KNQQIHEQEKKILELEK----LAEKNIILEEKIQVLQQQNEDLKARID----QNTVVT---RQLSEENANL-QEYVEKET 1346
Cdd:cd22887 2 LESELQELEKRLAELEAelasLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEeklRKLQEENDELvERWMAKKQ 81
|
90
....*....|
gi 2462536697 1347 QEKKRLSRTN 1356
Cdd:cd22887 82 QEADKMNEAN 91
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1019-1364 |
1.70e-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: 43.03 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1019 QAREAERQLVLRLKERCEQQTRQ--LGVAQGELKRAICGFDALAVATQHF-FRKNESALVKEKELSIELANIRDEVafHT 1095
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERInRARKAAPLAAHIKAVTQIEQQAQRI--HT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 akceKLQKEKEELERRFEDEVKRLgwQQQAELQELEERLQLQF--------EAEMARLQEEHGDQLLSIRCQHQEQVEDL 1167
Cdd:TIGR00618 315 ----ELQSKMRSRAKLLMKRAAHV--KQQSSIEEQRRLLQTLHsqeihirdAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1168 TASHD-----AALLEMENN--HTVAiTILQDDHDHKvQELMSTHELEKKeleenfEKLRLSLQDQVDTLTFQSQSLRDRA 1240
Cdd:TIGR00618 389 TTLTQklqslCKELDILQReqATID-TRTSAFRDLQ-GQLAHAKKQQEL------QQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1241 RRfEEALRKNTEEQLEIALAPYQHLEEDMKSL--KQVLEMKNQQ-----------------------------------I 1283
Cdd:TIGR00618 461 LQ-ESAQSLKEREQQLQTKEQIHLQETRKKAVvlARLLELQEEPcplcgscihpnparqdidnpgpltrrmqrgeqtyaQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1284 HEQEKKILELEKLAEKN--IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLW 1361
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
...
gi 2462536697 1362 KLQ 1364
Cdd:TIGR00618 620 KLQ 622
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1020-1364 |
1.94e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1020 AREAER----QLVLRLKERCEQQTRQLGVAQGELKRAICGFDAlavATQHFFRKNESALVKEKELsieLANIRDEVAfht 1095
Cdd:pfam05557 44 DRESDRnqelQKRIRLLEKREAEAEEALREQAELNRLKKKYLE---ALNKKLNEKESQLADAREV---ISCLKNELS--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1096 AKCEKLQKEKEELERrfedevkrlgwqQQAELQELEERLQLQfeaeMARLQEehgdqllsircqHQEQVEDLTASHDAAL 1175
Cdd:pfam05557 115 ELRRQIQRAELELQS------------TNSELEELQERLDLL----KAKASE------------AEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1176 lemennhtvaitilqdDHDHKVQELMsthelekkeleenfEKLRLSLQDQVDTLTFQS--------QSLRDRARRFEEAL 1247
Cdd:pfam05557 167 ----------------EAEQRIKELE--------------FEIQSQEQDSEIVKNSKSelaripelEKELERLREHNKHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1248 RKNTE--EQLEIALAPYQ---HLEEDMKSLKQVLEMKNQQIheqEKKILELEKLAE-------KNIILEEKIQVLQQQNE 1315
Cdd:pfam05557 217 NENIEnkLLLKEEVEDLKrklEREEKYREEAATLELEKEKL---EQELQSWVKLAQdtglnlrSPEDLSRRIEQLQQREI 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462536697 1316 DLKAridQNTVVTRQLSEENANLQE-------YVEKETQEKKRLSRTnEELLWKLQ 1364
Cdd:pfam05557 294 VLKE---ENSSLTSSARQLEKARREleqelaqYLKKIEDLNKKLKRH-KALVRRLQ 345
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1222-1320 |
1.97e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1222 LQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQvlemknqQIHEQEKKILELEKLAEKni 1301
Cdd:COG1842 56 LERQLEELEAEAEKWEEKAR---LALEKGREDLAREALERKAELEAQAEALEA-------QLAQLEEQVEKLKEALRQ-- 123
|
90
....*....|....*....
gi 2462536697 1302 iLEEKIQVLQQQNEDLKAR 1320
Cdd:COG1842 124 -LESKLEELKAKKDTLKAR 141
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1265-1360 |
2.08e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1265 LEEDMKSLKQVLEMKNQQIHEQEKKI----LELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQE 1340
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEkallKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100
....*....|....*....|
gi 2462536697 1341 YVEKETQEKKRLSRTNEELL 1360
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAL 124
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1077-1181 |
2.20e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1077 EKELSIELANIRDEVAfhTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQFEAEMARLQEEHgDQLLSI 1156
Cdd:cd16269 195 EKEKEIEAERAKAEAA--EQERKLLEEQQRELEQKLED--------QERSYEEHLRQLKEKMEEERENLLKEQ-ERALES 263
|
90 100
....*....|....*....|....*
gi 2462536697 1157 RCQHQEQVEDLTASHDAALLEMENN 1181
Cdd:cd16269 264 KLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1068-1372 |
2.41e-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: 42.65 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1068 RKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQE 1147
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1148 EHGD--QLLSIRCQHQEQVEDLTASHD------AALLEMENNHTVAITILqddhDHKVQELMSTHELekkeleenfeklr 1219
Cdd:TIGR00618 319 KMRSraKLLMKRAAHVKQQSSIEEQRRllqtlhSQEIHIRDAHEVATSIR----EISCQQHTLTQHI------------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1220 LSLQDQVDTLTFQSQSL--------RDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKil 1291
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLckeldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI-- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1292 ELEKLAEKniiLEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSP 1371
Cdd:TIGR00618 460 HLQESAQS---LKEREQQLQTKEQIHLQ-------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
.
gi 2462536697 1372 I 1372
Cdd:TIGR00618 530 M 530
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1015-1353 |
3.00e-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: 42.34 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1015 KPDPQAREAERQL---VLRLKERCEQQTRQLGVAQGELKRA-ICGFDALAVatQHFFRKNESALVKEKELSIELANIRDE 1090
Cdd:TIGR00606 744 KEIPELRNKLQKVnrdIQRLKNDIEEQETLLGTIMPEEESAkVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1091 VAFhtakcEKLQKEKEELERRFE------DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlLSIRCQHQEQV 1164
Cdd:TIGR00606 822 RTV-----QQVNQEKQEKQHELDtvvskiELNRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTN-----LQRRQQFEEQL 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1165 EDLTA---SHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELeenfEKLRLsLQDQVDTLTFQSQSLRDRAR 1241
Cdd:TIGR00606 891 VELSTevqSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ----DKVND-IKEKVKNIHGYMKDIENKIQ 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1242 RFEEALRKNTEEQLEIALAPY-------QHLEEDMKSLKQVLEMKNQQ---------IHEQEKKILELEKLAEKNIILEE 1305
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQerwlqdnltLRKRENELKEVEEELKQHLKEMG 1045
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462536697 1306 KIQVLQQQNEDLKARIDQNTvVTRQLSEENANLQEYVEKETQEKKRLS 1353
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENIDL-IKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1078-1349 |
3.43e-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: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1078 KELSIELANIRDEVAFHTakcEKLQKEKEELERRFEDEVKRLGWQQqaELQELEERLQLQFEAEMARLQEEHGDQLLSir 1157
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILT---QCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQDLQDVR-- 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1158 cQHQEQVEDLTASHDAALlemennHTVAITILQDDHDHKvqeLMSTHELEKKELEENFEKLRlSLQDQVDTLTF------ 1231
Cdd:TIGR00618 632 -LHLQQCSQELALKLTAL------HALQLTLTQERVREH---ALSIRVLPKELLASRQLALQ-KMQSEKEQLTYwkemla 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1232 QSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVL-EMKNQQIHEQEKKILELEKLAEKNIILEEKIQVL 1310
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462536697 1311 QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK 1349
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
1291-1343 |
3.55e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 37.64 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462536697 1291 LELEKLAEKNIILEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQEYVE 1343
Cdd:COG3074 25 MEVEELKEKNEELEQENEELQSENEELQSEN-------EQLKTENAEWQERIR 70
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1015-1359 |
3.58e-03 |
|
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: 41.88 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1015 KPDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELS-IELANIRDEVAF 1093
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSlKEKELAEEREKT 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1094 HTAKCEKLQK------EKEELERRFEDEVkrlgwqqQAELQELEERLQLQFEAEmarLQEEhgdqllsircQHQEQVEDL 1167
Cdd:pfam02463 784 EKLKVEEEKEeklkaqEEELRALEEELKE-------EAELLEEEQLLIEQEEKI---KEEE----------LEELALELK 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1168 TASHDAALLEMENNHTVAITILQDDHDHKVQELmsthelekkeLEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEAL 1247
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKE----------EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1248 RKNTEEQLEIAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVV 1327
Cdd:pfam02463 914 EKENEIEERIK----EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
330 340 350
....*....|....*....|....*....|..
gi 2462536697 1328 TRQLSEENANLQEyvEKETQEKKRLSRTNEEL 1359
Cdd:pfam02463 990 YNKDELEKERLEE--EKKKLIRAIIEETCQRL 1019
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1263-1351 |
3.86e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1263 QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN----IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1338
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAeeeaERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEA 88
|
90
....*....|...
gi 2462536697 1339 QEYVEKETQEKKR 1351
Cdd:pfam20492 89 QEEIARLEEEVER 101
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1157-1313 |
3.99e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1157 RCQHQEQVEDLTASHdaallemennhtvaITILQDDHDH--KVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQ 1234
Cdd:smart00787 138 RMKLLEGLKEGLDEN--------------LEGLKEDYKLlmKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1235 SLRDRARrfeEALRKnTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN--------IILEEK 1306
Cdd:smart00787 204 TELDRAK---EKLKK-LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKEQ 279
|
....*..
gi 2462536697 1307 IQVLQQQ 1313
Cdd:smart00787 280 LKLLQSL 286
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1084-1355 |
4.65e-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: 40.40 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1084 LANIRDEVAFHTAKCEKLQKEKEELERRFEDEvkrlgwqqQAELQELEERLQLQfEAEMARLQEehgdqLLSIRCQHQEQ 1163
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKA--------EAEVAALNRRIQLL-EEELERTEE-----RLAEALEKLEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1164 VEDLTASHDAALLEMENnhtvaiTILQDDhdhkvqelmsthelekkeleenfEKLRLsLQDQVDTLTFQSQslrDRARRF 1243
Cdd:pfam00261 69 AEKAADESERGRKVLEN------RALKDE-----------------------EKMEI-LEAQLKEAKEIAE---EADRKY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1244 EEALRK---------NTEEQLEIALAPYQHLEEDMKSLKQVLemknQQIHEQEkkilelEKLAEKNIILEEKIQVLQQQN 1314
Cdd:pfam00261 116 EEVARKlvvvegdleRAEERAELAESKIVELEEELKVVGNNL----KSLEASE------EKASEREDKYEEQIRFLTEKL 185
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462536697 1315 EDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRT 1355
Cdd:pfam00261 186 KEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEE 226
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1064-1347 |
4.74e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1064 QHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRL-------------GWQQ-QAELQE 1129
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrdelngelsaadaAVAKdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1130 LEERLqLQFEAEMARLQEEHGDQLLSIRCQHQEQVE----------DLTASHDA--ALLEMENNHTVAitilqdDHDHKV 1197
Cdd:pfam12128 327 LEDQH-GAFLDADIETAAADQEQLPSWQSELENLEErlkaltgkhqDVTAKYNRrrSKIKEQNNRDIA------GIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1198 QELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALrknteEQLEIALAPYQHLEEDMKSLKQVLE 1277
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEA---GKLEFNEEEYRLKSRL-----GELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1278 MKNQQIHEQEKKILELEKLAEKNIILE-------EKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQEYVEKETQ 1347
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHFLRKEAP 545
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1121-1323 |
4.84e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.12 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1121 WQQ-QAELQELEERLQlqfEAEMARLQEEHGDqllsircqHQEQVEDLTASHDAALLEMENNHTVAitilqDDHDHKVQE 1199
Cdd:cd00176 2 LQQfLRDADELEAWLS---EKEELLSSTDYGD--------DLESVEALLKKHEALEAELAAHEERV-----EALNELGEQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1200 LMSTHELEKKELEENFEKLRL---SLQDQVDTLTFQSQSLRDRARRFEEA--LRKNTEEQLEIALA-PYQHLEEDMKSLK 1273
Cdd:cd00176 66 LIEEGHPDAEEIQERLEELNQrweELRELAEERRQRLEEALDLQQFFRDAddLEQWLEEKEAALASeDLGKDLESVEELL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1274 QVLEMKNQQIHEQEKKILELEKLAEK---------NIILEEKIQVLQQQNEDLKARIDQ 1323
Cdd:cd00176 146 KKHKELEEELEAHEPRLKSLNELAEElleeghpdaDEEIEEKLEELNERWEELLELAEE 204
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
1099-1149 |
4.89e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 38.81 E-value: 4.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462536697 1099 EKLQKEKEELERRFEDEVKRLG---WQQQAELQELEERLQLqfeAEMARLQEEH 1149
Cdd:pfam04696 44 EKAKQEKEELEERKREEREELFeerRAEQIELRALEEKLEL---KELMETWHEN 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1066-1359 |
4.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1066 FFRKNESALVK-EKELSI---ELANIRDEVAfhtaKCEKLQKEKEELERRFEdEVKRlgwqqqaELQELEERLQL----- 1136
Cdd:PRK03918 301 FYEEYLDELREiEKRLSRleeEINGIEERIK----ELEEKEERLEELKKKLK-ELEK-------RLEELEERHELyeeak 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1137 QFEAEMARLQEEHGD--------QLLSIRCQHQEQVEDLT-------------ASHDAALLEMENNHTVAITILQDDHDH 1195
Cdd:PRK03918 369 AKKEELERLKKRLTGltpeklekELEELEKAKEEIEEEISkitarigelkkeiKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1196 KVQELMsthelekkeleenfEKLRLSLQD---QVDTLTFQSQSLRDRARRFEEALRKNTEeqleiaLAPYQHLEEDMKSL 1272
Cdd:PRK03918 449 HRKELL--------------EEYTAELKRiekELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1273 KQVLEMKNqqIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyVEKETQEK--- 1349
Cdd:PRK03918 509 EEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE-LLKELEELgfe 585
|
330
....*....|..
gi 2462536697 1350 --KRLSRTNEEL 1359
Cdd:PRK03918 586 svEELEERLKEL 597
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1090-1146 |
4.99e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.20 E-value: 4.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462536697 1090 EVAFHtAKCEKLQKEKEELERRFEDEVK------RLGWQQQAELQELEERLQLQFEAEMARLQ 1146
Cdd:pfam15070 84 EQRLQ-EEAEQLQKELEALAGQLQAQVQdneqlsRLNQEQEQRLLELERAAERWGEQAEDRKQ 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1236-1359 |
5.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1236 LRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQ---- 1311
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllq 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462536697 1312 -----QQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1359
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1030-1147 |
5.45e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1030 RLKERCEQQTRQLGvaqgELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDevafhtaKCEKLQKEKEELE 1109
Cdd:pfam13851 58 RLTEPLQKAQEEVE----ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQ-------RFEKVERERDELY 126
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462536697 1110 RRFEDEVKRLgwQQQAELQE--LEERLQL---QFEAEMARLQE 1147
Cdd:pfam13851 127 DKFEAAIQDV--QQKTGLKNllLEKKLQAlgeTLEKKEAQLNE 167
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1099-1312 |
6.22e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1099 EKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSIRCQHQEQVEDLTASHDAALlem 1178
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1179 ennhtvaitilqddhdhkvqelmsthelekkeleeNFEKLRLSLQDQVDTLTFqsQSLRDRARRFEEALRKNTEEQLEIA 1258
Cdd:pfam13868 246 -----------------------------------ELKERRLAEEAEREEEEF--ERMLRKQAEDEEIEQEEAEKRRMKR 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1259 LAPYQHLEedmkslKQVLEMKNQQIHEQEKKILELEKLAE-----KNIILEEKIQVLQQ 1312
Cdd:pfam13868 289 LEHRRELE------KQIEEREEQRAAEREEELEEGERLREeeaerRERIEEERQKKLKE 341
|
|
| FAM76 |
pfam16046 |
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ... |
1265-1338 |
8.13e-03 |
|
FAM76 protein; This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 233 and 341 amino acids in length.
Pssm-ID: 464993 [Multi-domain] Cd Length: 303 Bit Score: 40.16 E-value: 8.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462536697 1265 LEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDlkaRIDQNTVVTRQLSEENANL 1338
Cdd:pfam16046 227 LKEQIASLQKQLAQKDQQLLEKDKQITELKaKHFTKERELRNKMKTMEKEHED---KVEQLQIKIRSLLKEVATL 298
|
|
| DivIC |
pfam04977 |
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ... |
1290-1357 |
8.61e-03 |
|
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.
Pssm-ID: 428231 [Multi-domain] Cd Length: 69 Bit Score: 36.43 E-value: 8.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462536697 1290 ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTvvtrqlseenaNLQEYVEKETQEKKRLSRTNE 1357
Cdd:pfam04977 5 LLTYYQLKQEIAQLQAEIAKLKQENEELEAEIKDLK-----------SDPDYIEERARSELGMVKPGE 61
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1237-1362 |
8.63e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1237 RDRARRFEEALRK--NTEEQLEIalaPYQH---------LEEDMKS------------LKQVLEMKNQqIHEQEKKILEL 1293
Cdd:COG4026 72 RELAEKFFEELKGmvGHVERMKL---PLGHdveyvdvelVRKEIKNaiiraglkslqnIPEYNELREE-LLELKEKIDEI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462536697 1294 EKLAEKniiLEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQEYVEKETQEKKRLSRTNEELLWK 1362
Cdd:COG4026 148 AKEKEK---LTKENEELESELEELREEY-------KKLREENSILEEEFDNIKSEYSDLKSRFEELLKK 206
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
1266-1367 |
9.11e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 39.15 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1266 EEDMKSLKQV---LEM---------KNQQIHEQEKKILELEKLaEKNIILEEKIQvLQQQNEDLKARIDqntvVTRQLSE 1333
Cdd:pfam06391 34 EEDFPSLREYndyLEEvedivfnltNGIDVEETEKKIEQYEKE-NKDLILKNKMK-LSQEEEELEELLE----LEKREKE 107
|
90 100 110
....*....|....*....|....*....|....
gi 2462536697 1334 ENANLQEYVEKETQEKKRLSRtnEELLWKLQTGD 1367
Cdd:pfam06391 108 ERRKEEKQEEEEEKEKKEKAK--QELIDELMTSN 139
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1077-1366 |
9.84e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1077 EKELSIELANIRDEVAFHTAKCEKLQKEKEEL-ERRFE--DEVKRLgwqqQAELQELEERLQlQFEAEMARLQEEhgdql 1153
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELaEKRDElnAQVKEL----REEAQELREKRD-ELNEKVKELKEE----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1154 lsiRCQHQEQVEDLTASHDAALLEMENNHTVAITIlqddhdHKVQELMsthelekkeleenfEKLRLSLQDQVdtLTF-- 1231
Cdd:COG1340 80 ---RDELNEKLNELREELDELRKELAELNKAGGSI------DKLRKEI--------------ERLEWRQQTEV--LSPee 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462536697 1232 ------QSQSLRDRARRFEEALRKNteEQLEIALAPYQHLEEDMKSL-KQVLEMKN--QQIHEQEKKIL-ELEKLAEKNI 1301
Cdd:COG1340 135 ekelveKIKELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIhKKIKELAEeaQELHEEMIELYkEADELRKEAD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462536697 1302 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE--KETQEKKRLSRTNEELLWKLQTG 1366
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKKG 279
|
|
| |
