|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1322 |
3.08e-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: 74.71 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 989 AREAERQLV-LRLKERCEQQTRQLGVAQGELKRAicgfdaLAVATQHFFRKN-ESALVKEKELSIELANIRDEVAFHTAK 1066
Cdd:TIGR02168 195 LNELERQLKsLERQAEKAERYKELKAELRELELA------LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1067 CEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQ---EEHGDQLLSIRCQHQEQVEDLTAShDAA 1143
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELY-ALANEISRLEQQKQIL-RERLANLErqlEELEAQLEELESKLDELAEELAEL-EEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1144 LLEMENNHTVaitiLQDDHD--HKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1221
Cdd:TIGR02168 346 LEELKEELES----LEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1222 EQLEIALAPYQH-LEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDqntvVTRQL 1300
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD----SLERL 497
|
330 340
....*....|....*....|..
gi 1489865997 1301 SEENANLQEYVEKETQEKKRLS 1322
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1045-1328 |
1.32e-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: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1045 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLS 1124
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1125 IRCQHQEQVEDLTASHDAALLEMENNHTV---AITILQDDHD------HKVQELMSTHELEKKELEENFEKLRLSLQDQV 1195
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1196 DTLTFQSQSLRDrarrfEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEK 1275
Cdd:TIGR02168 852 EDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE---LREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489865997 1276 IQVLQQQNEDLKARIDQNtvvTRQLSEEN-------ANLQEYVEKETQE-KKRLSRTNEEL 1328
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNL---QERLSEEYsltleeaEALENKIEDDEEEaRRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
988-1328 |
2.19e-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: 68.93 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1067
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1068 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1147
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALD-ELRAELTLLNEEAA-NLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1148 ENnHTVAITILQDDHDHKVQELMSThelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1227
Cdd:TIGR02168 862 EE-LEELIEELESELEALLNERASL------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1228 LApyqhleedmkslKQVLEMKNQQIHEQ--EKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVT-------R 1298
Cdd:TIGR02168 929 LR------------LEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyE 996
|
330 340 350
....*....|....*....|....*....|
gi 1489865997 1299 QLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1062-1327 |
5.17e-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: 63.99 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1062 FHTAKCEKLQKEKEELERRFE--------DEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSiRCQHQEQV 1133
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVErrrkleeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE-RIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1134 EDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRlslQDQVDTLTFQSQSLRD-RARRF 1212
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEeRAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1213 EEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQ-IHEQEKKILELEKLAEKNIILEE--KIQVLQQQNEDLKA- 1288
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKa 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1489865997 1289 -------RIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 1327
Cdd:pfam17380 529 iyeeerrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1069-1329 |
2.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1069 KLQKEKEELERR---FEDEVKRlgwQQQAELQELEERLQLQFEAEMARLQEEHGdQLLSIRCQHQEQVEDLTAshdaaLL 1145
Cdd:COG1196 217 ELKEELKELEAElllLKLRELE---AELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEE-----AQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1146 EMENNHTVAITILQDDHDHKVQELmsthelekKELEENFEKlrlsLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLE 1225
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERR--------RELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1226 IAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNtvvTRQLSEENA 1305
Cdd:COG1196 356 AE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL---EEELEELEE 428
|
250 260
....*....|....*....|....
gi 1489865997 1306 NLQEYVEKETQEKKRLSRTNEELL 1329
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1048-1328 |
2.75e-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: 62.00 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1048 ELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEdEVKRLGWQQQAELQELEERLQLQfEAEMARLQEEhgdqllsirc 1127
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISAL-RKDLARLEAE---------- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1128 qhQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRD 1207
Cdd:TIGR02168 742 --VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA----------------EAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1208 RARRFEEALRkNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLK 1287
Cdd:TIGR02168 804 ALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1489865997 1288 ARIDQNTVVTR-QLSEENANLQEyVEKETQEKKR-LSRTNEEL 1328
Cdd:TIGR02168 883 ASLEEALALLRsELEELSEELRE-LESKRSELRReLEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
988-1312 |
5.25e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLVLRLKERcEQQTRQLGVAQGELKRAIcgfdalavatqhffRKNESALVKEKELSIELANIRDEVafhtakc 1067
Cdd:COG1196 219 KEELKELEAELLLLKL-RELEAELEELEAELEELE--------------AELEELEAELAELEAELEELRLEL------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1068 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1147
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA-RLEQDIARLEERRR-ELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1148 EnnhtvaitILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1227
Cdd:COG1196 354 E--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1228 LApyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1307
Cdd:COG1196 426 LE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
....*
gi 1489865997 1308 QEYVE 1312
Cdd:COG1196 504 EGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
990-1292 |
2.11e-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: 58.93 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 990 REAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKElsiELANIRDEVAFHTAKCEK 1069
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1070 LQKEKEELERRFEDEvkrlGWQQ-QAELQELEE---RLQLQFEAEMARLQEEHGD-QLLSIRCQH-QEQVEDLTASHDAA 1143
Cdd:TIGR02169 777 LEEALNDLEARLSHS----RIPEiQAELSKLEEevsRIEARLREIEQKLNRLTLEkEYLEKEIQElQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1144 LLEMENNHTVAITILQ--DDHDHKVQELMSTHELEKKELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1221
Cdd:TIGR02169 853 EKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1222 EQLEIALAPYQHLEE-----DMKSLKQVLEMKNQQIHEQE----KKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQ 1292
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIpeeelSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1045-1328 |
1.17e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1045 KEKElsIELANIRDEVAFHTAKCEKLQKEKEELERRFEdevkrlgwQQQAELQELEERLQlQFEAEMARLQEEHgDQLLS 1124
Cdd:TIGR04523 366 EEKQ--NEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIK-KLQQEKELLEKEI-ERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1125 IRCQHQEQVEDLTaSHDAALLEMENNH--------------TVAITILQDDHDHKVQELMSTHELEKKELEENFEklrls 1190
Cdd:TIGR04523 434 TIIKNNSEIKDLT-NQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1191 LQDQVDTLTFQSQSLRDRARRFE-EALRKNTEeqleialapYQHLEEDMKSLKQVLEMKN--QQIHEQEKKILEL----E 1263
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLEsEKKEKESK---------ISDLEDELNKDDFELKKENleKEIDEKNKEIEELkqtqK 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489865997 1264 KLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1041-1292 |
1.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1041 SALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFE--DEVKRLGWQQ------QAELQELEERL--------- 1103
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1104 --QLQF-----EAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMsthele 1176
Cdd:COG4913 687 laALEEqleelEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL------ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1177 kkeLEENFEKLRLSLQDQVDTltfqsqsLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM----KNQQI 1252
Cdd:COG4913 760 ---GDAVERELRENLEERIDA-------LRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALldrlEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1489865997 1253 HEQEKKILELEKLAEKNIIlEEKIQVLQQQNEDLKARIDQ 1292
Cdd:COG4913 830 PEYEERFKELLNENSIEFV-ADLLSKLRRAIREIKERIDP 868
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
986-1345 |
1.81e-07 |
|
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: 55.89 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 986 DPQAREAER--QLVLRLKERCE-QQTRQLGVAQG--ELKRAICGFDALAVATQHFFRKNESALVKEKelsIELANIRDEV 1060
Cdd:pfam15921 422 DDRNMEVQRleALLKAMKSECQgQMERQMAAIQGknESLEKVSSLTAQLESTKEMLRKVVEELTAKK---MTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1061 AFHTAKCEklqkEKEELERRFEDEVKRLGWQQQAELQEL------EERLQ-LQFEAEMARLQEEHGDQLLSIRCQHQEQV 1133
Cdd:pfam15921 499 SDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELqhlkneGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1134 EDLTASH---------DAALLEMENN----HTVAITILQDDHDHKVQEL-------------MSTHELEKKELEENFEKL 1187
Cdd:pfam15921 575 TQLVGQHgrtagamqvEKAQLEKEINdrrlELQEFKILKDKKDAKIRELearvsdlelekvkLVNAGSERLRAVKDIKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1188 RLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEE----------QLEIALAPYQHLEEDMKSL--------KQVLEMKN 1249
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmetttnklkmQLKSAQSELEQTRNTLKSMegsdghamKVAMGMQK 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1250 Q------QIHEQEKKILELEKL-----AEKNIILEEK--------------------IQVLQQQNEDLKARIDQNTVVTR 1298
Cdd:pfam15921 735 QitakrgQIDALQSKIQFLEEAmtnanKEKHFLKEEKnklsqelstvateknkmageLEVLRSQERRLKEKVANMEVALD 814
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1489865997 1299 QLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSPIKLSP 1345
Cdd:pfam15921 815 KASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKP 861
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1000-1328 |
2.98e-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: 55.11 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1000 LKERCEQQ---TRQLGVAQGELKRAICGFDAL----AVATQHFFRknesaLVKEKELSIELANIRDE------VAFHTAK 1066
Cdd:pfam05483 284 LKELIEKKdhlTKELEDIKMSLQRSMSTQKALeedlQIATKTICQ-----LTEEKEAQMEELNKAKAahsfvvTEFEATT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1067 C---EKLQKEKEELERRfEDEVKRLGWQQQAELQELEERLQLQF--EAEMARLQEEHGDQ--LLSIRCQHQEQVEDLTAS 1139
Cdd:pfam05483 359 CsleELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFKNnkEVELEELKKILAEDekLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1140 HD--AALLEMENNHT----VAITILQDDHDHKVQELMSTHELEKKELEENFEklrlsLQDQVDTLTFQSQSLRDRARRFE 1213
Cdd:pfam05483 438 EQelIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1214 EALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKI-LELEKLAEKNIILEEKIQVLQQQNEDL 1286
Cdd:pfam05483 513 LELKKhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1489865997 1287 KARIDQntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:pfam05483 593 ENKCNN---LKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
988-1328 |
3.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAE-RQLVLRLkERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEK--ELSIELANIRDEVAFHT 1064
Cdd:COG4717 84 EEKEEEyAELQEEL-EELEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1065 ---AKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQ------LQFEAEMARLQEEHGDqllsIRCQHQEQVED 1135
Cdd:COG4717 160 eleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEelqqrlAELEEELEEAQEELEE----LEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1136 LTASHDAALLEMENNHTVAITIlqddhdhkVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEA 1215
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAA--------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1216 LRKNTEEQLEIA-----LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQN----EDL 1286
Cdd:COG4717 308 QALPALEELEEEeleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1489865997 1287 KARIDQN----------TVVTRQLSEENANLQEYVEKETQE--KKRLSRTNEEL 1328
Cdd:COG4717 388 RAALEQAeeyqelkeelEELEEQLEELLGELEELLEALDEEelEEELEELEEEL 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1091-1334 |
5.52e-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: 54.30 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1091 QQQAELQELEERLQlQFEAEMARLQEE--HGDQLLSircQHQEQVEDLTASHDAALLEMEnnhtvaitILQDDHDHKVQE 1168
Cdd:TIGR02169 671 SEPAELQRLRERLE-GLKRELSSLQSElrRIENRLD---ELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1169 LmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlAPYQHL-EEDMKSLKQVLEM 1247
Cdd:TIGR02169 739 L---------------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLsHSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1248 KNQQIHEQEKKILELE----KLAEKNIILEEKIQVLQQQNEDLKARIDQN---------------------TVVTRQLSE 1302
Cdd:TIGR02169 803 LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienlngkkeeleeeleelEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|..
gi 1489865997 1303 ENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1334
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1049-1334 |
7.96e-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: 53.82 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1049 LSIELANIRDEVAFHTAKCEKLQKEKEELErrfedevKRLGWQQQA-ELQELEERLQLQfEAEMARLQEEhgdqlLSIRC 1127
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQE-------EQLKKQQLLkQLRARIEELRAQ-EAVLEETQER-----INRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1128 QHQEQVEdltasHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeLEENFEKLRLSLQDQVDTL-TFQSQSLR 1206
Cdd:TIGR00618 291 KAAPLAA-----HIKAVTQIEQQAQRIHTELQSKMRSRAKLLM---------KRAAHVKQQSSIEEQRRLLqTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1207 DRARRFEEALRKnteEQLEIALAPYQHLeedmKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDL 1286
Cdd:TIGR00618 357 IRDAHEVATSIR---EISCQQHTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489865997 1287 KARIdqntvvtrQLSEENANLQE-YVEKETQEKK-------RLSRTNEELLWKLQT 1334
Cdd:TIGR00618 430 KKQQ--------ELQQRYAELCAaAITCTAQCEKlekihlqESAQSLKEREQQLQT 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1005-1281 |
9.32e-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: 53.80 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1005 EQQTR--QLGVAQGELKRA--ICGFDAL----AVATQHFFRKNESA-----LVKEKELSIE-------------LANIRD 1058
Cdd:COG3096 407 VQQTRaiQYQQAVQALEKAraLCGLPDLtpenAEDYLAAFRAKEQQateevLELEQKLSVAdaarrqfekayelVCKIAG 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1059 EV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQFEAEmaRLQEEHGdQLLSIRCQHQEQ 1132
Cdd:COG3096 487 EVersqAWQTAR---------ELLRRYRSQQALAQRLQQlrAQLAELEQRLRQQQNAE--RLLEEFC-QRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1133 VEDLTASHDAallemennhtvaitiLQDDHDHKVQElmsthelekkeleenFEKLRLSLQDQVDTLTFQSQSLRDRA--- 1209
Cdd:COG3096 555 LEELLAELEA---------------QLEELEEQAAE---------------AVEQRSELRQQLEQLRARIKELAARApaw 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1210 RRFEEALRKnTEEQLEIALAPYQHLEEDMkslKQVLEmknqqiHEQEKKILElEKLAEKNIILEEKIQVLQQ 1281
Cdd:COG3096 605 LAAQDALER-LREQSGEALADSQEVTAAM---QQLLE------REREATVER-DELAARKQALESQIERLSQ 665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
984-1328 |
1.29e-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: 53.26 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 984 KPDPQAREAERQLVlRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 1063
Cdd:pfam01576 212 KLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1064 TAKCEKLQKEKEELERRFEDEVKRLGWQQQaelqeleerLQLQFEAEMARLQ----EE---HGDQLLSIRCQHQEQVEDL 1136
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTLDTTAAQQE---------LRSKREQEVTELKkaleEEtrsHEAQLQEMRQKHTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1137 TASHDAA------------LLEMENNHTVA-ITILQD---DHDHK-------VQELMSTHELEkkeleenfEKLRLSLQD 1193
Cdd:pfam01576 362 TEQLEQAkrnkanlekakqALESENAELQAeLRTLQQakqDSEHKrkklegqLQELQARLSES--------ERQRAELAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1194 QVDTLTFQSQSLRDRARRFEEALRKNTEE--QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILE-LEKLAEKNI 1270
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDvsSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEqLEEEEEAKR 513
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489865997 1271 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKKRLSRTNEEL 1328
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRL 578
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1203-1333 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1203 QSLRDRARRFEEALRKNtEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ 1282
Cdd:COG1196 235 RELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEER 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1489865997 1283 NEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1333
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1035-1334 |
2.32e-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: 52.38 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1035 FFRKNESAL-------VKEKELSIELANIRDEVafhtakcEKLQKEKEELERrFEDEVKRL----GWQQQAELQELEERL 1103
Cdd:TIGR02169 168 FDRKKEKALeeleeveENIERLDLIIDEKRQQL-------ERLRREREKAER-YQALLKEKreyeGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1104 QlQFEAEMARLQEEhgdqllsircqhqeqVEDLTASHDAALLEMEnnhtvAITILQDDHDHKVQELMSTHELEKKELEEN 1183
Cdd:TIGR02169 240 E-AIERQLASLEEE---------------LEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1184 FEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE--EQLEIALAPYQ----HLEEDMKSLKQVLEMKNQqiheqek 1257
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERkrrdKLTEEYAELKEELEDLRA------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1258 kilELEKLAEKNIILEEKIQVLQQQNEDLKARI-------DQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELL- 1329
Cdd:TIGR02169 372 ---ELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAl 448
|
330
....*....|.
gi 1489865997 1330 ------WKLQT 1334
Cdd:TIGR02169 449 eikkqeWKLEQ 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1047-1292 |
2.69e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQEehgdQLLSIR 1126
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAAL-EAELAELEK----EIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1127 CQHQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLR 1206
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1207 DrarrfeealrknTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 1286
Cdd:COG4942 164 A------------LRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAE---LAAELAELQQEAEEL 225
|
....*.
gi 1489865997 1287 KARIDQ 1292
Cdd:COG4942 226 EALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1047-1326 |
3.23e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAE-LQELEERLqlqfeaemarlqEEHGDQLLSI 1125
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKL------------KKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1126 RCQHQEQVEDLtashdaaLLEMENNhtvaITILQDDHDhKVQELMStHELEKKELEENFEKLRLSLQDQVDTLTFQS-QS 1204
Cdd:PRK03918 523 KAEEYEKLKEK-------LIKLKGE----IKSLKKELE-KLEELKK-KLAELEKKLDELEEELAELLKELEELGFESvEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1205 LRDRARRFEEALR-----KNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILEL---------EKLAEKNI 1270
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyEELREEYL 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489865997 1271 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 1326
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1191-1325 |
7.74e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1191 LQDQVDTLTFQSQSLRDRARRFEEALRKN------TEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKkilELEK 1264
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQArseleqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE---ELEE 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489865997 1265 LAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1325
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
997-1318 |
1.03e-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: 50.11 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 997 VLRLKERCEQQTRQLGVAQG-------ELKRAICGFDALAVATQHFFRKNESALvkeKELSIELANIRDEVAFHTAKCEK 1069
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQL---KIITMELQKKSSELEEMTKFKNN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1070 LQKEKEELERRFEDEVKRLGWQQQAElqELEERLQLQfEAEM-----ARLQEEHG--DQLLSIRCQHQ---EQVED---- 1135
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFE--KIAEELKGK-EQELifllqAREKEIHDleIQLTAIKTSEEhylKEVEDlkte 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1136 ----------LTASHDAALLEME------NNHTVAITILQDD--HDHKVQELMSTHELEKKELEENF----EKLRLSLQD 1193
Cdd:pfam05483 480 lekeklknieLTAHCDKLLLENKeltqeaSDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLrdelESVREEFIQ 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1194 QVDTLTFQSQSLRDRARRFEEALRK-------------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL 1260
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKkekqmkilenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1261 ELE-KLAEKNIILEEKIQVLQQQNEDLK---ARIDQNTVVTRQLSEENANLQEYVEKETQEK 1318
Cdd:pfam05483 640 KLElELASAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHK 701
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
985-1336 |
1.10e-05 |
|
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: 49.97 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 985 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1064
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1065 AKCEKLQKEKEELERR-----------------------FEDEVKRLGWQQQ---AELQELEERLQlQFEAEMARLQEEH 1118
Cdd:TIGR00618 494 ARLLELQEEPCPLCGScihpnparqdidnpgpltrrmqrGEQTYAQLETSEEdvyHQLTSERKQRA-SLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1119 gDQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEK----LRLSLQDQ 1194
Cdd:TIGR00618 573 -SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQelalKLTALHAL 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1195 VDTLTFQSQSLRDRARRFEEALRKnteEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniilee 1274
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELL---ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------ 722
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1275 kiqvLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKrlSRTNEELLWKLQTGD 1336
Cdd:TIGR00618 723 ----IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH--FNNNEEVTAALQTGA 778
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1066-1323 |
1.12e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1066 KCEKLQKEKEELERRFEDEVKRLGWQ---QQAELQEL-------EERLQL--------------------QFEAEMARLQ 1115
Cdd:pfam01576 198 KEEKGRQELEKAKRKLEGESTDLQEQiaeLQAQIAELraqlakkEEELQAalarleeetaqknnalkkirELEAQISELQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1116 E----------------------------EHGDQLLSIRCQHQ-----EQ--------VEDLTASHDAALLEMENNHTVA 1154
Cdd:pfam01576 278 EdleseraarnkaekqrrdlgeelealktELEDTLDTTAAQQElrskrEQevtelkkaLEEETRSHEAQLQEMRQKHTQA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1155 ITILQDDHDHkvqelmstheleKKELEENFEKLRLSLQDQVDTLTFQSQSLRdRARRFEEALRKNTEEQLEIALAPY--- 1231
Cdd:pfam01576 358 LEELTEQLEQ------------AKRNKANLEKAKQALESENAELQAELRTLQ-QAKQDSEHKRKKLEGQLQELQARLses 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1232 ----QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ-NEDLKARIDQNTVVtRQLSEENAN 1306
Cdd:pfam01576 425 erqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS---LESQLQDTQELlQEETRQKLNLSTRL-RQLEDERNS 500
|
330
....*....|....*..
gi 1489865997 1307 LQEYVEKETQEKKRLSR 1323
Cdd:pfam01576 501 LQEQLEEEEEAKRNVER 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1047-1328 |
1.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIELANIRDEVafhtakcEKLQKEKEELERRFE--DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlls 1124
Cdd:PRK03918 210 NEISSELPELREEL-------EKLEKEVKELEELKEeiEELEKELESLEGSKRKLEEKIR-ELEERIEELKKE------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1125 IRcQHQEQVEDLTAshdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTFQSQS 1204
Cdd:PRK03918 275 IE-ELEEKVKELKE------LKEKAEEYIKLSEFYEEYLDELREI---------------EKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1205 LRDRARRFEEALRKNTEEQLEIA-LAPYQHLEEDMKSLKQVLE-----MKNQQIHEQEKKILELEK----LAEKNIILEE 1274
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEeLEERHELYEEAKAKKEELErlkkrLTGLTPEKLEKELEELEKakeeIEEEISKITA 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1489865997 1275 KIQVLQQQNEDLKARIDQ-------NTVVTRQLSEENAnlQEYVEKETQEKKRLSRTNEEL 1328
Cdd:PRK03918 413 RIGELKKEIKELKKAIEElkkakgkCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEI 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1068-1310 |
1.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1068 EKLQKEKEELERRFedevKRLGWQQQAELQELEERLQlQFEAEMARLQEEHgDQLLSIRcqhqEQVEDLTAshdaallem 1147
Cdd:COG4717 49 ERLEKEADELFKPQ----GRKPELNLKELKELEEELK-EAEEKEEEYAELQ-EELEELE----EELEELEA--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1148 ennhtvAITILQDDHDhkvqelmsthelekkeleenfeklRLSLQDQVDTLTFQSQSLRDRARRFEEALrknteEQLEIA 1227
Cdd:COG4717 110 ------ELEELREELE------------------------KLEKLLQLLPLYQELEALEAELAELPERL-----EELEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1228 LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKK------------ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTV 1295
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LE 233
|
250
....*....|....*
gi 1489865997 1296 VTRQLSEENANLQEY 1310
Cdd:COG4717 234 NELEAAALEERLKEA 248
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
935-1327 |
1.68e-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: 49.45 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 935 GTKKDAQKDQDTNKPAVSSpkRVAASTTKLHSpGYPKQRTAAARNGFPPKPDPQAREAErqlvlrLKERCEQQTRQLGVA 1014
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKE--QNNRDIAGIKD-KLAKIREARDRQLAVAEDDLQALESE------LREQLEAGKLEFNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1015 QGELKRAICGFDALAVATQHffrknESALVKEKELSIELAN-IRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG---- 1089
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQATA-----TPELLLQLENFDERIErAREEQEAANAEVERLQSELRQARKRRDQASEALRqasr 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1090 --WQQQAELQELEERLQ------LQFEAEMARLQEEHGDQLLSIRCQHQeqvEDLTASHDAALLEMENN-HTVAITILQD 1160
Cdd:pfam12128 514 rlEERQSALDELELQLFpqagtlLHFLRKEAPDWEQSIGKVISPELLHR---TDLDPEVWDGSVGGELNlYGVKLDLKRI 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1161 DHDHKVQelmsthelekkeleeNFEKLRLSLqDQVDTlTFQSQslRDRARRFEEAL---RKNTEEQ---LEIALAPYQHL 1234
Cdd:pfam12128 591 DVPEWAA---------------SEEELRERL-DKAEE-ALQSA--REKQAAAEEQLvqaNGELEKAsreETFARTALKNA 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1235 EEDMKSL---KQVLEMK-NQQIHE-QEKKILELEKL-AEKNIILEEKIQVLQQQNEDLK----ARIDQNTVVTRQLSEEN 1304
Cdd:pfam12128 652 RLDLRRLfdeKQSEKDKkNKALAErKDSANERLNSLeAQLKQLDKKHQAWLEEQKEQKReartEKQAYWQVVEGALDAQL 731
|
410 420
....*....|....*....|....
gi 1489865997 1305 ANLQEYVEK-ETQEKKRLSRTNEE 1327
Cdd:pfam12128 732 ALLKAAIAArRSGAKAELKALETW 755
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
985-1326 |
1.69e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 985 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1064
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1065 AKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQE--EHGDQLLSI-RCQHQEQ-VE 1134
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEdfleelREERDELREREA-ELEATLRTARErvEEAEALLEAgKCPECGQpVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1135 DltASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRARR 1211
Cdd:PRK02224 463 G--SPHVETI---------------EEDRERVEEL---------------EAELEDLEEEVEEVEErleRAEDLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1212 FEEAL--RKNTEEQLEIALAPYQHLEEDMKSL---KQVLEMKNQqihEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 1286
Cdd:PRK02224 511 IERLEerREDLEELIAERRETIEEKRERAEELrerAAELEAEAE---EKREAAAEAEEEAEE---AREEVAELNSKLAEL 584
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1287 KARIDQ-NTVVTR---------QLSEENANLQEYVEKETQEKKRLSRTNE 1326
Cdd:PRK02224 585 KERIESlERIRTLlaaiadaedEIERLREKREALAELNDERRERLAEKRE 634
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
988-1289 |
2.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAErQLVLRLKERC--------EQQTR--QLGVAQGELKRA--ICGFDALAV----ATQHFFRKNESALVK-----E 1046
Cdd:PRK04863 384 RAEAAE-EEVDELKSQLadyqqaldVQQTRaiQYQQAVQALERAkqLCGLPDLTAdnaeDWLEEFQAKEQEATEellslE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIE-------------LANIRDEV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQF 1107
Cdd:PRK04863 463 QKLSVAqaahsqfeqayqlVRKIAGEVsrseAWDVAR---------ELLRRLREQRHLAEQLQQlrMRLSELEQRLRQQQ 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1108 EAEmaRLQEEHGdQLLSIRCQHQEQVEDLTASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKL 1187
Cdd:PRK04863 534 RAE--RLLAEFC-KRLGKNLDDEDELEQLQEELEARL---------------ESLSESVSEA---------------RER 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1188 RLSLQDQVDTLTFQSQSLRDRARRFEEAlrKNTEEQLeialapYQHLEEDMKSLKQVLE-MKNQQIHEQEkkilelekLA 1266
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAA--QDALARL------REQSGEEFEDSQDVTEyMQQLLERERE--------LT 644
|
330 340
....*....|....*....|...
gi 1489865997 1267 EKNIILEEKIQVLQQQNEDLKAR 1289
Cdd:PRK04863 645 VERDELAARKQALDEEIERLSQP 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1077-1305 |
2.90e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1077 LERRFEDEVKRLGWQQQaELQELEERLQlQFEAEMARLQEEHG------------DQLLSIRCQH---QEQVEDLTASHD 1141
Cdd:COG3206 166 LELRREEARKALEFLEE-QLPELRKELE-EAEAALEEFRQKNGlvdlseeaklllQQLSELESQLaeaRAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1142 AALLEMENNHTVAITILQDDhdhKVQELMSthelekkeleeNFEKLRLSLQDQVDTLTFQS---QSLRDRARRFEEALRK 1218
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSP---VIQQLRA-----------QLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTVVTR 1298
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-ARLAE 381
|
....*..
gi 1489865997 1299 QLSEENA 1305
Cdd:COG3206 382 ALTVGNV 388
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1219-1333 |
3.05e-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: 45.30 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKIlELEKLAEKNiiLEEKIQVLQQQNEDLKARIDQNTVVTR 1298
Cdd:pfam09744 33 NVLELLESLASRNQEHNVELEELREDNE---QLETQYEREK-ALRKRAEEE--LEEIEDQWEQETKDLLSQVESLEEENR 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1489865997 1299 QLSEENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 1333
Cdd:pfam09744 107 RLEADHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1036-1317 |
3.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1036 FRKNESALVKEKELSIELANIRDEVAFHTAkcEKLQKEKEELE------RRFEDEVKRLGwQQQAELQELEERLQLqFEA 1109
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEklkeklIKLKGEIKSLK-KELEKLEELKKKLAE-LEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1110 EMARLQEEHGDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleENFEKLRL 1189
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREE-------------KELKKLEE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1190 SLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN 1269
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEE-------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1489865997 1270 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQE 1317
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1047-1339 |
3.62e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQEEHG- 1119
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeleslQEEAEELQEELE-ELQKERQDLEQQRKq 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1120 -----DQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQ 1194
Cdd:COG4372 134 leaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1195 VDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM--KNQQIHEQEKKILELEKLAEKNIIL 1272
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1273 EEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTS 1339
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1038-1328 |
4.85e-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: 47.71 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1038 KNESALVKEKELSIE--LANIRDEvafHTAKCEKLQ--KEKEELERRFEDEVKRLGwQQQAELQELEERLQLQFEAEMAR 1113
Cdd:TIGR04523 172 ENELNLLEKEKLNIQknIDKIKNK---LLKLELLLSnlKKKIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1114 LQEEHgDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVaITILQDDhdhkVQELMSthelekkeleenfEKLRLSLQD 1193
Cdd:TIGR04523 248 ISNTQ-TQLNQLKDEQNKIKKQL----SEKQKELEQNNKK-IKELEKQ----LNQLKS-------------EISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1194 QVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlapyqHLEEDMKSLKQV---LEMKNQQIHEQ-EKKILELEKLAEKN 1269
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----QLNEQISQLKKEltnSESENSEKQRElEEKQNEIEKLKKEN 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489865997 1270 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1289 |
7.18e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1064 TAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQL------QFEAEMARLQEEHGD---QLLSIRCQ 1128
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKkeekalLKQLAALERRIAAlarrirALEQELAALEAELAElekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1129 HQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLRDR 1208
Cdd:COG4942 99 LEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1209 ARRFEEAlRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDLKA 1288
Cdd:COG4942 166 RAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAE 241
|
.
gi 1489865997 1289 R 1289
Cdd:COG4942 242 R 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
998-1331 |
7.27e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 998 LRLKERCEQQTRQLGVAQgelKRAI----CGFDALAVATQHFFRKNESaLVKEKELSIELANIRDEVAFHTA-KCEKLQK 1072
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQ---RKAIqelqFENEKVSLKLEEEIQENKD-LIKENNATRHLCNLLKETCARSAeKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1073 EKEELERRFEDevkrlgwqqqaeLQELEERLQLQFEAemARLQEEHgdqllsircqhqeqvedltashdaALLEMENNht 1152
Cdd:pfam05483 177 EREETRQVYMD------------LNNNIEKMILAFEE--LRVQAEN------------------------ARLEMHFK-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1153 vaitiLQDDHDhKVQELMSTHELEKKELEENFEKLRLSL---QDQVDTLTFQSQSLRDRARRFEEA-------LRKNTEE 1222
Cdd:pfam05483 217 -----LKEDHE-KIQHLEEEYKKEINDKEKQVSLLLIQItekENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1223 Q-------------LEIALAPYQHLEEDM----KSLKQVLEMKNQQIHEQEK----KILELEKLAEKNIILEEKIQVLQQ 1281
Cdd:pfam05483 291 KdhltkeledikmsLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKakaaHSFVVTEFEATTCSLEELLRTEQQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489865997 1282 QnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELLWK 1331
Cdd:pfam05483 371 R---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDE 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
986-1327 |
8.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 986 DPQAREAERQL--VLRLKERCEQQTRQLGVAQGELKRAICGFDALAVAT-QHFFRKNESALVKEKELSIELANIRDEVAF 1062
Cdd:COG4717 145 PERLEELEERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1063 HTAKCEKLQKEKE--ELERRFEDE--------------------------------------VKRLGWQQQAELQELEER 1102
Cdd:COG4717 225 LEEELEQLENELEaaALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1103 LQLQFEAEMARLQEEHGDQLLSIR----CQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELM-STHELEK 1177
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLaEAGVEDE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1178 KELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEMKNQQIHEQEK 1257
Cdd:COG4717 385 EELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL---EELEEELEELEEELEELREELAELEA 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489865997 1258 KILELEKlaekniilEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQ---EYVEKETQ--EKKRLSRTNEE 1327
Cdd:COG4717 461 ELEQLEE--------DGELAELLQELEELKAEL-------RELAEEWAALKlalELLEEAREeyREERLPPVLER 520
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
524-931 |
1.12e-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: 46.83 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 524 ARADSVLNIPAPLHPET--TVNMTYQPTTPSSSFQDVSVFGMDAGSPLVVPPPtdSARLLNTSPKVPDKNTCPSGIPKPV 601
Cdd:pfam05109 440 AAPNTTTGLPSSTHVPTnlTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSP--SPRDNGTESKAPDMTSPTSAVTTPT 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 602 FTHSKDTPSSQEGMENYQVEKTEERTETKPIIMPKPKHVRPkiityirrNPQALGQVDASLVPVGLPYAPPTC-TMPLPH 680
Cdd:pfam05109 518 PNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP--------TPAVTTPTPNATIPTLGKTSPTSAvTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 681 EEKAAGGDLKPSANLYEKFKPDLQKPRVFSSglmvsgikPPGHPFSQMSEkflqevtdhpGKEEFCSPPYAHYEVPPTFY 760
Cdd:pfam05109 590 ATSPTVGETSPQANTTNHTLGGTSSTPVVTS--------PPKNATSAVTT----------GQHNITSSSTSSMSLRPSSI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 761 RSAmlLKPQLGLGAMSRLPSAKS----------RILIASQRSSASAIHPPGPITTATSLYS--SDPSDLKKASSSNAAKS 828
Cdd:pfam05109 652 SET--LSPSTSDNSTSHMPLLTSahptggenitQVTPASTSTHHVSTSSPAPRPGTTSQASgpGNSSTSTKPGEVNVTKG 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 829 NLPKSGLRPpgysRLPAAKLAAFGFVrSSSVSSVSSTQSGDSAQPEQGRPATRST--FGNEEQpvlkaslpSKDTPKGAG 906
Cdd:pfam05109 730 TPPKNATSP----QAPSGQKTAVPTV-TSTGGKANSTTGGKHTTGHGARTSTEPTtdYGGDST--------TPRTRYNAT 796
|
410 420
....*....|....*....|....*
gi 1489865997 907 RVAPPASSSVTAPRRSLLPAPKSTS 931
Cdd:pfam05109 797 TYLPPSTSSKLRPRWTFTSPPVTTA 821
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1328 |
1.15e-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: 46.97 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1201 QSQSLRDRARRFEEALRKNTEE---QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNII---LE 1273
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEeKLEELRLEvseLE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489865997 1274 EKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQ-EYVEKETQ---EKKRLSRTNEEL 1328
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQleeLESKLDELAEEL 339
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1213-1342 |
1.82e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1213 EEALRKNTEEQLEialapyQHLEEDMKSLKQV-----------LEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQ 1281
Cdd:PHA02562 108 ESASSKDFQKYFE------QMLGMNYKSFKQIvvlgtagyvpfMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQ 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1282 QNEDLKARID--------QNTVVTRQLSEENANLQEY-------VEKETQEKKRLSRTNEELL-WKLQTGDPTSPIK 1342
Cdd:PHA02562 182 QIQTLDMKIDhiqqqiktYNKNIEEQRKKNGENIARKqnkydelVEEAKTIKAEIEELTDELLnLVMDIEDPSAALN 258
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
640-992 |
1.98e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 640 VRPKIITYIRrNPQALGQVDASLVPVGLPYAPPTCT----------MPLPHEEKAAGGDLKPSAnlyekfKPDLQKPRVf 709
Cdd:PHA03247 2529 VHPRMLTWIR-GLEELASDDAGDPPPPLPPAAPPAApdrsvppprpAPRPSEPAVTSRARRPDA------PPQSARPRA- 2600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 710 ssglmvsGIKPPGHPFSQMSEKflqevtdhpgkeefCSPPYAHYEVPPTFYRSAMLLKPQLGlGAMSRLPSAKSRILIAS 789
Cdd:PHA03247 2601 -------PVDDRGDPRGPAPPS--------------PLPPDTHAPDPPPPSPSPAANEPDPH-PPPTVPPPERPRDDPAP 2658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 790 QRSSAS--AIHPPGPITTATSLYSSDPSDLKKASSSNAAKSNLPksglrPPGYSRLPAAKLAAFGfvrssSVSSVSSTQS 867
Cdd:PHA03247 2659 GRVSRPrrARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPP-----PPPPTPEPAPHALVSA-----TPLPPGPAAA 2728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 868 GDSAQPEQGRPATRSTFGNEEQPVLKASLPSKDTPKGAGRVAPPASSSVTAPRRslLPAPKSTSTPAGTKKDAQKDQDTN 947
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPAD 2806
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1489865997 948 KPAVSSPKRVAASTTKLHSPGYPKQRTAAARNGFPPKPDPQAREA 992
Cdd:PHA03247 2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1219-1325 |
2.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALAPYQHLEEDMKSLKQVL-----EMKNQQIHEQEKKILEL-EKLAEKNIILEEKiQVLQQQNEDLKARIDQ 1292
Cdd:PRK11281 198 QAEQALLNAQNDLQRKSLEGNTQLQDLlqkqrDYLTARIQRLEHQLQLLqEAINSKRLTLSEK-TVQEAQSQDEAARIQA 276
|
90 100 110
....*....|....*....|....*....|...
gi 1489865997 1293 NTVVTRQLsEENANLQEYVEKETQEKKRLSRTN 1325
Cdd:PRK11281 277 NPLVAQEL-EINLQLSQRLLKATEKLNTLTQQN 308
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1064-1324 |
2.68e-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: 45.51 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1064 TAKCEKLQKEKEELeRRFEDEVKRL---GWQQQAELQ----EL------EERLQLQFE--------AEMARLQEEHGDQ- 1121
Cdd:pfam07111 62 SQQAELISRQLQEL-RRLEEEVRLLretSLQQKMRLEaqamELdalavaEKAGQAEAEglraalagAEMVRKNLEEGSQr 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1122 -LLSIRCQHQEQVEDLTASHDAALLEMENNHT---VAITILQDDHDHKVQELmSTHELEKKELEENFEKLRLSLQDQVdT 1197
Cdd:pfam07111 141 eLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEgleKSLNSLETKRAGEAKQL-AEAQKEAELLRKQLSKTQEELEAQV-T 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1198 LTfqsQSLRDRA--RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLE-----------MKNQQIHEQEKKI----- 1259
Cdd:pfam07111 219 LV---ESLRKYVgeQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVEllqvrvqslthMLALQEEELTRKIqpsds 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489865997 1260 LELEKLAEKNIIL---EEKIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRT 1324
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 ... |
1065-1328 |
2.89e-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: 45.55 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1065 AKCEKLQKEKE----------ELERRF---EDEVKRLGWQQQAEL-----------------QELEERLQlqfeaEM-AR 1113
Cdd:pfam01576 9 AKEEELQKVKErqqkaeselkELEKKHqqlCEEKNALQEQLQAETelcaeaeemrarlaarkQELEEILH-----ELeSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1114 LQEEH--GDQLLSIRCQHQEQVEDLTAShdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSL 1191
Cdd:pfam01576 84 LEEEEerSQQLQNEKKKMQQHIQDLEEQ-----LDEEEAARQKLQLEKVTTEAKIKKL---------------EEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1192 QDQVDTLTFQSQSLRDRARRFEEALRKntEEQLEIALAPYQHLEEDMKSLKQVlemknqQIHEQEKKILELEKLAEKnii 1271
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAE--EEEKAKSLSKLKNKHEAMISDLEE------RLKKEEKGRQELEKAKRK--- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1272 LEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1203-1327 |
2.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1203 QSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEmknQQIHEQEKKILELEK-LAEKNIILEEKIQVLQQ 1281
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFE---KELRERRNELQKLEKrLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1489865997 1282 QNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR-TNEE 1327
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEE 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1185-1329 |
3.33e-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: 45.43 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1185 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALA------PYQHLEEDMKSLKQVLEMKNQQIHEQEKK 1258
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1259 ILEL-EKLAEkniiLEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEELL 1329
Cdd:TIGR02168 332 LDELaEELAE----LEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVAQLELQIAS 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1045-1309 |
3.88e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1045 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG--WQQQAELQELEERLQLQFE--AEMARLQEEHGD 1120
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEAEIEDLREtiAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1121 QLLSircqHQEQVEDLtashdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDqvdtLTF 1200
Cdd:PRK02224 280 EVRD----LRERLEEL---------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----HNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1201 QSQSLRDRARRFEEALRKNTEEQLEialapyqhLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNII----LEEKI 1276
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnAEDFL 414
|
250 260 270
....*....|....*....|....*....|....*.
gi 1489865997 1277 QVLQQQNEDLKARIDQNTVVTRQLS---EENANLQE 1309
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARervEEAEALLE 450
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1042-1327 |
4.11e-04 |
|
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: 44.14 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1042 ALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLgwQQQAELQE-LEERLQLQFEAEMARLQEehGD 1120
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK--RYRQELEEqIEEREQKRQEEYEEKLQE--RE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1121 QLLSIrcQHQEQVEDltashdaaLLEMENNHtvaitilqddhdhkvqelmsthelekkeleenfeKLRLSLQDQVDtltf 1200
Cdd:pfam13868 102 QMDEI--VERIQEED--------QAEAEEKL----------------------------------EKQRQLREEID---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1201 qsqslrdrarRFEEALRKNTEEQLEialapyQHLEEDMKsLKQVLEMKNQQIHEQEKKILELEKLAEKNIileEKIQVLQ 1280
Cdd:pfam13868 134 ----------EFNEEQAEWKELEKE------EEREEDER-ILEYLKEKAEREEEREAEREEIEEEKEREI---ARLRAQQ 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1281 QQNEDLKARIDQntVVTRQLSEENANLQEYVEKETQEKKR-----LSRTNEE 1327
Cdd:pfam13868 194 EKAQDEKAERDE--LRAKLYQEEQERKERQKEREEAEKKArqrqeLQQAREE 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1185-1328 |
4.40e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1185 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapyQHLEEDMKSLKQVLEMKNQQIH------EQEKK 1258
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------KRLELEIEEVEARIKKYEEQLGnvrnnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1259 ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQeyvEKETQEKKRLSRTNEEL 1328
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAE---LEAELAELEAELE---EKKAELDEELAELEAEL 158
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1244-1334 |
4.65e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1244 VLEMKNQQIHEQEKKILELEKlaeKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1323
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90
....*....|.
gi 1489865997 1324 TNEELLWKLQT 1334
Cdd:TIGR04523 282 KIKELEKQLNQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1091-1328 |
4.85e-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: 43.98 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1091 QQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTAshdaallemennhtvAITILQDDHDHKVQELm 1170
Cdd:COG4942 24 EAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLA-ALERRIAALAR---------------RIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1171 sthelekkeleenfeklrLSLQDQVDTLTFQSQSLRDR-ARRFEEALRKNTEEQLEIALAP--YQHLEEDMKSLKQVLEM 1247
Cdd:COG4942 86 ------------------AELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1248 KNQQIHEQEKKILELEKLAEKNIILEEKIQVL----QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1323
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
....*
gi 1489865997 1324 TNEEL 1328
Cdd:COG4942 228 LIARL 232
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1236-1333 |
5.17e-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: 42.97 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1236 EDMKSLK-QVLEMKNQQIH--------EQEKKIL--ELEKLAEKNIILEEKIQVLQQQNEDL---KARIDQNTVVTRQLS 1301
Cdd:pfam13851 26 ELIKSLKeEIAELKKKEERneklmseiQQENKRLtePLQKAQEEVEELRKQLENYEKDKQSLknlKARLKVLEKELKDLK 105
|
90 100 110
....*....|....*....|....*....|..
gi 1489865997 1302 EENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1333
Cdd:pfam13851 106 WEHEVLEQRFEKVERERDELYDKFEAAIQDVQ 137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1025-1309 |
6.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1025 FDALAVATQHF--FRKNESALVKEKElSIE-LANIRdevafhtAKCEKLQKEKEELERrFEDEVKRLG-WQQQAELQELE 1100
Cdd:COG4913 224 FEAADALVEHFddLERAHEALEDARE-QIElLEPIR-------ELAERYAAARERLAE-LEYLRAALRlWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1101 ERLQlQFEAEMARLQEehgdqllsircqhqeQVEDLTASHDAA---LLEMENnhtvaiTILQDDHDhkvqelmsthelek 1177
Cdd:COG4913 295 AELE-ELRAELARLEA---------------ELERLEARLDALreeLDELEA------QIRGNGGD-------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1178 keleenfeklRL-SLQDQVDTLTFQSQSLRDRARRFEEALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQ 1250
Cdd:COG4913 339 ----------RLeQLEREIERLERELEERERRRARLEALLAAlglplpASAEEFAALRAEAAALLEALEEELEALE---E 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489865997 1251 QIHEQEKKILELEKLAEKniiLEEKIQVLQQQnedlKARIDQNTVVTRQLSEENANLQE 1309
Cdd:COG4913 406 ALAEAEAALRDLRRELRE---LEAEIASLERR----KSNIPARLLALRDALAEALGLDE 457
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
834-1070 |
9.27e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.52 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 834 GLRPPGYSRLPAAKLAAFGFVRSSSVSSVSSTQSGDSAQPEQGRPATRSTfgnEEQPvlKASLPSKDTPKGAGRVAPPAS 913
Cdd:PRK14959 377 GASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAP--SPRVPWDDAPPAPPRSGIPPR 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 914 SSVTAPRRSLLP-APKSTSTPAGTkkdaqkdqdtnkpavsSPKRVAASTTKLHSPGYPKQ-----RTAAARNGFPPKPDP 987
Cdd:PRK14959 452 PAPRMPEASPVPgAPDSVASASDA----------------PPTLGDPSDTAEHTPSGPRTwdgflEFCQGRNGQGGRLAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQL---VLRLKERCEQQTRQLGVAQGE-----LKRAICGFDA-LAVATQHFFRKNESALVKEKELSIELANIRD 1058
Cdd:PRK14959 516 VLRQATPEHadgRLRLATMSSVQYERLTDAATEttlagLVRDYFGDACrVEVLPPTRVRRTEAELRKEAEAHPAVQLLKE 595
|
250
....*....|..
gi 1489865997 1059 EVAFHTAKCEKL 1070
Cdd:PRK14959 596 EMGACILKCTPL 607
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
1262-1333 |
9.74e-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: 39.17 E-value: 9.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1262 LEKLAEKNIILEEKIQVLQQQNEDLKARidqntvvTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1333
Cdd:pfam06005 6 LEQLETKIQAAVDTIALLQMENEELKEE-------NEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1066-1321 |
1.31e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1066 KCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQF-------EAEMARLQEEHGdqllsiRCQhqEQVEDLTA 1138
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIndrirllEQEVARYKEESG------KAQ--AEVERLLG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1139 shdaALLEMENNhtvaitilQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALRK 1218
Cdd:pfam10174 587 ----ILREVENE--------KNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK---GAQLLEEARRREDNLADN 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEklAEKNIILEEkiqVLQQQNEDLKARI---DQNTV 1295
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR--AERRKQLEE---ILEMKQEALLAAIsekDANIA 726
|
250 260
....*....|....*....|....*.
gi 1489865997 1296 VTRQLSEENANLQEYVEKETQEKKRL 1321
Cdd:pfam10174 727 LLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1070-1328 |
1.32e-03 |
|
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: 43.14 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1070 LQKEKEELERR-FEDEvkrlgwQQQAELQEleERLQLQfeAEMARLQE-----EHGDQLLSIRC----QHQEQVEDLTAS 1139
Cdd:pfam05622 5 AQEEKDELAQRcHELD------QQVSLLQE--EKNSLQ--QENKKLQErldqlESGDDSGTPGGkkylLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1140 hdaaLLEMENNhtvaitilQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRArrfeEAL 1216
Cdd:pfam05622 75 ----NFRLETA--------RDDYRIKCEEL---------------EKEVLELQHRNEELTSlaeEAQALKDEM----DIL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1217 RKNTEE--QLEIALAPYQHLEEDMKSLK-QV--LEMKNQqIHEQEKkiLELEKLAEKNIILEEKIQVLQQQNEDLKARID 1291
Cdd:pfam05622 124 RESSDKvkKLEATVETYKKKLEDLGDLRrQVklLEERNA-EYMQRT--LQLEEELKKANALRGQLETYKRQVQELHGKLS 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1489865997 1292 QNTVVTRQLSEENANLQEYVEKETQEKKRLS-------RTNEEL 1328
Cdd:pfam05622 201 EESKKADKLEFEYKKLEEKLEALQKEKERLIierdtlrETNEEL 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1069-1312 |
1.44e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1069 KLQKEKEELERRF----------EDEVKRLGW---QQQAELQELEERLQ-------------LQFEAEMARLQEEHGD-- 1120
Cdd:pfam01576 149 KLSKERKLLEERIseftsnlaeeEEKAKSLSKlknKHEAMISDLEERLKkeekgrqelekakRKLEGESTDLQEQIAElq 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1121 -QLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQ-DDHDHKVQELMSTHELEKKELEEN-------FEKLRLSL 1191
Cdd:pfam01576 229 aQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQrrdlgeeLEALKTEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1192 QDQVDTLTFQsQSLRDRARRFEEALRKNTEEQLEIALAPYQHLE--------------EDMKSLKQVLEmKNQQIHEQEK 1257
Cdd:pfam01576 309 EDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMRqkhtqaleelteqlEQAKRNKANLE-KAKQALESEN 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1258 KIL--ELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE 1312
Cdd:pfam01576 387 AELqaELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1185-1329 |
1.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1185 EKLRLSLQDQVDTLTFQSQSLRDRARRFE------EALRKNTEEQLEIALAP--YQHLEEDMKSLKQvlemknqQIHEQE 1256
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLEleieevEARIKKYEEQLGNVRNNkeYEALQKEIESLKR-------RISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489865997 1257 KKILEL-EKLAEKNIILEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRT-NEELL 1329
Cdd:COG1579 110 DEILELmERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEELEAEREELAAKiPPELL 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1208-1328 |
1.51e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1208 RARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDL 1286
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEeELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1489865997 1287 KARIDQNTVVTRQL---SEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:COG4372 90 QAAQAELAQAQEELeslQEEAEELQEELEELQKERQDLEQQRKQL 134
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1038-1288 |
1.53e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1038 KNESALVKEKE-LSIELANIRDEVAFHTAKCEKLQKEKEELERRFED---EVKRLGWQQQAELQ---------------- 1097
Cdd:TIGR02169 230 KEKEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGEEEQLRVKekigeleaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1098 --ELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQddhdhKVQELMSTHEL 1175
Cdd:TIGR02169 310 iaEKERELE-DAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRA-----ELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1176 EKKELEENFEKL------RLSLQDQVDTLTFQSQSLRDRARRFEEAL-----RKN------TEEQLEIALAPYQ--HLEE 1236
Cdd:TIGR02169 383 TRDELKDYREKLeklkreINELKRELDRLQEELQRLSEELADLNAAIagieaKINeleeekEDKALEIKKQEWKleQLAA 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1237 DMKSLKQVLEMKNQQIHEQEKkilELEKLAEKNIILEEKIQVLQQQNEDLKA 1288
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
988-1308 |
1.54e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLvlrlKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALV----KEKELSIELANIRDEVAFH 1063
Cdd:pfam15921 332 ELREAKRMY----EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1064 TAKCEKLQKEKEELERRfEDEVKRLgwqqQAELQELEERLQLQFEAEMARLQEEHgdqllsircQHQEQVEDLTAshdaa 1143
Cdd:pfam15921 408 TGNSITIDHLRRELDDR-NMEVQRL----EALLKAMKSECQGQMERQMAAIQGKN---------ESLEKVSSLTA----- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1144 llEMENNHTVAitilqddhdHKVQELMSTHELEKKELEENFEKLRLSLQDQ---VDTLTFQSQSLRDRARRFEEALR--K 1218
Cdd:pfam15921 469 --QLESTKEML---------RKVVEELTAKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLRSRVDLKLQELQhlK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAekNIILEEKIQVLQQQN------EDLKARIDQ 1292
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTA--GAMQVEKAQLEKEINdrrlelQEFKILKDK 615
|
330
....*....|....*.
gi 1489865997 1293 NTVVTRQLSEENANLQ 1308
Cdd:pfam15921 616 KDAKIRELEARVSDLE 631
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1210-1334 |
1.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1210 RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL----ELEKLAEKNIILEEKIQVLQQQNED 1285
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEqarsELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1489865997 1286 LKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1334
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1047-1123 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1047 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQfEAEMARLQEEHgDQLL 1123
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDLEEELKEKNKANEI--------LNDELIALQIENNLL-EEKLRKLQEEN-DELV 73
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
988-1227 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLVLRLKERCEQQtrqLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1067
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1068 EKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSIRCQHQEQVEDLTASHDAALLEM 1147
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1148 E-NNHTVAITILQDDHDHKVQELMSTHELEKKEleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFE---EALRKNTEEQ 1223
Cdd:TIGR02168 441 ElEELEEELEELQEELERLEEALEELREELEEA-----EQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQ 515
|
....
gi 1489865997 1224 LEIA 1227
Cdd:TIGR02168 516 SGLS 519
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1214-1307 |
1.93e-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: 41.05 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1214 EALRKNTEEQ------LEIALAPYQHLEEDMKSLK---QVLEMKNQQIHE--------QEKKILEL-EKLAEKNIILEEK 1275
Cdd:pfam13851 71 EELRKQLENYekdkqsLKNLKARLKVLEKELKDLKwehEVLEQRFEKVERerdelydkFEAAIQDVqQKTGLKNLLLEKK 150
|
90 100 110
....*....|....*....|....*....|....
gi 1489865997 1276 IQVLQqqnEDLKARidqntvvTRQLSE--ENANL 1307
Cdd:pfam13851 151 LQALG---ETLEKK-------EAQLNEvlAAANL 174
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
988-1254 |
1.95e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLVLRLKERCEQQTR----QLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 1063
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLYEKEIEdlrrQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1064 T-------AKCEKLQKEKEELERRFEDEVKrlgwqqqaELQELEERLQLQFEAEMARLQEEhgDQLLS-IRCQHQEQVED 1135
Cdd:pfam00038 116 TlarvdleAKIESLKEELAFLKKNHEEEVR--------ELQAQVSDTQVNVEMDAARKLDL--TSALAeIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1136 LTAshdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKeleenfeklrlsLQDQVDTLTFQSQSLRDRARRFEEA 1215
Cdd:pfam00038 186 NRE-------EAEEWYQSKLEELQQAAARNGDALRSAKEEITE------------LRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1489865997 1216 LRKnTEEQLEIALAPYQ----HLEEDMKSLKQVLEMKNQQIHE 1254
Cdd:pfam00038 247 LAE-TEERYELQLADYQelisELEAELQETRQEMARQLREYQE 288
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
1219-1336 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1219 NTEEQLEIALApYQHLEEDMKSLKQVLEMKNQQIHEQEKKI---------LELEKLAEKNIILEEKIQVLQQQNEDLKAR 1289
Cdd:pfam15254 378 NTNIQAEIALA-LQPLRSENAQLRRQLRILNQQLREQEKTEktsgsgdcnLELFSLQSLNMSLQNQLQESLKSQELLQSK 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1489865997 1290 idqntvvtrqlseeNANLQEYVEKETQEKKRLSRT----NEELLWKLQTGD 1336
Cdd:pfam15254 457 --------------NEELLKVIENQKEENKKLTKIfkekEQTLLENKQQFD 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
992-1310 |
2.03e-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: 42.73 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 992 AERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQ 1071
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1072 KEKEELERRFEDEVKRlgwqQQAELQELEERLqlqfeaemarlqeehgDQLLSIRCQHQEQVEDltaSHDAALLEMENNH 1151
Cdd:TIGR00606 923 QEKEELISSKETSNKK----AQDKVNDIKEKV----------------KNIHGYMKDIENKIQD---GKDDYLKQKETEL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1152 TVAITILQDDHDHKvqelmsthelekkeleENFEK-LRLSLQDqvdtltFQSQSLRDRARRFEEALRKNTEEQLEIALAP 1230
Cdd:TIGR00606 980 NTVNAQLEECEKHQ----------------EKINEdMRLMRQD------IDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1231 YQHLEE-------DMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKiQVLQQQNEDLKARIDQNTVVTRQLSEE 1303
Cdd:TIGR00606 1038 KQHLKEmgqmqvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK-ELREPQFRDAEEKYREMMIVMRTTELV 1116
|
....*..
gi 1489865997 1304 NANLQEY 1310
Cdd:TIGR00606 1117 NKDLDIY 1123
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1190-1289 |
2.21e-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: 41.20 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1190 SLQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKn 1269
Cdd:pfam04012 54 QLERRLEQQTEQAKKLEEKAQ---AALTKGNEELAREALAEKKSLEKQAEALETQLA-------QQRSAVEQLRKQLAA- 122
|
90 100
....*....|....*....|
gi 1489865997 1270 iiLEEKIQVLQQQNEDLKAR 1289
Cdd:pfam04012 123 --LETKIQQLKAKKNLLKAR 140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1234-1329 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1234 LEEDMKSLKQVLEMKNQQIHEQEKKI----LELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQE 1309
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEkallKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100
....*....|....*....|
gi 1489865997 1310 YVEKETQEKKRLSRTNEELL 1329
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAL 124
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1248-1325 |
2.71e-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: 38.32 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1248 KNQQIHEQEKKILELEK----LAEKNIILEEKIQVLQQQNEDLKARID----QNTVVT---RQLSEENANL-QEYVEKET 1315
Cdd:cd22887 2 LESELQELEKRLAELEAelasLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEeklRKLQEENDELvERWMAKKQ 81
|
90
....*....|
gi 1489865997 1316 QEKKRLSRTN 1325
Cdd:cd22887 82 QEADKMNEAN 91
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1191-1289 |
2.90e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1191 LQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQvlemknqQIHEQEKKILELEKLAEKni 1270
Cdd:COG1842 56 LERQLEELEAEAEKWEEKAR---LALEKGREDLAREALERKAELEAQAEALEA-------QLAQLEEQVEKLKEALRQ-- 123
|
90
....*....|....*....
gi 1489865997 1271 iLEEKIQVLQQQNEDLKAR 1289
Cdd:COG1842 124 -LESKLEELKAKKDTLKAR 141
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1046-1150 |
3.10e-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: 41.41 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1046 EKELSIELANIRDEVAfhTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQFEAEMARLQEEHgDQLLSI 1125
Cdd:cd16269 195 EKEKEIEAERAKAEAA--EQERKLLEEQQRELEQKLED--------QERSYEEHLRQLKEKMEEERENLLKEQ-ERALES 263
|
90 100
....*....|....*....|....*
gi 1489865997 1126 RCQHQEQVEDLTASHDAALLEMENN 1150
Cdd:cd16269 264 KLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1040-1336 |
3.60e-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: 41.63 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1040 ESALVKEKELSIELANIRDEVAFHTAK-CEKLQKEKEELERRFEDEVKRLGW------QQQAELQEL-----EERLQLQF 1107
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEdHEKIQHLEEEYKKEINDKEKQVSLlliqitEKENKMKDLtflleESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1108 EAEMARLQEEHGDQLLSIRCQHQEQVEDL------TASHDAALLEMENNHTVAITILQDDHDHKVQEL---MSTHE---L 1175
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnkaKAAHSfvvT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1176 EKKELEENFEKL----RLSLQDQVDTLTFQSQSLRDRARRFEE--ALRKNTE---EQLEIALAP----------YQHLEE 1236
Cdd:pfam05483 353 EFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEvelEELKKILAEdeklldekkqFEKIAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1237 DMKSLKQ----VLEMKNQQIHEQEKKIL------------------ELEKLAEKNI---------ILEEKIQVLQQQNED 1285
Cdd:pfam05483 433 ELKGKEQelifLLQAREKEIHDLEIQLTaiktseehylkevedlktELEKEKLKNIeltahcdklLLENKELTQEASDMT 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1489865997 1286 LKARIDQNTVVTRQLSEEN--ANLQEYVEKETQEKKRLSRTNEELlwkLQTGD 1336
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRDELESVREEF---IQKGD 562
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
988-1333 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 988 QAREAERQLVLRLKERCEQQTRQ--LGVAQGELKRAICGFDALAVATQHF-FRKNESALVKEKELSIELANIRDEVafHT 1064
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERInRARKAAPLAAHIKAVTQIEQQAQRI--HT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1065 akceKLQKEKEELERRFEDEVKRLgwQQQAELQELEERLQLQF--------EAEMARLQEEHGDQLLSIRCQHQEQVEDL 1136
Cdd:TIGR00618 315 ----ELQSKMRSRAKLLMKRAAHV--KQQSSIEEQRRLLQTLHsqeihirdAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1137 TASHD-----AALLEMENN--HTVAiTILQDDHDHKvQELMSTHELEKKeleenfEKLRLSLQDQVDTLTFQSQSLRDRA 1209
Cdd:TIGR00618 389 TTLTQklqslCKELDILQReqATID-TRTSAFRDLQ-GQLAHAKKQQEL------QQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1210 RRfEEALRKNTEEQLEIALAPYQHLEEDMKSL--KQVLEMKNQQ-----------------------------------I 1252
Cdd:TIGR00618 461 LQ-ESAQSLKEREQQLQTKEQIHLQETRKKAVvlARLLELQEEPcplcgscihpnparqdidnpgpltrrmqrgeqtyaQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1253 HEQEKKILELEKLAEKN--IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLW 1330
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
...
gi 1489865997 1331 KLQ 1333
Cdd:TIGR00618 620 KLQ 622
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1037-1341 |
4.39e-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: 41.49 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1037 RKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQE 1116
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1117 EHGD--QLLSIRCQHQEQVEDLTASHD------AALLEMENNHTVAITILqddhDHKVQELMSTHELekkeleenfeklr 1188
Cdd:TIGR00618 319 KMRSraKLLMKRAAHVKQQSSIEEQRRllqtlhSQEIHIRDAHEVATSIR----EISCQQHTLTQHI------------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1189 LSLQDQVDTLTFQSQSL--------RDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKil 1260
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLckeldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI-- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1261 ELEKLAEKniiLEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSP 1340
Cdd:TIGR00618 460 HLQESAQS---LKEREQQLQTKEQIHLQ-------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
.
gi 1489865997 1341 I 1341
Cdd:TIGR00618 530 M 530
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
631-994 |
4.80e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 631 PIIMPKPKHVRPKIITYIRRnPQALGQVDASLVPVGLPYAPPTCTMPLPHEEKAAGGDLKPSAnlyekfkpdlQKPRVFS 710
Cdd:PHA03247 2569 PPPRPAPRPSEPAVTSRARR-PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS----------PSPAANE 2637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 711 SGLMVSGIKPPghPFSQMSEKFLQEVTDHPGKEEFCSPPYAhyEVPPTFYRSAMLLKPQLGLGAMSRLPSAKSRILIASQ 790
Cdd:PHA03247 2638 PDPHPPPTVPP--PERPRDDPAPGRVSRPRRARRLGRAAQA--SSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPH 2713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 791 RSSASAIHPPGPITTATSLYSSDPSDLKKASSSNAAKSNLPKSGLRPPGYSRLPAAKLAAfgfVRSSSVSSVSSTQSGDS 870
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA---APAAGPPRRLTRPAVAS 2790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 871 AQPEQGRPATRSTFGNEEQPVL--KASLPSKDTPkgAGRVAPPASSSVTAPrrSLLPAPKSTSTPAGTKKDAQKDQDTNK 948
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLapAAALPPAASP--AGPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRRP 2866
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1489865997 949 PAVSSPKRVAAST----TKLHSPGYPKQRTAAARNGFPPKPDPQAREAER 994
Cdd:PHA03247 2867 PSRSPAAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
1260-1312 |
5.14e-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: 37.26 E-value: 5.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1489865997 1260 LELEKLAEKNIILEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQEYVE 1312
Cdd:COG3074 25 MEVEELKEKNEELEQENEELQSENEELQSEN-------EQLKTENAEWQERIR 70
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
989-1333 |
5.29e-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: 41.26 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 989 AREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDAlavATQHFFRKNESALVKEKELsieLANIRDEVAfhtAKCE 1068
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE---ALNKKLNEKESQLADAREV---ISCLKNELS---ELRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1069 KLQKEKEELERrfedevkrlgwqQQAELQELEERLQLQfeaeMARLQEehgdqllsircqHQEQVEDLTASHDAALleme 1148
Cdd:pfam05557 119 QIQRAELELQS------------TNSELEELQERLDLL----KAKASE------------AEQLRQNLEKQQSSLA---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1149 nnhtvaitilqdDHDHKVQELMsthelekkeleenfEKLRLSLQDQVDTLTFQS--------QSLRDRARRFEEALRKNT 1220
Cdd:pfam05557 167 ------------EAEQRIKELE--------------FEIQSQEQDSEIVKNSKSelaripelEKELERLREHNKHLNENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1221 E--EQLEIALAPYQ---HLEEDMKSLKQVLEMKNQQIheqEKKILELEKLAE-------KNIILEEKIQVLQQQNEDLKA 1288
Cdd:pfam05557 221 EnkLLLKEEVEDLKrklEREEKYREEAATLELEKEKL---EQELQSWVKLAQdtglnlrSPEDLSRRIEQLQQREIVLKE 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1489865997 1289 ridQNTVVTRQLSEENANLQE-------YVEKETQEKKRLSRTnEELLWKLQ 1333
Cdd:pfam05557 298 ---ENSSLTSSARQLEKARREleqelaqYLKKIEDLNKKLKRH-KALVRRLQ 345
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1126-1282 |
5.38e-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: 40.39 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1126 RCQHQEQVEDLTASHdaallemennhtvaITILQDDHDH--KVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQ 1203
Cdd:smart00787 138 RMKLLEGLKEGLDEN--------------LEGLKEDYKLlmKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1204 SLRDRARrfeEALRKnTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN--------IILEEK 1275
Cdd:smart00787 204 TELDRAK---EKLKK-LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKEQ 279
|
....*..
gi 1489865997 1276 IQVLQQQ 1282
Cdd:smart00787 280 LKLLQSL 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1047-1318 |
5.56e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1047 KELSIELANIRDEVAFHTakcEKLQKEKEELERRFEDEVKRLGWQQqaELQELEERLQLQFEAEMARLQEEHGDQLLSir 1126
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILT---QCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQDLQDVR-- 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1127 cQHQEQVEDLTASHDAALlemennHTVAITILQDDHDHKvqeLMSTHELEKKELEENFEKLRlSLQDQVDTLTF------ 1200
Cdd:TIGR00618 632 -LHLQQCSQELALKLTAL------HALQLTLTQERVREH---ALSIRVLPKELLASRQLALQ-KMQSEKEQLTYwkemla 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1201 QSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVL-EMKNQQIHEQEKKILELEKLAEKNIILEEKIQVL 1279
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
250 260 270
....*....|....*....|....*....|....*....
gi 1489865997 1280 QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK 1318
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
984-1322 |
5.89e-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: 41.19 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 984 KPDPQAREAERQL---VLRLKERCEQQTRQLGVAQGELKRA-ICGFDALAVatQHFFRKNESALVKEKELSIELANIRDE 1059
Cdd:TIGR00606 744 KEIPELRNKLQKVnrdIQRLKNDIEEQETLLGTIMPEEESAkVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1060 VAFhtakcEKLQKEKEELERRFE------DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlLSIRCQHQEQV 1133
Cdd:TIGR00606 822 RTV-----QQVNQEKQEKQHELDtvvskiELNRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTN-----LQRRQQFEEQL 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1134 EDLTA---SHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELeenfEKLRLsLQDQVDTLTFQSQSLRDRAR 1210
Cdd:TIGR00606 891 VELSTevqSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ----DKVND-IKEKVKNIHGYMKDIENKIQ 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1211 RFEEALRKNTEEQLEIALAPY-------QHLEEDMKSLKQVLEMKNQQ---------IHEQEKKILELEKLAEKNIILEE 1274
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQerwlqdnltLRKRENELKEVEEELKQHLKEMG 1045
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1489865997 1275 KIQVLQQQNEDLKARIDQNTvVTRQLSEENANLQEYVEKETQEKKRLS 1322
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENIDL-IKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1232-1320 |
6.47e-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: 37.98 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1232 QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN----IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1307
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAeeeaERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEA 88
|
90
....*....|...
gi 1489865997 1308 QEYVEKETQEKKR 1320
Cdd:pfam20492 89 QEEIARLEEEVER 101
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1059-1115 |
6.73e-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: 40.82 E-value: 6.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489865997 1059 EVAFHtAKCEKLQKEKEELERRFEDEVK------RLGWQQQAELQELEERLQLQFEAEMARLQ 1115
Cdd:pfam15070 84 EQRLQ-EEAEQLQKELEALAGQLQAQVQdneqlsRLNQEQEQRLLELERAAERWGEQAEDRKQ 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1205-1328 |
6.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1205 LRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQ---- 1280
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllq 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1489865997 1281 -----QQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1328
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1033-1316 |
6.94e-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: 40.98 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1033 QHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRL-------------GWQQ-QAELQE 1098
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrdelngelsaadaAVAKdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1099 LEERLqLQFEAEMARLQEEHGDQLLSIRCQHQEQVE----------DLTASHDA--ALLEMENNHTVAitilqdDHDHKV 1166
Cdd:pfam12128 327 LEDQH-GAFLDADIETAAADQEQLPSWQSELENLEErlkaltgkhqDVTAKYNRrrSKIKEQNNRDIA------GIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1167 QELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALrknteEQLEIALAPYQHLEEDMKSLKQVLE 1246
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEA---GKLEFNEEEYRLKSRL-----GELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1489865997 1247 MKNQQIHEQEKKILELEKLAEKNIILE-------EKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQEYVEKETQ 1316
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHFLRKEAP 545
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
984-1328 |
7.79e-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: 40.73 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 984 KPDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELS-IELANIRDEVAF 1062
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSlKEKELAEEREKT 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1063 HTAKCEKLQK------EKEELERRFEDEVkrlgwqqQAELQELEERLQLQFEAEmarLQEEhgdqllsircQHQEQVEDL 1136
Cdd:pfam02463 784 EKLKVEEEKEeklkaqEEELRALEEELKE-------EAELLEEEQLLIEQEEKI---KEEE----------LEELALELK 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1137 TASHDAALLEMENNHTVAITILQDDHDHKVQELmsthelekkeLEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEAL 1216
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKE----------EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1217 RKNTEEQLEIAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVV 1296
Cdd:pfam02463 914 EKENEIEERIK----EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
330 340 350
....*....|....*....|....*....|..
gi 1489865997 1297 TRQLSEENANLQEyvEKETQEKKRLSRTNEEL 1328
Cdd:pfam02463 990 YNKDELEKERLEE--EKKKLIRAIIEETCQRL 1019
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
1068-1118 |
7.87e-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: 38.04 E-value: 7.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1489865997 1068 EKLQKEKEELERRFEDEVKRLG---WQQQAELQELEERLQLqfeAEMARLQEEH 1118
Cdd:pfam04696 44 EKAKQEKEELEERKREEREELFeerRAEQIELRALEEKLEL---KELMETWHEN 94
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
999-1116 |
8.49e-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: 39.12 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 999 RLKERCEQQTRQLGvaqgELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDevafhtaKCEKLQKEKEELE 1078
Cdd:pfam13851 58 RLTEPLQKAQEEVE----ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQ-------RFEKVERERDELY 126
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489865997 1079 RRFEDEVKRLgwQQQAELQE--LEERLQL---QFEAEMARLQE 1116
Cdd:pfam13851 127 DKFEAAIQDV--QQKTGLKNllLEKKLQAlgeTLEKKEAQLNE 167
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1090-1292 |
9.36e-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: 39.35 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1090 WQQ-QAELQELEERLQlqfEAEMARLQEEHGDqllsircqHQEQVEDLTASHDAALLEMENNHTVAitilqDDHDHKVQE 1168
Cdd:cd00176 2 LQQfLRDADELEAWLS---EKEELLSSTDYGD--------DLESVEALLKKHEALEAELAAHEERV-----EALNELGEQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489865997 1169 LMSTHELEKKELEENFEKLRL---SLQDQVDTLTFQSQSLRDRARRFEEA--LRKNTEEQLEIALA-PYQHLEEDMKSLK 1242
Cdd:cd00176 66 LIEEGHPDAEEIQERLEELNQrweELRELAEERRQRLEEALDLQQFFRDAddLEQWLEEKEAALASeDLGKDLESVEELL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1489865997 1243 QVLEMKNQQIHEQEKKILELEKLAEK---------NIILEEKIQVLQQQNEDLKARIDQ 1292
Cdd:cd00176 146 KKHKELEEELEAHEPRLKSLNELAEElleeghpdaDEEIEEKLEELNERWEELLELAEE 204
|
|
| FAM76 |
pfam16046 |
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ... |
1234-1307 |
9.45e-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: 39.77 E-value: 9.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489865997 1234 LEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDlkaRIDQNTVVTRQLSEENANL 1307
Cdd:pfam16046 227 LKEQIASLQKQLAQKDQQLLEKDKQITELKaKHFTKERELRNKMKTMEKEHED---KVEQLQIKIRSLLKEVATL 298
|
|
| |
