|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
990-1323 |
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 1860299437 990 AREAERQLV-LRLKERCEQQTRQLGVAQGELKRAicgfdaLAVATQHFFRKN-ESALVKEKELSIELANIRDEVAFHTAK 1067
Cdd:TIGR02168 195 LNELERQLKsLERQAEKAERYKELKAELRELELA------LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1068 CEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQ---EEHGDQLLSIRCQHQEQVEDLTAShDAA 1144
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELY-ALANEISRLEQQKQIL-RERLANLErqlEELEAQLEELESKLDELAEELAEL-EEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1145 LLEMENNHTVaitiLQDDHD--HKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1222
Cdd:TIGR02168 346 LEELKEELES----LEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1223 EQLEIALAPYQH-LEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDqntvVTRQL 1301
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD----SLERL 497
|
330 340
....*....|....*....|..
gi 1860299437 1302 SEENANLQEYVEKETQEKKRLS 1323
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1046-1329 |
1.34e-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: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1046 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLS 1125
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1126 IRCQHQEQVEDLTASHDAALLEMENNHTV---AITILQDDHD------HKVQELMSTHELEKKELEENFEKLRLSLQDQV 1196
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1197 DTLTFQSQSLRDrarrfEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEK 1276
Cdd:TIGR02168 852 EDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE---LREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 1277 IQVLQQQNEDLKARIDQNtvvTRQLSEEN-------ANLQEYVEKETQE-KKRLSRTNEEL 1329
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNL---QERLSEEYsltleeaEALENKIEDDEEEaRRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1329 |
2.22e-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: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1068
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1069 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1148
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALD-ELRAELTLLNEEAA-NLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1149 ENnHTVAITILQDDHDHKVQELMSThelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1228
Cdd:TIGR02168 862 EE-LEELIEELESELEALLNERASL------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1229 LApyqhleedmkslKQVLEMKNQQIHEQ--EKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVT-------R 1299
Cdd:TIGR02168 929 LR------------LEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyE 996
|
330 340 350
....*....|....*....|....*....|
gi 1860299437 1300 QLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1063-1328 |
5.30e-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: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1063 FHTAKCEKLQKEKEELERRFE--------DEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSiRCQHQEQV 1134
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVErrrkleeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE-RIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1135 EDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRlslQDQVDTLTFQSQSLRD-RARRF 1213
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEeRAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1214 EEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQ-IHEQEKKILELEKLAEKNIILEE--KIQVLQQQNEDLKA- 1289
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKa 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1860299437 1290 -------RIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 1328
Cdd:pfam17380 529 iyeeerrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1070-1330 |
2.25e-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: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1070 KLQKEKEELERR---FEDEVKRlgwQQQAELQELEERLQLQFEAEMARLQEEHGdQLLSIRCQHQEQVEDLTAshdaaLL 1146
Cdd:COG1196 217 ELKEELKELEAElllLKLRELE---AELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEE-----AQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1147 EMENNHTVAITILQDDHDHKVQELmsthelekKELEENFEKlrlsLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLE 1226
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERR--------RELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1227 IAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNtvvTRQLSEENA 1306
Cdd:COG1196 356 AE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL---EEELEELEE 428
|
250 260
....*....|....*....|....
gi 1860299437 1307 NLQEYVEKETQEKKRLSRTNEELL 1330
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1049-1329 |
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 1860299437 1049 ELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEdEVKRLGWQQQAELQELEERLQLQfEAEMARLQEEhgdqllsirc 1128
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISAL-RKDLARLEAE---------- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1129 qhQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRD 1208
Cdd:TIGR02168 742 --VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA----------------EAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1209 RARRFEEALRkNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLK 1288
Cdd:TIGR02168 804 ALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1860299437 1289 ARIDQNTVVTR-QLSEENANLQEyVEKETQEKKR-LSRTNEEL 1329
Cdd:TIGR02168 883 ASLEEALALLRsELEELSEELRE-LESKRSELRReLEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
989-1313 |
5.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAERQLVLRLKERcEQQTRQLGVAQGELKRAIcgfdalavatqhffRKNESALVKEKELSIELANIRDEVafhtakc 1068
Cdd:COG1196 219 KEELKELEAELLLLKL-RELEAELEELEAELEELE--------------AELEELEAELAELEAELEELRLEL------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1069 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 1148
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA-RLEQDIARLEERRR-ELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1149 EnnhtvaitILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 1228
Cdd:COG1196 354 E--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1229 LApyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1308
Cdd:COG1196 426 LE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
....*
gi 1860299437 1309 QEYVE 1313
Cdd:COG1196 504 EGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
991-1293 |
2.13e-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: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 991 REAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKElsiELANIRDEVAFHTAKCEK 1070
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1071 LQKEKEELERRFEDEvkrlGWQQ-QAELQELEE---RLQLQFEAEMARLQEEHGD-QLLSIRCQH-QEQVEDLTASHDAA 1144
Cdd:TIGR02169 777 LEEALNDLEARLSHS----RIPEiQAELSKLEEevsRIEARLREIEQKLNRLTLEkEYLEKEIQElQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1145 LLEMENNHTVAITILQ--DDHDHKVQELMSTHELEKKELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 1222
Cdd:TIGR02169 853 EKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1223 EQLEIALAPYQHLEE-----DMKSLKQVLEMKNQQIHEQE----KKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQ 1293
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIpeeelSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1046-1329 |
1.14e-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: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1046 KEKElsIELANIRDEVAFHTAKCEKLQKEKEELERRFEdevkrlgwQQQAELQELEERLQlQFEAEMARLQEEHgDQLLS 1125
Cdd:TIGR04523 366 EEKQ--NEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIK-KLQQEKELLEKEI-ERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1126 IRCQHQEQVEDLTaSHDAALLEMENNH--------------TVAITILQDDHDHKVQELMSTHELEKKELEENFEklrls 1191
Cdd:TIGR04523 434 TIIKNNSEIKDLT-NQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1192 LQDQVDTLTFQSQSLRDRARRFE-EALRKNTEeqleialapYQHLEEDMKSLKQVLEMKN--QQIHEQEKKILEL----E 1264
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLEsEKKEKESK---------ISDLEDELNKDDFELKKENleKEIDEKNKEIEELkqtqK 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299437 1265 KLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1042-1293 |
1.48e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1042 SALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFE--DEVKRLGWQQ------QAELQELEERL--------- 1104
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEidvasaEREIAELEAELerldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1105 --QLQF-----EAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMsthele 1177
Cdd:COG4913 687 laALEEqleelEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL------ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1178 kkeLEENFEKLRLSLQDQVDTltfqsqsLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM----KNQQI 1253
Cdd:COG4913 760 ---GDAVERELRENLEERIDA-------LRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALldrlEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1860299437 1254 HEQEKKILELEKLAEKNIIlEEKIQVLQQQNEDLKARIDQ 1293
Cdd:COG4913 830 PEYEERFKELLNENSIEFV-ADLLSKLRRAIREIKERIDP 868
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
987-1346 |
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 1860299437 987 DPQAREAER--QLVLRLKERCE-QQTRQLGVAQG--ELKRAICGFDALAVATQHFFRKNESALVKEKelsIELANIRDEV 1061
Cdd:pfam15921 422 DDRNMEVQRleALLKAMKSECQgQMERQMAAIQGknESLEKVSSLTAQLESTKEMLRKVVEELTAKK---MTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1062 AFHTAKCEklqkEKEELERRFEDEVKRLGWQQQAELQEL------EERLQ-LQFEAEMARLQEEHGDQLLSIRCQHQEQV 1134
Cdd:pfam15921 499 SDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELqhlkneGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1135 EDLTASH---------DAALLEMENN----HTVAITILQDDHDHKVQEL-------------MSTHELEKKELEENFEKL 1188
Cdd:pfam15921 575 TQLVGQHgrtagamqvEKAQLEKEINdrrlELQEFKILKDKKDAKIRELearvsdlelekvkLVNAGSERLRAVKDIKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1189 RLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEE----------QLEIALAPYQHLEEDMKSL--------KQVLEMKN 1250
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmetttnklkmQLKSAQSELEQTRNTLKSMegsdghamKVAMGMQK 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1251 Q------QIHEQEKKILELEKL-----AEKNIILEEK--------------------IQVLQQQNEDLKARIDQNTVVTR 1299
Cdd:pfam15921 735 QitakrgQIDALQSKIQFLEEAmtnanKEKHFLKEEKnklsqelstvateknkmageLEVLRSQERRLKEKVANMEVALD 814
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1860299437 1300 QLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSPIKLSP 1346
Cdd:pfam15921 815 KASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKP 861
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1001-1329 |
2.99e-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: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1001 LKERCEQQ---TRQLGVAQGELKRAICGFDAL----AVATQHFFRknesaLVKEKELSIELANIRDE------VAFHTAK 1067
Cdd:pfam05483 284 LKELIEKKdhlTKELEDIKMSLQRSMSTQKALeedlQIATKTICQ-----LTEEKEAQMEELNKAKAahsfvvTEFEATT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1068 C---EKLQKEKEELERRfEDEVKRLGWQQQAELQELEERLQLQF--EAEMARLQEEHGDQ--LLSIRCQHQEQVEDLTAS 1140
Cdd:pfam05483 359 CsleELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFKNnkEVELEELKKILAEDekLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1141 HD--AALLEMENNHT----VAITILQDDHDHKVQELMSTHELEKKELEENFEklrlsLQDQVDTLTFQSQSLRDRARRFE 1214
Cdd:pfam05483 438 EQelIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1215 EALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKI-LELEKLAEKNIILEEKIQVLQQQNEDL 1287
Cdd:pfam05483 513 LELKKhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1860299437 1288 KARIDQntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:pfam05483 593 ENKCNN---LKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
989-1329 |
3.03e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAE-RQLVLRLkERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEK--ELSIELANIRDEVAFHT 1065
Cdd:COG4717 84 EEKEEEyAELQEEL-EELEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1066 ---AKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQ------LQFEAEMARLQEEHGDqllsIRCQHQEQVED 1136
Cdd:COG4717 160 eleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEelqqrlAELEEELEEAQEELEE----LEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1137 LTASHDAALLEMENNHTVAITIlqddhdhkVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEA 1216
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAA--------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1217 LRKNTEEQLEIA-----LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQN----EDL 1287
Cdd:COG4717 308 QALPALEELEEEeleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1860299437 1288 KARIDQN----------TVVTRQLSEENANLQEYVEKETQE--KKRLSRTNEEL 1329
Cdd:COG4717 388 RAALEQAeeyqelkeelEELEEQLEELLGELEELLEALDEEelEEELEELEEEL 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1092-1335 |
5.62e-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: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1092 QQQAELQELEERLQlQFEAEMARLQEE--HGDQLLSircQHQEQVEDLTASHDAALLEMEnnhtvaitILQDDHDHKVQE 1169
Cdd:TIGR02169 671 SEPAELQRLRERLE-GLKRELSSLQSElrRIENRLD---ELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1170 LmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlAPYQHL-EEDMKSLKQVLEM 1248
Cdd:TIGR02169 739 L---------------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLsHSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1249 KNQQIHEQEKKILELE----KLAEKNIILEEKIQVLQQQNEDLKARIDQN---------------------TVVTRQLSE 1303
Cdd:TIGR02169 803 LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienlngkkeeleeeleelEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|..
gi 1860299437 1304 ENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1335
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1050-1335 |
8.04e-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: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1050 LSIELANIRDEVAFHTAKCEKLQKEKEELErrfedevKRLGWQQQA-ELQELEERLQLQfEAEMARLQEEhgdqlLSIRC 1128
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQE-------EQLKKQQLLkQLRARIEELRAQ-EAVLEETQER-----INRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1129 QHQEQVEdltasHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeLEENFEKLRLSLQDQVDTL-TFQSQSLR 1207
Cdd:TIGR00618 291 KAAPLAA-----HIKAVTQIEQQAQRIHTELQSKMRSRAKLLM---------KRAAHVKQQSSIEEQRRLLqTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1208 DRARRFEEALRKnteEQLEIALAPYQHLeedmKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDL 1287
Cdd:TIGR00618 357 IRDAHEVATSIR---EISCQQHTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860299437 1288 KARIdqntvvtrQLSEENANLQE-YVEKETQEKK-------RLSRTNEELLWKLQT 1335
Cdd:TIGR00618 430 KKQQ--------ELQQRYAELCAaAITCTAQCEKlekihlqESAQSLKEREQQLQT 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1006-1282 |
9.49e-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: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1006 EQQTR--QLGVAQGELKRA--ICGFDAL----AVATQHFFRKNESA-----LVKEKELSIE-------------LANIRD 1059
Cdd:COG3096 407 VQQTRaiQYQQAVQALEKAraLCGLPDLtpenAEDYLAAFRAKEQQateevLELEQKLSVAdaarrqfekayelVCKIAG 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1060 EV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQFEAEmaRLQEEHGdQLLSIRCQHQEQ 1133
Cdd:COG3096 487 EVersqAWQTAR---------ELLRRYRSQQALAQRLQQlrAQLAELEQRLRQQQNAE--RLLEEFC-QRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1134 VEDLTASHDAallemennhtvaitiLQDDHDHKVQElmsthelekkeleenFEKLRLSLQDQVDTLTFQSQSLRDRA--- 1210
Cdd:COG3096 555 LEELLAELEA---------------QLEELEEQAAE---------------AVEQRSELRQQLEQLRARIKELAARApaw 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1211 RRFEEALRKnTEEQLEIALAPYQHLEEDMkslKQVLEmknqqiHEQEKKILElEKLAEKNIILEEKIQVLQQ 1282
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 ... |
985-1329 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 985 KPDPQAREAERQLVlRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 1064
Cdd:pfam01576 212 KLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1065 TAKCEKLQKEKEELERRFEDEVKRLGWQQQaelqeleerLQLQFEAEMARLQ----EE---HGDQLLSIRCQHQEQVEDL 1137
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTLDTTAAQQE---------LRSKREQEVTELKkaleEEtrsHEAQLQEMRQKHTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1138 TASHDAA------------LLEMENNHTVA-ITILQD---DHDHK-------VQELMSTHELEkkeleenfEKLRLSLQD 1194
Cdd:pfam01576 362 TEQLEQAkrnkanlekakqALESENAELQAeLRTLQQakqDSEHKrkklegqLQELQARLSES--------ERQRAELAE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1195 QVDTLTFQSQSLRDRARRFEEALRKNTEE--QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILE-LEKLAEKNI 1271
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDvsSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEqLEEEEEAKR 513
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299437 1272 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKKRLSRTNEEL 1329
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRL 578
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1204-1334 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1204 QSLRDRARRFEEALRKNtEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ 1283
Cdd:COG1196 235 RELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEER 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 1284 NEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1334
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1335 |
2.39e-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: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1036 FFRKNESAL-------VKEKELSIELANIRDEVafhtakcEKLQKEKEELERrFEDEVKRL----GWQQQAELQELEERL 1104
Cdd:TIGR02169 168 FDRKKEKALeeleeveENIERLDLIIDEKRQQL-------ERLRREREKAER-YQALLKEKreyeGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1105 QlQFEAEMARLQEEhgdqllsircqhqeqVEDLTASHDAALLEMEnnhtvAITILQDDHDHKVQELMSTHELEKKELEEN 1184
Cdd:TIGR02169 240 E-AIERQLASLEEE---------------LEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1185 FEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE--EQLEIALAPYQ----HLEEDMKSLKQVLEMKNQqiheqek 1258
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERkrrdKLTEEYAELKEELEDLRA------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1259 kilELEKLAEKNIILEEKIQVLQQQNEDLKARI-------DQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLW 1331
Cdd:TIGR02169 372 ---ELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
....
gi 1860299437 1332 KLQT 1335
Cdd:TIGR02169 449 EIKK 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1048-1293 |
2.92e-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: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1048 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQEehgdQLLSIR 1127
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAAL-EAELAELEK----EIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1128 CQHQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLR 1207
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1208 DrarrfeealrknTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 1287
Cdd:COG4942 164 A------------LRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAE---LAAELAELQQEAEEL 225
|
....*.
gi 1860299437 1288 KARIDQ 1293
Cdd:COG4942 226 EALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1048-1327 |
3.07e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1048 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAE-LQELEERLqlqfeaemarlqEEHGDQLLSI 1126
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKL------------KKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1127 RCQHQEQVEDLtashdaaLLEMENNhtvaITILQDDHDhKVQELMStHELEKKELEENFEKLRLSLQDQVDTLTFQS-QS 1205
Cdd:PRK03918 523 KAEEYEKLKEK-------LIKLKGE----IKSLKKELE-KLEELKK-KLAELEKKLDELEEELAELLKELEELGFESvEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1206 LRDRARRFEEALR-----KNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILEL---------EKLAEKNI 1271
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyEELREEYL 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860299437 1272 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 1327
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1192-1326 |
7.95e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1192 LQDQVDTLTFQSQSLRDRARRFEEALRKN------TEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKkilELEK 1265
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQArseleqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE---ELEE 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 1266 LAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1326
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
998-1319 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 998 VLRLKERCEQQTRQLGVAQG-------ELKRAICGFDALAVATQHFFRKNESALvkeKELSIELANIRDEVAFHTAKCEK 1070
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQL---KIITMELQKKSSELEEMTKFKNN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1071 LQKEKEELERRFEDEVKRLGWQQQAElqELEERLQLQfEAEM-----ARLQEEHG--DQLLSIRCQHQ---EQVED---- 1136
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFE--KIAEELKGK-EQELifllqAREKEIHDleIQLTAIKTSEEhylKEVEDlkte 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1137 ----------LTASHDAALLEME------NNHTVAITILQDD--HDHKVQELMSTHELEKKELEENF----EKLRLSLQD 1194
Cdd:pfam05483 480 lekeklknieLTAHCDKLLLENKeltqeaSDMTLELKKHQEDiiNCKKQEERMLKQIENLEEKEMNLrdelESVREEFIQ 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1195 QVDTLTFQSQSLRDRARRFEEALRK-------------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL 1261
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKkekqmkilenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1262 ELE-KLAEKNIILEEKIQVLQQQNEDLK---ARIDQNTVVTRQLSEENANLQEYVEKETQEK 1319
Cdd:pfam05483 640 KLElELASAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHK 701
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
986-1337 |
1.09e-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: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 986 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1065
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1066 AKCEKLQKEKEELERR-----------------------FEDEVKRLGWQQQ---AELQELEERLQlQFEAEMARLQEEH 1119
Cdd:TIGR00618 494 ARLLELQEEPCPLCGScihpnparqdidnpgpltrrmqrGEQTYAQLETSEEdvyHQLTSERKQRA-SLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1120 gDQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEK----LRLSLQDQ 1195
Cdd:TIGR00618 573 -SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQelalKLTALHAL 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1196 VDTLTFQSQSLRDRARRFEEALRKnteEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniilee 1275
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELL---ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------ 722
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1276 kiqvLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKrlSRTNEELLWKLQTGD 1337
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 ... |
1067-1324 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1067 KCEKLQKEKEELERRFEDEVKRLGWQ---QQAELQEL-------EERLQL--------------------QFEAEMARLQ 1116
Cdd:pfam01576 198 KEEKGRQELEKAKRKLEGESTDLQEQiaeLQAQIAELraqlakkEEELQAalarleeetaqknnalkkirELEAQISELQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1117 E----------------------------EHGDQLLSIRCQHQ-----EQ--------VEDLTASHDAALLEMENNHTVA 1155
Cdd:pfam01576 278 EdleseraarnkaekqrrdlgeelealktELEDTLDTTAAQQElrskrEQevtelkkaLEEETRSHEAQLQEMRQKHTQA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1156 ITILQDDHDHkvqelmstheleKKELEENFEKLRLSLQDQVDTLTFQSQSLRdRARRFEEALRKNTEEQLEIALAPY--- 1232
Cdd:pfam01576 358 LEELTEQLEQ------------AKRNKANLEKAKQALESENAELQAELRTLQ-QAKQDSEHKRKKLEGQLQELQARLses 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1233 ----QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ-NEDLKARIDQNTVVtRQLSEENAN 1307
Cdd:pfam01576 425 erqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS---LESQLQDTQELlQEETRQKLNLSTRL-RQLEDERNS 500
|
330
....*....|....*..
gi 1860299437 1308 LQEYVEKETQEKKRLSR 1324
Cdd:pfam01576 501 LQEQLEEEEEAKRNVER 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1048-1329 |
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 1860299437 1048 KELSIELANIRDEVafhtakcEKLQKEKEELERRFE--DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlls 1125
Cdd:PRK03918 210 NEISSELPELREEL-------EKLEKEVKELEELKEeiEELEKELESLEGSKRKLEEKIR-ELEERIEELKKE------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1126 IRcQHQEQVEDLTAshdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTFQSQS 1205
Cdd:PRK03918 275 IE-ELEEKVKELKE------LKEKAEEYIKLSEFYEEYLDELREI---------------EKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1206 LRDRARRFEEALRKNTEEQLEIA-LAPYQHLEEDMKSLKQVLE-----MKNQQIHEQEKKILELEK----LAEKNIILEE 1275
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEeLEERHELYEEAKAKKEELErlkkrLTGLTPEKLEKELEELEKakeeIEEEISKITA 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 1276 KIQVLQQQNEDLKARIDQ-------NTVVTRQLSEENAnlQEYVEKETQEKKRLSRTNEEL 1329
Cdd:PRK03918 413 RIGELKKEIKELKKAIEElkkakgkCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEI 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1069-1311 |
1.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1069 EKLQKEKEELERRFedevKRLGWQQQAELQELEERLQlQFEAEMARLQEEHgDQLLSIRcqhqEQVEDLTAshdaallem 1148
Cdd:COG4717 49 ERLEKEADELFKPQ----GRKPELNLKELKELEEELK-EAEEKEEEYAELQ-EELEELE----EELEELEA--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1149 ennhtvAITILQDDHDhkvqelmsthelekkeleenfeklRLSLQDQVDTLTFQSQSLRDRARRFEEALrknteEQLEIA 1228
Cdd:COG4717 110 ------ELEELREELE------------------------KLEKLLQLLPLYQELEALEAELAELPERL-----EELEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1229 LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKK------------ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTV 1296
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LE 233
|
250
....*....|....*
gi 1860299437 1297 VTRQLSEENANLQEY 1311
Cdd:COG4717 234 NELEAAALEERLKEA 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
986-1327 |
1.70e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 986 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 1065
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1066 AKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQE--EHGDQLLSI-RCQHQEQ-VE 1135
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEdfleelREERDELREREA-ELEATLRTARErvEEAEALLEAgKCPECGQpVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1136 DltASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRARR 1212
Cdd:PRK02224 463 G--SPHVETI---------------EEDRERVEEL---------------EAELEDLEEEVEEVEErleRAEDLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1213 FEEAL--RKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDLKAR 1290
Cdd:PRK02224 511 IERLEerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE---AREEVAELNSKLAELKER 587
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1860299437 1291 IDQ-NTVVTR---------QLSEENANLQEYVEKETQEKKRLSRTNE 1327
Cdd:PRK02224 588 IESlERIRTLlaaiadaedEIERLREKREALAELNDERRERLAEKRE 634
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
936-1328 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 936 GTKKDAQKDQDTNKPAVSSpkRVAASTTKLHSpGYPKQRTAAARNGFPPKPDPQAREAErqlvlrLKERCEQQTRQLGVA 1015
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKE--QNNRDIAGIKD-KLAKIREARDRQLAVAEDDLQALESE------LREQLEAGKLEFNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1016 QGELKRAICGFDALAVATQHffrknESALVKEKELSIELAN-IRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG---- 1090
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQATA-----TPELLLQLENFDERIErAREEQEAANAEVERLQSELRQARKRRDQASEALRqasr 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1091 --WQQQAELQELEERLQ------LQFEAEMARLQEEHGDQLLSIRCQHQeqvEDLTASHDAALLEMENN-HTVAITILQD 1161
Cdd:pfam12128 514 rlEERQSALDELELQLFpqagtlLHFLRKEAPDWEQSIGKVISPELLHR---TDLDPEVWDGSVGGELNlYGVKLDLKRI 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1162 DHDHKVQelmsthelekkeleeNFEKLRLSLqDQVDTlTFQSQslRDRARRFEEAL---RKNTEEQ---LEIALAPYQHL 1235
Cdd:pfam12128 591 DVPEWAA---------------SEEELRERL-DKAEE-ALQSA--REKQAAAEEQLvqaNGELEKAsreETFARTALKNA 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1236 EEDMKSL---KQVLEMK-NQQIHE-QEKKILELEKL-AEKNIILEEKIQVLQQQNEDLK----ARIDQNTVVTRQLSEEN 1305
Cdd:pfam12128 652 RLDLRRLfdeKQSEKDKkNKALAErKDSANERLNSLeAQLKQLDKKHQAWLEEQKEQKReartEKQAYWQVVEGALDAQL 731
|
410 420
....*....|....*....|....
gi 1860299437 1306 ANLQEYVEK-ETQEKKRLSRTNEE 1328
Cdd:pfam12128 732 ALLKAAIAArRSGAKAELKALETW 755
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
989-1290 |
2.11e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAErQLVLRLKERC--------EQQTR--QLGVAQGELKRA--ICGFDALAV----ATQHFFRKNESALVK-----E 1047
Cdd:PRK04863 384 RAEAAE-EEVDELKSQLadyqqaldVQQTRaiQYQQAVQALERAkqLCGLPDLTAdnaeDWLEEFQAKEQEATEellslE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1048 KELSIE-------------LANIRDEV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQF 1108
Cdd:PRK04863 463 QKLSVAqaahsqfeqayqlVRKIAGEVsrseAWDVAR---------ELLRRLREQRHLAEQLQQlrMRLSELEQRLRQQQ 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1109 EAEmaRLQEEHGdQLLSIRCQHQEQVEDLTASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKL 1188
Cdd:PRK04863 534 RAE--RLLAEFC-KRLGKNLDDEDELEQLQEELEARL---------------ESLSESVSEA---------------RER 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1189 RLSLQDQVDTLTFQSQSLRDRARRFEEAlrKNTEEQLeialapYQHLEEDMKSLKQVLE-MKNQQIHEQEkkilelekLA 1267
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAA--QDALARL------REQSGEEFEDSQDVTEyMQQLLERERE--------LT 644
|
330 340
....*....|....*....|...
gi 1860299437 1268 EKNIILEEKIQVLQQQNEDLKAR 1290
Cdd:PRK04863 645 VERDELAARKQALDEEIERLSQP 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1078-1306 |
2.93e-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: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1078 LERRFEDEVKRLGWQQQaELQELEERLQlQFEAEMARLQEEHG------------DQLLSIRCQH---QEQVEDLTASHD 1142
Cdd:COG3206 166 LELRREEARKALEFLEE-QLPELRKELE-EAEAALEEFRQKNGlvdlseeaklllQQLSELESQLaeaRAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1143 AALLEMENNHTVAITILQDDhdhKVQELMSthelekkeleeNFEKLRLSLQDQVDTLTFQS---QSLRDRARRFEEALRK 1219
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSP---VIQQLRA-----------QLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1220 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTVVTR 1299
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-ARLAE 381
|
....*..
gi 1860299437 1300 QLSEENA 1306
Cdd:COG3206 382 ALTVGNV 388
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1037-1318 |
2.98e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1037 FRKNESALVKEKELSIELANIRDEVAFHTAkcEKLQKEKEELE------RRFEDEVKRLGwQQQAELQELEERLQLqFEA 1110
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEklkeklIKLKGEIKSLK-KELEKLEELKKKLAE-LEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1111 EMARLQEEHGDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleENFEKLRL 1190
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREE-------------KELKKLEE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1191 SLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN 1270
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEE-------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1860299437 1271 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQE 1318
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1220-1334 |
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 1860299437 1220 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKIlELEKLAEKNiiLEEKIQVLQQQNEDLKARIDQNTVVTR 1299
Cdd:pfam09744 33 NVLELLESLASRNQEHNVELEELREDNE---QLETQYEREK-ALRKRAEEE--LEEIEDQWEQETKDLLSQVESLEEENR 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1860299437 1300 QLSEENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 1334
Cdd:pfam09744 107 RLEADHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1048-1340 |
3.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1048 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQlQFEAEMARLQEEHG- 1120
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeleslQEEAEELQEELE-ELQKERQDLEQQRKq 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1121 -----DQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQ 1195
Cdd:COG4372 134 leaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1196 VDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM--KNQQIHEQEKKILELEKLAEKNIIL 1273
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299437 1274 EEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTS 1340
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1039-1329 |
4.61e-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: 48.09 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1039 KNESALVKEKELSIE--LANIRDEvafHTAKCEKLQ--KEKEELERRFEDEVKRLGwQQQAELQELEERLQLQFEAEMAR 1114
Cdd:TIGR04523 172 ENELNLLEKEKLNIQknIDKIKNK---LLKLELLLSnlKKKIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1115 LQEEHgDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVaITILQDDhdhkVQELMSthelekkeleenfEKLRLSLQD 1194
Cdd:TIGR04523 248 ISNTQ-TQLNQLKDEQNKIKKQL----SEKQKELEQNNKK-IKELEKQ----LNQLKS-------------EISDLNNQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1195 QVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlapyqHLEEDMKSLKQV---LEMKNQQIHEQ-EKKILELEKLAEKN 1270
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----QLNEQISQLKKEltnSESENSEKQRElEEKQNEIEKLKKEN 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860299437 1271 IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
999-1332 |
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 1860299437 999 LRLKERCEQQTRQLGVAQgelKRAI----CGFDALAVATQHFFRKNESaLVKEKELSIELANIRDEVAFHTA-KCEKLQK 1073
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQ---RKAIqelqFENEKVSLKLEEEIQENKD-LIKENNATRHLCNLLKETCARSAeKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1074 EKEELERRFEDevkrlgwqqqaeLQELEERLQLQFEAemARLQEEHgdqllsircqhqeqvedltashdaALLEMENNht 1153
Cdd:pfam05483 177 EREETRQVYMD------------LNNNIEKMILAFEE--LRVQAEN------------------------ARLEMHFK-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1154 vaitiLQDDHDhKVQELMSTHELEKKELEENFEKLRLSL---QDQVDTLTFQSQSLRDRARRFEEA-------LRKNTEE 1223
Cdd:pfam05483 217 -----LKEDHE-KIQHLEEEYKKEINDKEKQVSLLLIQItekENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1224 Q-------------LEIALAPYQHLEEDM----KSLKQVLEMKNQQIHEQEK----KILELEKLAEKNIILEEKIQVLQQ 1282
Cdd:pfam05483 291 KdhltkeledikmsLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKakaaHSFVVTEFEATTCSLEELLRTEQQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860299437 1283 QnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELLWK 1332
Cdd:pfam05483 371 R---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDE 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1290 |
7.77e-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: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1065 TAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQL------QFEAEMARLQEEHGD---QLLSIRCQ 1129
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKkeekalLKQLAALERRIAAlarrirALEQELAALEAELAElekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1130 HQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLRDR 1209
Cdd:COG4942 99 LEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1210 ARRFEEAlRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDLKA 1289
Cdd:COG4942 166 RAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAE 241
|
.
gi 1860299437 1290 R 1290
Cdd:COG4942 242 R 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
987-1328 |
8.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 987 DPQAREAERQL--VLRLKERCEQQTRQLGVAQGELKRAICGFDALAVAT-QHFFRKNESALVKEKELSIELANIRDEVAF 1063
Cdd:COG4717 145 PERLEELEERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1064 HTAKCEKLQKEKE--ELERRFEDE--------------------------------------VKRLGWQQQAELQELEER 1103
Cdd:COG4717 225 LEEELEQLENELEaaALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1104 LQLQFEAEMARLQEEHGDQLLSIR----CQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELM-STHELEK 1178
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLaEAGVEDE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1179 KELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEMKNQQIHEQEK 1258
Cdd:COG4717 385 EELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL---EELEEELEELEEELEELREELAELEA 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299437 1259 KILELEKlaekniilEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQ---EYVEKETQ--EKKRLSRTNEE 1328
Cdd:COG4717 461 ELEQLEE--------DGELAELLQELEELKAEL-------RELAEEWAALKlalELLEEAREeyREERLPPVLER 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1202-1329 |
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 1860299437 1202 QSQSLRDRARRFEEALRKNTEE---QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNII---LE 1274
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEeKLEELRLEvseLE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860299437 1275 EKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQ-EYVEKETQ---EKKRLSRTNEEL 1329
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQleeLESKLDELAEEL 339
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
640-993 |
1.38e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 640 VRPKIITYIRrNPQALGQVDASLVPVGLPYAPPTCT----------MPLPHEEKAAGGDLKPSAnlyekfKPDLQKPRVf 709
Cdd:PHA03247 2529 VHPRMLTWIR-GLEELASDDAGDPPPPLPPAAPPAApdrsvppprpAPRPSEPAVTSRARRPDA------PPQSARPRA- 2600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 710 ssglmvsGIKPPGHPFSQMSEKflqevtdhpgkeefCSPPYAHYEVPPTFYRSAMLLKPQLGLGAMSRLP------SAKS 783
Cdd:PHA03247 2601 -------PVDDRGDPRGPAPPS--------------PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPerprddPAPG 2659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 784 RIliASQRSSASAIHPPGPitTATSLYSSDPSADLKKASSSNAAKSNLPKSGLRPPGYSRLPAAKLaafgfvrsssvsSV 863
Cdd:PHA03247 2660 RV--SRPRRARRLGRAAQA--SSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPL------------PP 2723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 864 SSTQSGDSAQPEQGRPATRSTFGNEEQPVLKASLPSKDTPKGAGRVAPPASSSVTAPRRslLPAPKSTSTPAGTKKDAQK 943
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSP 2801
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1860299437 944 DQDTNKPAVSSPKRVAASTTKLHSPGYPKQRTAAARNGFPPKPDPQAREA 993
Cdd:PHA03247 2802 WDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1214-1343 |
1.81e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1214 EEALRKNTEEQLEialapyQHLEEDMKSLKQV-----------LEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQ 1282
Cdd:PHA02562 108 ESASSKDFQKYFE------QMLGMNYKSFKQIvvlgtagyvpfMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQ 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299437 1283 QNEDLKARID--------QNTVVTRQLSEENANLQEY-------VEKETQEKKRLSRTNEELL-WKLQTGDPTSPIK 1343
Cdd:PHA02562 182 QIQTLDMKIDhiqqqiktYNKNIEEQRKKNGENIARKqnkydelVEEAKTIKAEIEELTDELLnLVMDIEDPSAALN 258
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
524-932 |
1.83e-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: 46.06 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 524 ARADSVLNIPAPLHPET--TVNMTYQPTTPSSSFQDVSVFGMDAGSPLVVPPPtdSARLLNTSPKVPDKNTCPSGIPKPV 601
Cdd:pfam05109 440 AAPNTTTGLPSSTHVPTnlTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSP--SPRDNGTESKAPDMTSPTSAVTTPT 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 602 FTHSKDTPSSQEGMENYQVEKTEERTETKPIIMPKPKHVRPkiityirrNPQALGQVDASLVPVGLPYAPPTC-TMPLPH 680
Cdd:pfam05109 518 PNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP--------TPAVTTPTPNATIPTLGKTSPTSAvTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 681 EEKAAGGDLKPSANLYEKFKPDLQKPRVFSSglmvsgikPPGHPFSQMSEkflqevtdhpGKEEFCSPPYAHYEVPPTFY 760
Cdd:pfam05109 590 ATSPTVGETSPQANTTNHTLGGTSSTPVVTS--------PPKNATSAVTT----------GQHNITSSSTSSMSLRPSSI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 761 RSAmlLKPQLGLGAMSRLPSAKS----------RILIASQRSSASAIHPPGPITTATSlYSSDP--SADLKKASSSNAAK 828
Cdd:pfam05109 652 SET--LSPSTSDNSTSHMPLLTSahptggenitQVTPASTSTHHVSTSSPAPRPGTTS-QASGPgnSSTSTKPGEVNVTK 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 829 SNLPKSGLRPpgysRLPAAKLAAFGFVrSSSVSSVSSTQSGDSAQPEQGRPATRST--FGNEEQpvlkaslpSKDTPKGA 906
Cdd:pfam05109 729 GTPPKNATSP----QAPSGQKTAVPTV-TSTGGKANSTTGGKHTTGHGARTSTEPTtdYGGDST--------TPRTRYNA 795
|
410 420
....*....|....*....|....*.
gi 1860299437 907 GRVAPPASSSVTAPRRSLLPAPKSTS 932
Cdd:pfam05109 796 TTYLPPSTSSKLRPRWTFTSPPVTTA 821
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1220-1326 |
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 1860299437 1220 NTEEQLEIALAPYQHLEEDMKSLKQVL-----EMKNQQIHEQEKKILEL-EKLAEKNIILEEKiQVLQQQNEDLKARIDQ 1293
Cdd:PRK11281 198 QAEQALLNAQNDLQRKSLEGNTQLQDLlqkqrDYLTARIQRLEHQLQLLqEAINSKRLTLSEK-TVQEAQSQDEAARIQA 276
|
90 100 110
....*....|....*....|....*....|...
gi 1860299437 1294 NTVVTRQLsEENANLQEYVEKETQEKKRLSRTN 1326
Cdd:PRK11281 277 NPLVAQEL-EINLQLSQRLLKATEKLNTLTQQN 308
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1065-1325 |
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 1860299437 1065 TAKCEKLQKEKEELeRRFEDEVKRL---GWQQQAELQ----EL------EERLQLQFE--------AEMARLQEEHGDQ- 1122
Cdd:pfam07111 62 SQQAELISRQLQEL-RRLEEEVRLLretSLQQKMRLEaqamELdalavaEKAGQAEAEglraalagAEMVRKNLEEGSQr 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1123 -LLSIRCQHQEQVEDLTASHDAALLEMENNHT---VAITILQDDHDHKVQELmSTHELEKKELEENFEKLRLSLQDQVdT 1198
Cdd:pfam07111 141 eLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEgleKSLNSLETKRAGEAKQL-AEAQKEAELLRKQLSKTQEELEAQV-T 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1199 LTfqsQSLRDRA--RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLE-----------MKNQQIHEQEKKI----- 1260
Cdd:pfam07111 219 LV---ESLRKYVgeQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVEllqvrvqslthMLALQEEELTRKIqpsds 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860299437 1261 LELEKLAEKNIIL---EEKIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRT 1325
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 ... |
1066-1329 |
2.87e-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: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1066 AKCEKLQKEKE----------ELERRF---EDEVKRLGWQQQAEL-----------------QELEERLQlqfeaEM-AR 1114
Cdd:pfam01576 9 AKEEELQKVKErqqkaeselkELEKKHqqlCEEKNALQEQLQAETelcaeaeemrarlaarkQELEEILH-----ELeSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1115 LQEEH--GDQLLSIRCQHQEQVEDLTAShdaalLEMENNHTVAITILQDDHDHKVQELmsthelekkeleenfEKLRLSL 1192
Cdd:pfam01576 84 LEEEEerSQQLQNEKKKMQQHIQDLEEQ-----LDEEEAARQKLQLEKVTTEAKIKKL---------------EEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1193 QDQVDTLTFQSQSLRDRARRFEEALRKntEEQLEIALAPYQHLEEDMKSLKQVlemknqQIHEQEKKILELEKLAEKnii 1272
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAE--EEEKAKSLSKLKNKHEAMISDLEE------RLKKEEKGRQELEKAKRK--- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299437 1273 LEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1204-1328 |
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 1860299437 1204 QSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEmknQQIHEQEKKILELEK-LAEKNIILEEKIQVLQQ 1282
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFE---KELRERRNELQKLEKrLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1860299437 1283 QNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR-TNEE 1328
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEE 154
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1186-1330 |
3.36e-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: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1186 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALA------PYQHLEEDMKSLKQVLEMKNQQIHEQEKK 1259
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1260 ILEL-EKLAEkniiLEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEELL 1330
Cdd:TIGR02168 332 LDELaEELAE----LEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVAQLELQIAS 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1046-1310 |
3.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1046 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG--WQQQAELQELEERLQLQFE--AEMARLQEEHGD 1121
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEAEIEDLREtiAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1122 QLLSircqHQEQVEDLtashdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDqvdtLTF 1201
Cdd:PRK02224 280 EVRD----LRERLEEL---------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----HNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1202 QSQSLRDRARRFEEALRKNTEEQLEialapyqhLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNII----LEEKI 1277
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnAEDFL 414
|
250 260 270
....*....|....*....|....*....|....*.
gi 1860299437 1278 QVLQQQNEDLKARIDQNTVVTRQLS---EENANLQE 1310
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARervEEAEALLE 450
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1043-1328 |
4.15e-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: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1043 ALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLgwQQQAELQE-LEERLQLQFEAEMARLQEehGD 1121
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK--RYRQELEEqIEEREQKRQEEYEEKLQE--RE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1122 QLLSIrcQHQEQVEDltashdaaLLEMENNHtvaitilqddhdhkvqelmsthelekkeleenfeKLRLSLQDQVDtltf 1201
Cdd:pfam13868 102 QMDEI--VERIQEED--------QAEAEEKL----------------------------------EKQRQLREEID---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1202 qsqslrdrarRFEEALRKNTEEQLEialapyQHLEEDMKsLKQVLEMKNQQIHEQEKKILELEKLAEKNIileEKIQVLQ 1281
Cdd:pfam13868 134 ----------EFNEEQAEWKELEKE------EEREEDER-ILEYLKEKAEREEEREAEREEIEEEKEREI---ARLRAQQ 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1282 QQNEDLKARIDQntVVTRQLSEENANLQEYVEKETQEKKR-----LSRTNEE 1328
Cdd:pfam13868 194 EKAQDEKAERDE--LRAKLYQEEQERKERQKEREEAEKKArqrqeLQQAREE 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1186-1329 |
4.44e-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: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1186 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapyQHLEEDMKSLKQVLEMKNQQIH------EQEKK 1259
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------KRLELEIEEVEARIKKYEEQLGnvrnnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1260 ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQeyvEKETQEKKRLSRTNEEL 1329
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 ... |
1245-1335 |
4.50e-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: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1245 VLEMKNQQIHEQEKKILELEKlaeKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1324
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90
....*....|.
gi 1860299437 1325 TNEELLWKLQT 1335
Cdd:TIGR04523 282 KIKELEKQLNQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1092-1329 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1092 QQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTAshdaallemennhtvAITILQDDHDHKVQELm 1171
Cdd:COG4942 24 EAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLA-ALERRIAALAR---------------RIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1172 sthelekkeleenfeklrLSLQDQVDTLTFQSQSLRDR-ARRFEEALRKNTEEQLEIALAP--YQHLEEDMKSLKQVLEM 1248
Cdd:COG4942 86 ------------------AELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1249 KNQQIHEQEKKILELEKLAEKNIILEEKIQVL----QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1324
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
....*
gi 1860299437 1325 TNEEL 1329
Cdd:COG4942 228 LIARL 232
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1237-1334 |
5.04e-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: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1237 EDMKSLK-QVLEMKNQQIH--------EQEKKIL--ELEKLAEKNIILEEKIQVLQQQNEDL---KARIDQNTVVTRQLS 1302
Cdd:pfam13851 26 ELIKSLKeEIAELKKKEERneklmseiQQENKRLtePLQKAQEEVEELRKQLENYEKDKQSLknlKARLKVLEKELKDLK 105
|
90 100 110
....*....|....*....|....*....|..
gi 1860299437 1303 EENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1334
Cdd:pfam13851 106 WEHEVLEQRFEKVERERDELYDKFEAAIQDVQ 137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1310 |
7.00e-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: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1026 FDALAVATQHF--FRKNESALVKEKElSIE-LANIRdevafhtAKCEKLQKEKEELERrFEDEVKRLG-WQQQAELQELE 1101
Cdd:COG4913 224 FEAADALVEHFddLERAHEALEDARE-QIElLEPIR-------ELAERYAAARERLAE-LEYLRAALRlWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1102 ERLQlQFEAEMARLQEehgdqllsircqhqeQVEDLTASHDAA---LLEMENnhtvaiTILQDDHDhkvqelmsthelek 1178
Cdd:COG4913 295 AELE-ELRAELARLEA---------------ELERLEARLDALreeLDELEA------QIRGNGGD-------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1179 keleenfeklRL-SLQDQVDTLTFQSQSLRDRARRFEEALRK------NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQ 1251
Cdd:COG4913 339 ----------RLeQLEREIERLERELEERERRRARLEALLAAlglplpASAEEFAALRAEAAALLEALEEELEALE---E 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860299437 1252 QIHEQEKKILELEKLAEKniiLEEKIQVLQQQnedlKARIDQNTVVTRQLSEENANLQE 1310
Cdd:COG4913 406 ALAEAEAALRDLRRELRE---LEAEIASLERR----KSNIPARLLALRDALAEALGLDE 457
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
835-1071 |
9.68e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 43.52 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 835 GLRPPGYSRLPAAKLAAFGFVRSSSVSSVSSTQSGDSAQPEQGRPATRSTfgnEEQPvlKASLPSKDTPKGAGRVAPPAS 914
Cdd:PRK14959 377 GASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAP--SPRVPWDDAPPAPPRSGIPPR 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 915 SSVTAPRRSLLP-APKSTSTPAGTkkdaqkdqdtnkpavsSPKRVAASTTKLHSPGYPKQ-----RTAAARNGFPPKPDP 988
Cdd:PRK14959 452 PAPRMPEASPVPgAPDSVASASDA----------------PPTLGDPSDTAEHTPSGPRTwdgflEFCQGRNGQGGRLAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAERQL---VLRLKERCEQQTRQLGVAQGE-----LKRAICGFDA-LAVATQHFFRKNESALVKEKELSIELANIRD 1059
Cdd:PRK14959 516 VLRQATPEHadgRLRLATMSSVQYERLTDAATEttlagLVRDYFGDACrVEVLPPTRVRRTEAELRKEAEAHPAVQLLKE 595
|
250
....*....|..
gi 1860299437 1060 EVAFHTAKCEKL 1071
Cdd:PRK14959 596 EMGACILKCTPL 607
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
1263-1334 |
9.75e-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: 9.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1263 LEKLAEKNIILEEKIQVLQQQNEDLKARidqntvvTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1334
Cdd:pfam06005 6 LEQLETKIQAAVDTIALLQMENEELKEE-------NEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1071-1329 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1071 LQKEKEELERR-FEDEvkrlgwQQQAELQEleERLQLQfeAEMARLQE-----EHGDQLLSIRC----QHQEQVEDLTAS 1140
Cdd:pfam05622 5 AQEEKDELAQRcHELD------QQVSLLQE--EKNSLQ--QENKKLQErldqlESGDDSGTPGGkkylLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1141 hdaaLLEMENNhtvaitilQDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVDTLTF---QSQSLRDRArrfeEAL 1217
Cdd:pfam05622 75 ----NFRLETA--------RDDYRIKCEEL---------------EKEVLELQHRNEELTSlaeEAQALKDEM----DIL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1218 RKNTEE--QLEIALAPYQHLEEDMKSLK-QV--LEMKNQqIHEQEKkiLELEKLAEKNIILEEKIQVLQQQNEDLKARID 1292
Cdd:pfam05622 124 RESSDKvkKLEATVETYKKKLEDLGDLRrQVklLEERNA-EYMQRT--LQLEEELKKANALRGQLETYKRQVQELHGKLS 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1860299437 1293 QNTVVTRQLSEENANLQEYVEKETQEKKRLS-------RTNEEL 1329
Cdd:pfam05622 201 EESKKADKLEFEYKKLEEKLEALQKEKERLIierdtlrETNEEL 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1067-1322 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1067 KCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQF-------EAEMARLQEEHGdqllsiRCQhqEQVEDLTA 1139
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIndrirllEQEVARYKEESG------KAQ--AEVERLLG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1140 shdaALLEMENNhtvaitilQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALRK 1219
Cdd:pfam10174 587 ----ILREVENE--------KNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK---GAQLLEEARRREDNLADN 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1220 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEklAEKNIILEEkiqVLQQQNEDLKARI---DQNTV 1296
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR--AERRKQLEE---ILEMKQEALLAAIsekDANIA 726
|
250 260
....*....|....*....|....*.
gi 1860299437 1297 VTRQLSEENANLQEYVEKETQEKKRL 1322
Cdd:pfam10174 727 LLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1070-1313 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1070 KLQKEKEELERRF----------EDEVKRLGW---QQQAELQELEERLQ-------------LQFEAEMARLQEEHGD-- 1121
Cdd:pfam01576 149 KLSKERKLLEERIseftsnlaeeEEKAKSLSKlknKHEAMISDLEERLKkeekgrqelekakRKLEGESTDLQEQIAElq 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1122 -QLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQ-DDHDHKVQELMSTHELEKKELEEN-------FEKLRLSL 1192
Cdd:pfam01576 229 aQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAEKQrrdlgeeLEALKTEL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1193 QDQVDTLTFQsQSLRDRARRFEEALRKNTEEQLEIALAPYQHLE--------------EDMKSLKQVLEmKNQQIHEQEK 1258
Cdd:pfam01576 309 EDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMRqkhtqaleelteqlEQAKRNKANLE-KAKQALESEN 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299437 1259 KIL--ELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE 1313
Cdd:pfam01576 387 AELqaELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1186-1330 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1186 EKLRLSLQDQVDTLTFQSQSLRDRARRFE------EALRKNTEEQLEIALAP--YQHLEEDMKSLKQvlemknqQIHEQE 1257
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLEleieevEARIKKYEEQLGNVRNNkeYEALQKEIESLKR-------RISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299437 1258 KKILEL-EKLAEKNIILEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRT-NEELL 1330
Cdd:COG1579 110 DEILELmERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEELEAEREELAAKiPPELL 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1209-1329 |
1.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1209 RARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDL 1287
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEeELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1860299437 1288 KARIDQNTVVTRQL---SEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:COG4372 90 QAAQAELAQAQEELeslQEEAEELQEELEELQKERQDLEQQRKQL 134
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1039-1289 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1039 KNESALVKEKE-LSIELANIRDEVAFHTAKCEKLQKEKEELERRFED---EVKRLGWQQQAELQ---------------- 1098
Cdd:TIGR02169 230 KEKEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGEEEQLRVKekigeleaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1099 --ELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQddhdhKVQELMSTHEL 1176
Cdd:TIGR02169 310 iaEKERELE-DAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRA-----ELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1177 EKKELEENFEKL------RLSLQDQVDTLTFQSQSLRDRARRFEEAL-----RKN------TEEQLEIALAPYQ--HLEE 1237
Cdd:TIGR02169 383 TRDELKDYREKLeklkreINELKRELDRLQEELQRLSEELADLNAAIagieaKINeleeekEDKALEIKKQEWKleQLAA 462
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1238 DMKSLKQVLEMKNQQIHEQEKkilELEKLAEKNIILEEKIQVLQQQNEDLKA 1289
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
989-1309 |
1.57e-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: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 989 QAREAERQLvlrlKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALV----KEKELSIELANIRDEVAFH 1064
Cdd:pfam15921 332 ELREAKRMY----EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1065 TAKCEKLQKEKEELERRfEDEVKRLgwqqQAELQELEERLQLQFEAEMARLQEEHgdqllsircQHQEQVEDLTAshdaa 1144
Cdd:pfam15921 408 TGNSITIDHLRRELDDR-NMEVQRL----EALLKAMKSECQGQMERQMAAIQGKN---------ESLEKVSSLTA----- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1145 llEMENNHTVAitilqddhdHKVQELMSTHELEKKELEENFEKLRLSLQDQ---VDTLTFQSQSLRDRARRFEEALR--K 1219
Cdd:pfam15921 469 --QLESTKEML---------RKVVEELTAKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLRSRVDLKLQELQhlK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1220 NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAekNIILEEKIQVLQQQN------EDLKARIDQ 1293
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTA--GAMQVEKAQLEKEINdrrlelQEFKILKDK 615
|
330
....*....|....*.
gi 1860299437 1294 NTVVTRQLSEENANLQ 1309
Cdd:pfam15921 616 KDAKIRELEARVSDLE 631
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1211-1335 |
1.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1211 RRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKIL----ELEKLAEKNIILEEKIQVLQQQNED 1286
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEqarsELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1860299437 1287 LKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1335
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1048-1124 |
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 1860299437 1048 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQfEAEMARLQEEHgDQLL 1124
Cdd:cd22887 7 QELEKRLAELEAELASLEEEIKDLEEELKEKNKANEI--------LNDELIALQIENNLL-EEKLRKLQEEN-DELV 73
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1228 |
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 1860299437 989 QAREAERQLVLRLKERCEQQtrqLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 1068
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQ---KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1069 EKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSIRCQHQEQVEDLTASHDAALLEM 1148
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1149 E-NNHTVAITILQDDHDHKVQELMSTHELEKKEleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFE---EALRKNTEEQ 1224
Cdd:TIGR02168 441 ElEELEEELEELQEELERLEEALEELREELEEA-----EQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQ 515
|
....
gi 1860299437 1225 LEIA 1228
Cdd:TIGR02168 516 SGLS 519
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
993-1311 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 993 AERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQ 1072
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1073 KEKEELERRFEDEVKRlgwqQQAELQELEERLqlqfeaemarlqeehgDQLLSIRCQHQEQVEDltaSHDAALLEMENNH 1152
Cdd:TIGR00606 923 QEKEELISSKETSNKK----AQDKVNDIKEKV----------------KNIHGYMKDIENKIQD---GKDDYLKQKETEL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1153 TVAITILQDDHDHKvqelmsthelekkeleENFEK-LRLSLQDqvdtltFQSQSLRDRARRFEEALRKNTEEQLEIALAP 1231
Cdd:TIGR00606 980 NTVNAQLEECEKHQ----------------EKINEdMRLMRQD------IDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1232 YQHLEE-------DMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKiQVLQQQNEDLKARIDQNTVVTRQLSEE 1304
Cdd:TIGR00606 1038 KQHLKEmgqmqvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK-ELREPQFRDAEEKYREMMIVMRTTELV 1116
|
....*..
gi 1860299437 1305 NANLQEY 1311
Cdd:TIGR00606 1117 NKDLDIY 1123
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1215-1308 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1215 EALRKNTEEQ------LEIALAPYQHLEEDMKSLK---QVLEMKNQQIHE--------QEKKILEL-EKLAEKNIILEEK 1276
Cdd:pfam13851 71 EELRKQLENYekdkqsLKNLKARLKVLEKELKDLKwehEVLEQRFEKVERerdelydkFEAAIQDVqQKTGLKNLLLEKK 150
|
90 100 110
....*....|....*....|....*....|....
gi 1860299437 1277 IQVLQqqnEDLKARidqntvvTRQLSE--ENANL 1308
Cdd:pfam13851 151 LQALG---ETLEKK-------EAQLNEvlAAANL 174
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
989-1255 |
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 1860299437 989 QAREAERQLVLRLKERCEQQTR----QLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 1064
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLYEKEIEdlrrQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1065 T-------AKCEKLQKEKEELERRFEDEVKrlgwqqqaELQELEERLQLQFEAEMARLQEEhgDQLLS-IRCQHQEQVED 1136
Cdd:pfam00038 116 TlarvdleAKIESLKEELAFLKKNHEEEVR--------ELQAQVSDTQVNVEMDAARKLDL--TSALAeIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1137 LTAshdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKeleenfeklrlsLQDQVDTLTFQSQSLRDRARRFEEA 1216
Cdd:pfam00038 186 NRE-------EAEEWYQSKLEELQQAAARNGDALRSAKEEITE------------LRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1860299437 1217 LRKnTEEQLEIALAPYQ----HLEEDMKSLKQVLEMKNQQIHE 1255
Cdd:pfam00038 247 LAE-TEERYELQLADYQelisELEAELQETRQEMARQLREYQE 288
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
1220-1337 |
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 1860299437 1220 NTEEQLEIALApYQHLEEDMKSLKQVLEMKNQQIHEQEKKI---------LELEKLAEKNIILEEKIQVLQQQNEDLKAR 1290
Cdd:pfam15254 378 NTNIQAEIALA-LQPLRSENAQLRRQLRILNQQLREQEKTEktsgsgdcnLELFSLQSLNMSLQNQLQESLKSQELLQSK 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 1291 idqntvvtrqlseeNANLQEYVEKETQEKKRLSRT----NEELLWKLQTGD 1337
Cdd:pfam15254 457 --------------NEELLKVIENQKEENKKLTKIfkekEQTLLENKQQFD 493
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1191-1290 |
2.35e-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: 40.82 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1191 SLQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKn 1270
Cdd:pfam04012 54 QLERRLEQQTEQAKKLEEKAQ---AALTKGNEELAREALAEKKSLEKQAEALETQLA-------QQRSAVEQLRKQLAA- 122
|
90 100
....*....|....*....|
gi 1860299437 1271 iiLEEKIQVLQQQNEDLKAR 1290
Cdd:pfam04012 123 --LETKIQQLKAKKNLLKAR 140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1235-1330 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1235 LEEDMKSLKQVLEMKNQQIHEQEKKI----LELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQE 1310
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEkallKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100
....*....|....*....|
gi 1860299437 1311 YVEKETQEKKRLSRTNEELL 1330
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAL 124
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
1249-1326 |
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 1860299437 1249 KNQQIHEQEKKILELEK----LAEKNIILEEKIQVLQQQNEDLKARID----QNTVVT---RQLSEENANL-QEYVEKET 1316
Cdd:cd22887 2 LESELQELEKRLAELEAelasLEEEIKDLEEELKEKNKANEILNDELIalqiENNLLEeklRKLQEENDELvERWMAKKQ 81
|
90
....*....|
gi 1860299437 1317 QEKKRLSRTN 1326
Cdd:cd22887 82 QEADKMNEAN 91
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1192-1290 |
2.96e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1192 LQDQVDTLTFQSQSLRDRARrfeEALRKNTEEQLEIALAPYQHLEEDMKSLKQvlemknqQIHEQEKKILELEKLAEKni 1271
Cdd:COG1842 56 LERQLEELEAEAEKWEEKAR---LALEKGREDLAREALERKAELEAQAEALEA-------QLAQLEEQVEKLKEALRQ-- 123
|
90
....*....|....*....
gi 1860299437 1272 iLEEKIQVLQQQNEDLKAR 1290
Cdd:COG1842 124 -LESKLEELKAKKDTLKAR 141
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
631-995 |
3.02e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 631 PIIMPKPKHVRPKIITYIRRnPQALGQVDASLVPVGLPYAPPTCTMPLPHEEKAAGGDLKPSAnlyekfkpdlQKPRVFS 710
Cdd:PHA03247 2569 PPPRPAPRPSEPAVTSRARR-PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS----------PSPAANE 2637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 711 SGLMVSGIKPPghPFSQMSEKFLQEVTDHPGKEEFCSPPYAhyEVPPTFYRSAMLLKPQLGLGAMSRLPSAKSRILIASQ 790
Cdd:PHA03247 2638 PDPHPPPTVPP--PERPRDDPAPGRVSRPRRARRLGRAAQA--SSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPH 2713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 791 RSSASAIHPPGPiTTATSLYSSDPSADLKKASSSNAAKSNLPKSGLRPPGYSRLPAAKLAAfgfVRSSSVSSVSSTQSGD 870
Cdd:PHA03247 2714 ALVSATPLPPGP-AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA---APAAGPPRRLTRPAVA 2789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 871 SAQPEQGRPATRSTFGNEEQPVL--KASLPSKDTPkgAGRVAPPASSSVTAPrrSLLPAPKSTSTPAGTKKDAQKDQDTN 948
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLapAAALPPAASP--AGPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVAPGGDVRRR 2865
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1860299437 949 KPAVSSPKRVAAST----TKLHSPGYPKQRTAAARNGFPPKPDPQAREAER 995
Cdd:PHA03247 2866 PPSRSPAAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1047-1151 |
3.11e-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: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1047 EKELSIELANIRDEVAfhTAKCEKLQKEKEELERRFEDevkrlgwqQQAELQELEERLQLQFEAEMARLQEEHgDQLLSI 1126
Cdd:cd16269 195 EKEKEIEAERAKAEAA--EQERKLLEEQQRELEQKLED--------QERSYEEHLRQLKEKMEEERENLLKEQ-ERALES 263
|
90 100
....*....|....*....|....*
gi 1860299437 1127 RCQHQEQVEDLTASHDAALLEMENN 1151
Cdd:cd16269 264 KLKEQEALLEEGFKEQAELLQEEIR 288
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1041-1337 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1041 ESALVKEKELSIELANIRDEVAFHTAK-CEKLQKEKEELERRFEDEVKRLGW------QQQAELQEL-----EERLQLQF 1108
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEdHEKIQHLEEEYKKEINDKEKQVSLlliqitEKENKMKDLtflleESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1109 EAEMARLQEEHGDQLLSIRCQHQEQVEDL------TASHDAALLEMENNHTVAITILQDDHDHKVQEL---MSTHE---L 1176
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnkaKAAHSfvvT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1177 EKKELEENFEKL----RLSLQDQVDTLTFQSQSLRDRARRFEE--ALRKNTE---EQLEIALAP----------YQHLEE 1237
Cdd:pfam05483 353 EFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEvelEELKKILAEdeklldekkqFEKIAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1238 DMKSLKQ----VLEMKNQQIHEQEKKIL------------------ELEKLAEKNI---------ILEEKIQVLQQQNED 1286
Cdd:pfam05483 433 ELKGKEQelifLLQAREKEIHDLEIQLTaiktseehylkevedlktELEKEKLKNIeltahcdklLLENKELTQEASDMT 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1860299437 1287 LKARIDQNTVVTRQLSEEN--ANLQEYVEKETQEKKRLSRTNEELlwkLQTGD 1337
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRDELESVREEF---IQKGD 562
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
989-1334 |
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 1860299437 989 QAREAERQLVLRLKERCEQQTRQ--LGVAQGELKRAICGFDALAVATQHF-FRKNESALVKEKELSIELANIRDEVafHT 1065
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERInRARKAAPLAAHIKAVTQIEQQAQRI--HT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1066 akceKLQKEKEELERRFEDEVKRLgwQQQAELQELEERLQLQF--------EAEMARLQEEHGDQLLSIRCQHQEQVEDL 1137
Cdd:TIGR00618 315 ----ELQSKMRSRAKLLMKRAAHV--KQQSSIEEQRRLLQTLHsqeihirdAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1138 TASHD-----AALLEMENN--HTVAiTILQDDHDHKvQELMSTHELEKKeleenfEKLRLSLQDQVDTLTFQSQSLRDRA 1210
Cdd:TIGR00618 389 TTLTQklqslCKELDILQReqATID-TRTSAFRDLQ-GQLAHAKKQQEL------QQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1211 RRfEEALRKNTEEQLEIALAPYQHLEEDMKSL--KQVLEMKNQQ-----------------------------------I 1253
Cdd:TIGR00618 461 LQ-ESAQSLKEREQQLQTKEQIHLQETRKKAVvlARLLELQEEPcplcgscihpnparqdidnpgpltrrmqrgeqtyaQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1254 HEQEKKILELEKLAEKN--IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLW 1331
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
...
gi 1860299437 1332 KLQ 1334
Cdd:TIGR00618 620 KLQ 622
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1038-1342 |
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 1860299437 1038 RKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQE 1117
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1118 EHGD--QLLSIRCQHQEQVEDLTASHD------AALLEMENNHTVAITILqddhDHKVQELMSTHELekkeleenfeklr 1189
Cdd:TIGR00618 319 KMRSraKLLMKRAAHVKQQSSIEEQRRllqtlhSQEIHIRDAHEVATSIR----EISCQQHTLTQHI------------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1190 LSLQDQVDTLTFQSQSL--------RDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKil 1261
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLckeldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI-- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1262 ELEKLAEKniiLEEKIQVLQQQNEDLKAridqntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSP 1341
Cdd:TIGR00618 460 HLQESAQS---LKEREQQLQTKEQIHLQ-------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
.
gi 1860299437 1342 I 1342
Cdd:TIGR00618 530 M 530
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
1261-1313 |
5.05e-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: 5.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1860299437 1261 LELEKLAEKNIILEEKIQVLQQQNEDLKARIdqntvvtRQLSEENANLQEYVE 1313
Cdd:COG3074 25 MEVEELKEKNEELEQENEELQSENEELQSEN-------EQLKTENAEWQERIR 70
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
990-1334 |
5.30e-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: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 990 AREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDAlavATQHFFRKNESALVKEKELsieLANIRDEVAfhtAKCE 1069
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE---ALNKKLNEKESQLADAREV---ISCLKNELS---ELRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1070 KLQKEKEELERrfedevkrlgwqQQAELQELEERLQLQfeaeMARLQEehgdqllsircqHQEQVEDLTASHDAALleme 1149
Cdd:pfam05557 119 QIQRAELELQS------------TNSELEELQERLDLL----KAKASE------------AEQLRQNLEKQQSSLA---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1150 nnhtvaitilqdDHDHKVQELMsthelekkeleenfEKLRLSLQDQVDTLTFQS--------QSLRDRARRFEEALRKNT 1221
Cdd:pfam05557 167 ------------EAEQRIKELE--------------FEIQSQEQDSEIVKNSKSelaripelEKELERLREHNKHLNENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1222 E--EQLEIALAPYQ---HLEEDMKSLKQVLEMKNQQIheqEKKILELEKLAE-------KNIILEEKIQVLQQQNEDLKA 1289
Cdd:pfam05557 221 EnkLLLKEEVEDLKrklEREEKYREEAATLELEKEKL---EQELQSWVKLAQdtglnlrSPEDLSRRIEQLQQREIVLKE 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1860299437 1290 ridQNTVVTRQLSEENANLQE-------YVEKETQEKKRLSRTnEELLWKLQ 1334
Cdd:pfam05557 298 ---ENSSLTSSARQLEKARREleqelaqYLKKIEDLNKKLKRH-KALVRRLQ 345
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1127-1283 |
5.34e-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: 40.77 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1127 RCQHQEQVEDLTASHdaallemennhtvaITILQDDHDH--KVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQ 1204
Cdd:smart00787 138 RMKLLEGLKEGLDEN--------------LEGLKEDYKLlmKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1205 SLRDRARrfeEALRKnTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN--------IILEEK 1276
Cdd:smart00787 204 TELDRAK---EKLKK-LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKEQ 279
|
....*..
gi 1860299437 1277 IQVLQQQ 1283
Cdd:smart00787 280 LKLLQSL 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1048-1319 |
5.52e-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: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1048 KELSIELANIRDEVAFHTakcEKLQKEKEELERRFEDEVKRLGWQQqaELQELEERLQLQFEAEMARLQEEHGDQLLSir 1127
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILT---QCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQDLQDVR-- 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1128 cQHQEQVEDLTASHDAALlemennHTVAITILQDDHDHKvqeLMSTHELEKKELEENFEKLRlSLQDQVDTLTF------ 1201
Cdd:TIGR00618 632 -LHLQQCSQELALKLTAL------HALQLTLTQERVREH---ALSIRVLPKELLASRQLALQ-KMQSEKEQLTYwkemla 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1202 QSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVL-EMKNQQIHEQEKKILELEKLAEKNIILEEKIQVL 1280
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
250 260 270
....*....|....*....|....*....|....*....
gi 1860299437 1281 QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK 1319
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
985-1323 |
5.60e-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: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 985 KPDPQAREAERQL---VLRLKERCEQQTRQLGVAQGELKRA-ICGFDALAVatQHFFRKNESALVKEKELSIELANIRDE 1060
Cdd:TIGR00606 744 KEIPELRNKLQKVnrdIQRLKNDIEEQETLLGTIMPEEESAkVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGSDLD 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1061 VAFhtakcEKLQKEKEELERRFE------DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEhgdqlLSIRCQHQEQV 1134
Cdd:TIGR00606 822 RTV-----QQVNQEKQEKQHELDtvvskiELNRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTN-----LQRRQQFEEQL 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1135 EDLTA---SHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELeenfEKLRLsLQDQVDTLTFQSQSLRDRAR 1211
Cdd:TIGR00606 891 VELSTevqSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ----DKVND-IKEKVKNIHGYMKDIENKIQ 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1212 RFEEALRKNTEEQLEIALAPY-------QHLEEDMKSLKQVLEMKNQQ---------IHEQEKKILELEKLAEKNIILEE 1275
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQerwlqdnltLRKRENELKEVEEELKQHLKEMG 1045
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1860299437 1276 KIQVLQQQNEDLKARIDQNTvVTRQLSEENANLQEYVEKETQEKKRLS 1323
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENIDL-IKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1233-1321 |
6.60e-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: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1233 QHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKN----IILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1308
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAeeeaERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEA 88
|
90
....*....|...
gi 1860299437 1309 QEYVEKETQEKKR 1321
Cdd:pfam20492 89 QEEIARLEEEVER 101
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1060-1116 |
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 1860299437 1060 EVAFHtAKCEKLQKEKEELERRFEDEVK------RLGWQQQAELQELEERLQLQFEAEMARLQ 1116
Cdd:pfam15070 84 EQRLQ-EEAEQLQKELEALAGQLQAQVQdneqlsRLNQEQEQRLLELERAAERWGEQAEDRKQ 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1206-1329 |
7.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1206 LRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQ---- 1281
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllq 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1860299437 1282 -----QQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1329
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1034-1317 |
7.00e-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: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1034 QHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRL-------------GWQQ-QAELQE 1099
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrdelngelsaadaAVAKdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1100 LEERLqLQFEAEMARLQEEHGDQLLSIRCQHQEQVE----------DLTASHDA--ALLEMENNHTVAitilqdDHDHKV 1167
Cdd:pfam12128 327 LEDQH-GAFLDADIETAAADQEQLPSWQSELENLEErlkaltgkhqDVTAKYNRrrSKIKEQNNRDIA------GIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1168 QELMSTHELEKKELEENFEKLRLSLQDQVDTltfQSQSLRDRARRFEEALrknteEQLEIALAPYQHLEEDMKSLKQVLE 1247
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEA---GKLEFNEEEYRLKSRL-----GELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860299437 1248 MKNQQIHEQEKKILELEKLAEKNIILE-------EKIQVLQQQNEDLKARIDQntvVTRQLSEENANLQEYVEKETQ 1317
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHFLRKEAP 545
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
1069-1119 |
7.65e-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: 7.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1860299437 1069 EKLQKEKEELERRFEDEVKRLG---WQQQAELQELEERLQLqfeAEMARLQEEH 1119
Cdd:pfam04696 44 EKAKQEKEELEERKREEREELFeerRAEQIELRALEEKLEL---KELMETWHEN 94
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
985-1329 |
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 1860299437 985 KPDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELS-IELANIRDEVAF 1063
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSlKEKELAEEREKT 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1064 HTAKCEKLQK------EKEELERRFEDEVkrlgwqqQAELQELEERLQLQFEAEmarLQEEhgdqllsircQHQEQVEDL 1137
Cdd:pfam02463 784 EKLKVEEEKEeklkaqEEELRALEEELKE-------EAELLEEEQLLIEQEEKI---KEEE----------LEELALELK 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1138 TASHDAALLEMENNHTVAITILQDDHDHKVQELmsthelekkeLEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEAL 1217
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKE----------EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1218 RKNTEEQLEIAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVV 1297
Cdd:pfam02463 914 EKENEIEERIK----EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
330 340 350
....*....|....*....|....*....|..
gi 1860299437 1298 TRQLSEENANLQEyvEKETQEKKRLSRTNEEL 1329
Cdd:pfam02463 990 YNKDELEKERLEE--EKKKLIRAIIEETCQRL 1019
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1000-1117 |
8.35e-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: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1000 RLKERCEQQTRQLGvaqgELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDevafhtaKCEKLQKEKEELE 1079
Cdd:pfam13851 58 RLTEPLQKAQEEVE----ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQ-------RFEKVERERDELY 126
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1860299437 1080 RRFEDEVKRLgwQQQAELQE--LEERLQL---QFEAEMARLQE 1117
Cdd:pfam13851 127 DKFEAAIQDV--QQKTGLKNllLEKKLQAlgeTLEKKEAQLNE 167
|
|
| FAM76 |
pfam16046 |
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ... |
1235-1308 |
9.14e-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: 9.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860299437 1235 LEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDlkaRIDQNTVVTRQLSEENANL 1308
Cdd:pfam16046 227 LKEQIASLQKQLAQKDQQLLEKDKQITELKaKHFTKERELRNKMKTMEKEHED---KVEQLQIKIRSLLKEVATL 298
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1091-1293 |
9.28e-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: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1091 WQQ-QAELQELEERLQlqfEAEMARLQEEHGDqllsircqHQEQVEDLTASHDAALLEMENNHTVAitilqDDHDHKVQE 1169
Cdd:cd00176 2 LQQfLRDADELEAWLS---EKEELLSSTDYGD--------DLESVEALLKKHEALEAELAAHEERV-----EALNELGEQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860299437 1170 LMSTHELEKKELEENFEKLRL---SLQDQVDTLTFQSQSLRDRARRFEEA--LRKNTEEQLEIALA-PYQHLEEDMKSLK 1243
Cdd:cd00176 66 LIEEGHPDAEEIQERLEELNQrweELRELAEERRQRLEEALDLQQFFRDAddLEQWLEEKEAALASeDLGKDLESVEELL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860299437 1244 QVLEMKNQQIHEQEKKILELEKLAEK---------NIILEEKIQVLQQQNEDLKARIDQ 1293
Cdd:cd00176 146 KKHKELEEELEAHEPRLKSLNELAEElleeghpdaDEEIEEKLEELNERWEELLELAEE 204
|
|
| |
