|
Name |
Accession |
Description |
Interval |
E-value |
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
83-801 |
0e+00 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 1042.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR 162
Cdd:pfam09730 1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730 81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 243 ALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDD---AAEPNNDAEALvNGFEHG--GLAKLPLDNKT 317
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDegaGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 318 STPKKEGLAPPSPSLVSDLLSELNLSEIQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL 397
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 398 RRLQAGKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKVLRSTHEAREAQHAEEKGRYEAE 477
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 478 GQALMEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 557
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 558 REGQGGAGRtspggRTSPEGRGRRSPILLPKGLLAPEAGRAdGGSGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQ 637
Cdd:pfam09730 480 REGAGARAR-----KSHQEPRGLRSPRLLTRGLFMGEVGTA-DTTSNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 638 IKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYEN 717
Cdd:pfam09730 554 IKHLQVAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYEN 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 718 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 797
Cdd:pfam09730 634 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLE 713
|
....
gi 383872874 798 LLEL 801
Cdd:pfam09730 714 DLEF 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-535 |
1.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRGEMEQLKEAfg 83
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAE-LEELEAELAELEAELeELRLELEELELELEEAQAEEYELLAE-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 84 qahtnhkkvaadgESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNVEIQ 159
Cdd:COG1196 297 -------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 160 RGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQ 239
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 240 LEEALETLKTEREQKNSLRKELShymsiNDSFYTSHLHVSLDGLKFSDDAAEPN----NDAEALVNGFEHGGLAKLPLDN 315
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLA-----ELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 316 KTSTPKKEGLAPPSPSLVSD--------LLSELNLSEIQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKV 387
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 388 TRLTENLSALRRLQAGKERQ--TALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGEL-REQLKVLRSTHEARE 464
Cdd:COG1196 599 AAVDLVASDLREADARYYVLgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLtGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872874 465 AQHAEEKGRYEAEGQALMEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELA 535
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-264 |
5.47e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRGEMEQLK----- 79
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEE-LEELTAELQELEEKLeELRLEVSELEEEIEELQKELYALAneisr 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 80 -EAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEI 158
Cdd:TIGR02168 300 lEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 159 QRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQ--VEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEIS 236
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260
....*....|....*....|....*...
gi 383872874 237 ERQLEEALETLKTEREQKNSLRKELSHY 264
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-262 |
1.05e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGEsREE 101
Cdd:TIGR02168 676 RREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 182 SELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:TIGR02168 834 AATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
.
gi 383872874 262 S 262
Cdd:TIGR02168 911 S 911
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-261 |
5.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 38 REKIQAAEYgLAVLEEKHQLK-----LQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREESLIQESAskeq 112
Cdd:COG1196 207 RQAEKAERY-RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 113 yyvrKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQ 192
Cdd:COG1196 282 ----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383872874 193 KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-264 |
7.40e-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: 56.23 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 5 SEEEEYARLVMEAQPEWLRAEVKRLSHELaETTREKIQAAEYGLAVLE-EKHQLKLQFEELEVDYEAIRGEMEQLKeafg 83
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEK-EALERQKEAIERQLASLEeELEKLTEEISELEKRLEEIEQLLEELN---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 84 qahtnhKKVAADGESREESL---IQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEinqNVEIQR 160
Cdd:TIGR02169 279 ------KKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER---EIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEI--------------KRLEEETEYLNSQL 226
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrlqeelQRLSEELADLNAAI 429
|
250 260 270
....*....|....*....|....*....|....*...
gi 383872874 227 EDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHY 264
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
52-813 |
6.58e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 52 EEKHQLKLQFEELEV-----DYEAIRGEMEQLKEAFGQAHTNHKkvaadgesREESLIQESASKEQYYVRKVLELQTELK 126
Cdd:TIGR02168 213 ERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELE--------ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 127 QLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKqvsvlrqnqvEFE 206
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----------ELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 207 GLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTEREQKNSLRKELShymsindsfytshlhvSLDGLKFS 286
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEEL-------EEQLETLRSKVAQLELQIASLNNEIE----------------RLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 287 DDAAEPNNDAEalvngfehgglaklpldnktstpkkeglappspslVSDLLSELNLSEIQKLKQQLMQMEREKAGLLVTL 366
Cdd:TIGR02168 412 LEDRRERLQQE-----------------------------------IEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 367 QDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQAGKERQ------------TALDNEKDRDSHED--GDYYEVDingp 432
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlegfsegvkALLKNQSGLSGILGvlSELISVD---- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 433 eilaCKYHVAVAEAGELREQLKVLRSTHEAREAQhaeekgryEAEGQALMEKVSLLEKASRQDRELLARLEKELKKVSDV 512
Cdd:TIGR02168 533 ----EGYEAAIEAALGGRLQAVVVENLNAAKKAI--------AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 513 AGetqgslsvAQDELVTFSEE----LANLYHHVCMCNNETPNRVMLDYYREGQG---------GAGRTSPGGRTSPEGR- 578
Cdd:TIGR02168 601 LG--------VAKDLVKFDPKlrkaLSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvRPGGVITGGSAKTNSSi 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 579 -GRRSPI---------LLPKGLLAPEAGRADGGSGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRT 648
Cdd:TIGR02168 673 lERRREIeeleekieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 649 -----------TELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSkYEN 717
Cdd:TIGR02168 753 skelteleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-LER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 718 EKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDE-------MQRQLAAAEDEKKTLNSLLRMAIQQKL 790
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELESKRS 911
|
810 820
....*....|....*....|...
gi 383872874 791 ALTQRLELLELDHEQTRRGRTKA 813
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGL 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6-200 |
1.54e-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: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTReKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRGEM-EQLKEAFG 83
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAElAELEKEIAELRAELEAQKEELaELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 84 QAHTNHKKVAADGESreeslIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRL 163
Cdd:COG4942 116 LGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 383872874 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQ 200
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-261 |
1.69e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 16 EAQPEWLRAEVKRLSHELAETTR---EKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRGEMEQLkeaFGQAHTNHKKV 92
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKfknNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQEL---IFLLQAREKEI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 93 aadgeSREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKF 172
Cdd:pfam05483 453 -----HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 173 REARLLQDYSELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
....*....
gi 383872874 253 QKNSLRKEL 261
Cdd:pfam05483 605 NKNKNIEEL 613
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
20-299 |
4.77e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.29 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 20 EWLRAEVKRLSHELAET-TREKIQAAEYGLAVLEEKHQLKLQfEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PLN02939 166 EALQGKINILEMRLSETdARIKLAAQEKIHVEILEEQLEKLR-NELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 99 REESLIQESASKEQYYVrkvLE-----LQTELKQLRNVLTNTQSENERLASVAQE-LKEINQNVEIQRGRLRDDIKEYkf 172
Cdd:PLN02939 245 LKAELIEVAETEERVFK---LEkerslLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 173 reARLLQDYSELEEENISLQ---KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKT 249
Cdd:PLN02939 320 --ALVLDQNQDLRDKVDKLEaslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 383872874 250 EREqknslRKELSHYMSINDSFYTSHLHVSLDGlkFSDDAAEPNNDAEAL 299
Cdd:PLN02939 398 ESK-----KRSLEHPADDMPSEFWSRILLLIDG--WLLEKKISNNDAKLL 440
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-250 |
5.31e-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: 50.45 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 102 SLiqeSASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02169 787 RL---SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383872874 182 SELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNS---QLEDAIRLKEISERQLEEALETLKTE 250
Cdd:TIGR02169 864 EELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-247 |
6.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 6 EEEEYARLVMEAQPEWLRAEVKRLS-HELAETTREKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRGEMEQLKEAFG 83
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTlLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 84 QAHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLTNTQSE----NERLASVAQELKEINQNV--- 156
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIE--------ELESELEALLNERASLEEAlallRSELEELSEELRELESKRsel 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 157 EIQRGRLRDDIKEYKFREARLLQDYSEL-----EEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI- 230
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIe 993
|
250 260
....*....|....*....|....*.
gi 383872874 231 RLKEISERQ---------LEEALETL 247
Cdd:TIGR02168 994 EYEELKERYdfltaqkedLTEAKETL 1019
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
20-229 |
1.88e-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: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 20 EWLRAEVKRLSHELAETtREKIQA--AEYGLAVLEEKHQLKL-QFEELEVDYEAIRGEMEQLKEAFGQAhtnhKKVAADG 96
Cdd:COG3206 178 EFLEEQLPELRKELEEA-EAALEEfrQKNGLVDLSEEAKLLLqQLSELESQLAEARAELAEAEARLAAL----RAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 97 ESREESLIQESAskEQYYVRKVLELQTELKQLRNVLTntqSENERLASVAQELKEINQNVEIQRGRLRDDIK-EYKFREA 175
Cdd:COG3206 253 PDALPELLQSPV--IQQLRAQLAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 383872874 176 RLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDA 229
Cdd:COG3206 328 RE----ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-537 |
3.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDdiKEYKFREAR 176
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-LKEISERQLEEALETLKTEREQKN 255
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 256 SLRKELSHYMSINDSfytshLHVSLDGLKFSDDAAEPNND-AEALVNGFEHGGLAKLPLDNKTSTPKKEGLAP------- 327
Cdd:COG4717 210 ELEEELEEAQEELEE-----LEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 328 -----------PSPSLVSDLLSELNLSEIQKLKQQLMQMEREKAGLLVTLQDTqkQLEHTRGSLSEQQEKVTRLTENLSA 396
Cdd:COG4717 285 llallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 397 LRRLQAGKERQTALDNEKDRDsheDGDYYEVDINGPEilackYHVAVAEAGELREQLKVLRSTHEAREAQHAEEkgRYEA 476
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVED---EEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEE--ELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383872874 477 EGQALMEKVSLLEKASRQDRELLARLEKELKKVsdvagETQGSLSVAQDELVTFSEELANL 537
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELREL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-253 |
4.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 116 RKVLELQTELKQLRNVLTNTQSENERLASVAQELKeinqnveiQRGRLRDDIKEYKFREarllQDYSELEEENISLQKQV 195
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQ--------ERREALQRLAEYSWDE----IDVASAEREIAELEAEL 677
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 383872874 196 SVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 253
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-271 |
5.53e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 6 EEEEYARLVMEAQPEwLRAEVKRLSHELAETtREKIQAAEyglAVLEEKHQLKLQFEELEVDYEAIRGEMEQLKEAFGQa 85
Cdd:TIGR02169 781 LNDLEARLSHSRIPE-IQAELSKLEEEVSRI-EARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 86 htnhkkvaadgesREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRD 165
Cdd:TIGR02169 855 -------------EIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 166 DIKEYKFREARLLQDYSELEEENISLQKQVSvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISER---QLEE 242
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrldELKE 993
|
250 260 270
....*....|....*....|....*....|....*...
gi 383872874 243 ALETLKTER-------EQKNSLRKE--LSHYMSINDSF 271
Cdd:TIGR02169 994 KRAKLEEERkaileriEEYEKKKREvfMEAFEAINENF 1031
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
100-264 |
6.05e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 100 EESLIQESASKEQYYVRKVLELQTELKQLRnvltntqsenerlaSVAQELKEINQNVEIQRGRLRDDIKEYKfreaRLLQ 179
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPELNKLHEVESKLK--------------ETSEEYEDLLKKSTILVREGNKANSELK----NFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 180 DYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQ--LEDAIRLKEISERQLEEALETLKTEREqkNSL 257
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRE--NSL 1077
|
....*..
gi 383872874 258 RKELSHY 264
Cdd:COG5022 1078 LDDKQLY 1084
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-205 |
2.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 22 LRAEVKRLS-----HELAETTREKIQAAEYGLAVL------EEKHQLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTN-- 88
Cdd:COG4913 247 AREQIELLEpirelAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREEld 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 89 --HKKVAADGESREESLIQESASKEQYY---VRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEinqNVEIQRGRL 163
Cdd:COG4913 327 elEAQIRGNGGDRLEQLEREIERLERELeerERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE---ALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 383872874 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEF 205
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-537 |
2.51e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 343 SEIQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQAGKERQTALDNEKDRDSHEDG 422
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 423 dyyevdingpEILACKYHVAVAEAGELREQLKVLRSTHEAREAQHAEEKGRYEAEGQALMEKVSLLEKASRQDRELLARL 502
Cdd:COG1196 347 ----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190
....*....|....*....|....*....|....*
gi 383872874 503 EKELKKVSDVAGETQGSLSVAQDELVTFSEELANL 537
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
113-265 |
2.65e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 113 YYVRKVLeLQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGR------LRDDIKEYKFREARLLQDYSELEE 186
Cdd:PRK12704 22 YFVRKKI-AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefekeLRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383872874 187 ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDaiRLKEISERQLEEALETLKTEREQKnsLRKELSHYM 265
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ--ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-261 |
3.63e-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: 43.60 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 62 EELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREESLIQESaskeqyyvRKVLELQTELKQLRNVLTNTQSENER 141
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--------RRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 142 LASVAQELKE--INQNVEIQRGRLRDDIK--------EYKFREARLLQDYSELEEENI-SLQKQVSVLRQNQVEFEGLKH 210
Cdd:COG4942 95 LRAELEAQKEelAELLRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 383872874 211 EIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-512 |
5.72e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 118 VLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVsv 197
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 198 lRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELShymsindsfytshlh 277
Cdd:TIGR02168 750 -AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------------- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 278 vsldglKFSDDAAEPNNDAEALVNgfehgglaklpldnktstpkkeglappspslvsdllselnlsEIQKLKQQLMQMER 357
Cdd:TIGR02168 814 ------LLNEEAANLRERLESLER------------------------------------------RIAATERRLEDLEE 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 358 EKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLTENLSAL-RRLQAGKERQTALDNEKDRDSHEDGDyyevdingpeila 436
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeEALALLRSELEELSEELRELESKRSE------------- 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 437 ckyhvAVAEAGELREQLKVLRSTHEAREAQHAEEKGR----YEAEGQALMEKVSLLEKASRQDRELLARLEKELKKVSDV 512
Cdd:TIGR02168 913 -----LRRELEELREKLAQLELRLEGLEVRIDNLQERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-534 |
5.87e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRGEMEQLKEAfGQA 85
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 86 HTNH----KKVAADGESREESLIQESASKEQYYVR-KVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQR 160
Cdd:TIGR02168 398 LNNEierlEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 161 GRLRDDIKEYKFREARLlqdySELEEENISLQKQVSVLRQNQVEFEGLKH---EIKRLEEETE-------------YLNS 224
Cdd:TIGR02168 478 DAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGYEaaieaalggrlqaVVVE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 225 QLEDAIR-----------------LKEISERQLEEALETLKTEREQKNSLRKELSHYmsinDSFYTSHLHVSLDGLKFSD 287
Cdd:TIGR02168 554 NLNAAKKaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF----DPKLRKALSYLLGGVLVVD 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 288 DAAEPNNDAEALvngfeHGGLAKLPLDNKTSTPKkeGLAPPSPSLVSDLLSELNlSEIQKLKQQLMQMEREKAGLLVTLQ 367
Cdd:TIGR02168 630 DLDNALELAKKL-----RPGYRIVTLDGDLVRPG--GVITGGSAKTNSSILERR-REIEELEEKIEELEEKIAELEKALA 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 368 DTQKQLE----HTRGSLSEQQEKVTRLTENLSALRRLQAGKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAV 443
Cdd:TIGR02168 702 ELRKELEeleeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 444 AEAGELREQLKVLRSTHEAREAQHAEEKGRYEAEGQALMEKVSLLEKASRQDRELLARLEkELKKVSDVAGETQGSLSVA 523
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAE 860
|
570
....*....|.
gi 383872874 524 QDELVTFSEEL 534
Cdd:TIGR02168 861 IEELEELIEEL 871
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-508 |
6.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 60 QFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAAdGESREESLIQESASKEQyyVRKVLELQTELKQLRNVLtntQSEN 139
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEK--LLQLLPLYQELEALEAEL---AELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 140 ERLASVAQELKEInQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEEnislqkqvsvlrqnqvEFEGLKHEIKRLEEET 219
Cdd:COG4717 146 ERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEE----------------ELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 220 EYLNSQLEDAIRLKEISERQLEEaLETLKTEREQKNSLRKELSHYMSI---------NDSFYTSHLHV-----------S 279
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEARLLLLIAaallallglGGSLLSLILTIagvlflvlgllA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 280 LDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDnktSTPKKEGLAPP-SPSLVSDLLSElnLSEIQKLKQQLMQMERE 358
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELE---ELLAALGLPPDlSPEELLELLDR--IEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 359 KAglLVTLQDTQKQLEHTRGSLSEQQekvtrLTENLSALRRLQAGKERQTALdnEKDRDSHEDGDYYEVDINGPEILACK 438
Cdd:COG4717 363 LQ--LEELEQEIAALLAEAGVEDEEE-----LRAALEQAEEYQELKEELEEL--EEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383872874 439 YHVAVAEAGELREQLKVLRSTHEAREAQ--HAEEKGRYEAEGQALMEKVSLLEKASRQD------RELLARLEKELKK 508
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEEWaalklaLELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-253 |
7.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 22 LRAEVKRLS--HELAETTREKIQAaeygLAVLEEKHQlklQFEELEVDYEAIRGEMEQLKEAFGQahtnhkKVAADGESR 99
Cdd:COG4913 230 LVEHFDDLEraHEALEDAREQIEL----LEPIRELAE---RYAAARERLAELEYLRAALRLWFAQ------RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 100 EESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTqsENERLASVAQELKEINQnveiQRGRLRDDIKEYKFREARLLQ 179
Cdd:COG4913 297 LEELRAELARLEA----ELERLEARLDALREELDEL--EAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383872874 180 DYSELEEEnislqkqvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQ 253
Cdd:COG4913 367 LLAALGLP----------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
98-261 |
7.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 98 SREESLIQESASKEQYYVRKVLELQTELKQLrnvLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARL 177
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 178 LQdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSL 257
Cdd:TIGR02169 775 HK--LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
....
gi 383872874 258 RKEL 261
Cdd:TIGR02169 853 EKEI 856
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-513 |
9.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 173 REARLLQDYSELEEENISLQKQVSVLRqnqvefeglkheIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 253 QKNSLRKELshymsindsfytshlhvsldglkfsDDAAEPNNDAEALVNGFEHgglaklpldNKTSTPKKEGLAPPSPSL 332
Cdd:TIGR02168 275 EVSELEEEI-------------------------EELQKELYALANEISRLEQ---------QKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 333 VSDLLsELNLSEIQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQAGKERQTALDN 412
Cdd:TIGR02168 321 LEAQL-EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 413 E---------KDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKVLRSTHEAREAQHAEEKGRYEAEGQALME 483
Cdd:TIGR02168 400 NeierlearlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350
....*....|....*....|....*....|
gi 383872874 484 KVSLLEKASRQDRELLARLEKELKKVSDVA 513
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-254 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRGEMEQLKEAFGQAhtnhkkvaadgESREE 101
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----------EKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEykfrearLLQDY 181
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383872874 182 SELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQK 254
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
60-263 |
1.15e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 60 QFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQyyvrKVLELQTELKQLRNVLTNTQSEN 139
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN----ELSELRRQIQRAELELQSTNSEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 140 ERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlqdySELEEEnISLQKQ----VSVLRQNQVEFEGLKHEIKRL 215
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI----KELEFE-IQSQEQdseiVKNSKSELARIPELEKELERL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 383872874 216 EEETEYLNSQLEDAIRLKEISErQLEEALETLKTEREQKNSLRKELSH 263
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEK 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-260 |
1.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 23 RAEVKRLSHELAETTREKIQAAEYGLAVLEEK--HQLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESRE 100
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 101 ESLIQESASKEQYyVRKVLELQT--ELK---QLRNVLTNTQSENERLASV--AQELKEINQNVEIQRGRLRDDIKEYKFR 173
Cdd:PTZ00121 1532 EAKKADEAKKAEE-KKKADELKKaeELKkaeEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 174 EARLLQDYSELEEE---NISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEdaiRLKEISERQLEEALETLKTE 250
Cdd:PTZ00121 1611 EAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEEDE 1687
|
250
....*....|
gi 383872874 251 REQKNSLRKE 260
Cdd:PTZ00121 1688 KKAAEALKKE 1697
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
343-508 |
1.57e-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: 41.06 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 343 SEIQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR-RLQAGKERQTALDNEKDRDSHED 421
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYEEQLGNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 422 gdyyEVDINGPEILACKYHV--AVAEAGELREQLKVLRSTHEAREAQHAEEKGRYEAEGQALMEKVSLLEKASrqdRELL 499
Cdd:COG1579 97 ----EIESLKRRISDLEDEIleLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER---EELA 169
|
....*....
gi 383872874 500 ARLEKELKK 508
Cdd:COG1579 170 AKIPPELLA 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-511 |
2.46e-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: 41.29 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 334 SDLLSELNLSE--IQKLKQQLMQMEREKAGLLVTLQDTQKQLEHTRGSLSEQQEKVTRLtenLSALRRLQAGKERQTALD 411
Cdd:COG4942 51 KALLKQLAALErrIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 412 NEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKVLRSTHEAREAQHAEEKGRYEAEGQALMEKVSLLEKA 491
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180
....*....|....*....|
gi 383872874 492 SRQDRELLARLEKELKKVSD 511
Cdd:COG4942 208 LAELAAELAELQQEAEELEA 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-261 |
2.46e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 120 ELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLR 199
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383872874 200 QnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:TIGR04523 433 E---TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-262 |
2.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 22 LRAEVKRLSHELAETTREKIQAAEY---GLAVLEEKHQLKLQFEELEVDYEAIR---GEMEQLKEAFGQAHTNHKKVAAD 95
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLRetiAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 96 GESREESLIQE----SASKEQYYVRKVlELQTELKQLRnvltntqsenERLASVAQELKEINQNVEiqrgRLRDDIKEYK 171
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEARRE-ELEDRDEELR----------DRLEECRVAAQAHNEEAE----SLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 172 FREARLLQDYSELEEEnisLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTER 251
Cdd:PRK02224 356 ERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELR 425
|
250
....*....|.
gi 383872874 252 EQKNSLRKELS 262
Cdd:PRK02224 426 EREAELEATLR 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-261 |
2.64e-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: 40.29 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 116 RKVLELQTELKQLRNVLTNTQsenERLASVAQELKEINQNVEIQRGRLRDDikEYKFREARLLQDYSELEEENISLQKQV 195
Cdd:COG1579 31 AELAELEDELAALEARLEAAK---TELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383872874 196 SVLRQNQVEFEglkHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKEL 261
Cdd:COG1579 106 SDLEDEILELM---ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
49-262 |
3.07e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 49 AVLEEKHQLKL-QFEELEVDYEAIRGE------------MEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYV 115
Cdd:PRK05771 20 EVLEALHELGVvHIEDLKEELSNERLRklrslltklseaLDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 116 RKVLELQTELKQLRNVLTNTQSENERL---ASVAQELKEINQ--NVEIQRGRlrddIKEYKFREARLLQDYSELEEENIS 190
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGfkYVSVFVGT----VPEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 191 LQKQVSVL-------------------RQNQVEFEG-LKHEIKRLEEETEYLNSQLEDAI-RLKEISERQLEEAL---ET 246
Cdd:PRK05771 176 KGYVYVVVvvlkelsdeveeelkklgfERLELEEEGtPSELIREIKEELEEIEKERESLLeELKELAKKYLEELLalyEY 255
|
250
....*....|....*.
gi 383872874 247 LKTEREQKNSLRKELS 262
Cdd:PRK05771 256 LEIELERAEALSKFLK 271
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
66-262 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 66 VDYEAIRGEMEQLKEAFGQAHTNHKKVAA------DGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSEN 139
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 140 ErlASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIK-RLEEE 218
Cdd:pfam12128 314 D--AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRD 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 383872874 219 TEYLNSQLEdaiRLKEISERQLEEA---LETLKTE-REQKNSLRKELS 262
Cdd:pfam12128 392 IAGIKDKLA---KIREARDRQLAVAeddLQALESElREQLEAGKLEFN 436
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5-258 |
4.79e-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: 40.59 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 5 SEEEEYARLVMEAQPEWLR---AEVKRLSHELAETTREKIQAAEYGLAVLEekHQLKLQFEELEVDYEAIRgemEQLKEA 81
Cdd:pfam12128 638 SREETFARTALKNARLDLRrlfDEKQSEKDKKNKALAERKDSANERLNSLE--AQLKQLDKKHQAWLEEQK---EQKREA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 82 FGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKqlrNVLTNTQSENERLASVAQELKEINQNVEIQRG 161
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIAKLKREIRTLERKIERIAV 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 162 RlRDDIKEY-KFREARLLQdyseleeENISLQKQVSVLRQNQVEfegLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:pfam12128 790 R-RQEVLRYfDWYQETWLQ-------RRPRLATQLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
250
....*....|....*...
gi 383872874 241 EEALETLKTEREQKNSLR 258
Cdd:pfam12128 859 SENLRGLRCEMSKLATLK 876
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
17-247 |
5.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 17 AQPEWLRAEVKRLSHELAETtREKIQAAEYGLAVLEEkhqLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHkkvaadg 96
Cdd:COG4913 654 AEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKEL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREAR 176
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA 802
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383872874 177 LLQDYSELEEENISLQKQVSVLRQN-----QVEFEGLKHEikRLEEETEYLNSQLEDAIRlkEISER--QLEEALETL 247
Cdd:COG4913 803 ETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNE--NSIEFVADLLSKLRRAIR--EIKERidPLNDSLKRI 876
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-269 |
7.77e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 24 AEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREESL 103
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 104 IQESASKeqyyvrkvlelQTELKQLRNVLTNTQSENERLASVAQELKeinQNVEIQRGRLRDDIKEYKFREARLLQDYSE 183
Cdd:pfam15921 698 KMQLKSA-----------QSELEQTRNTLKSMEGSDGHAMKVAMGMQ---KQITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 184 ---LEEENISLQKQVSVL--RQNQV--EFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLktEREQKNS 256
Cdd:pfam15921 764 khfLKEEKNKLSQELSTVatEKNKMagELEVLRSQERRLKEKVANMEVALDKA-------SLQFAECQDII--QRQEQES 834
|
250
....*....|...
gi 383872874 257 LRKELSHYMSIND 269
Cdd:pfam15921 835 VRLKLQHTLDVKE 847
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-260 |
7.99e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 54 KHQLKLQFEELEVDYEAIRGEMEQLKEAFGQAHTNHKKVAADGESREESL------IQESASKEQYYVRKVLELQTELKQ 127
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkISSLKEKIEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872874 128 LRNVLTNTQSENERlASVAQELKEINQNVEiqrgRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSvlrQNQVEFEG 207
Cdd:TIGR04523 543 LEDELNKDDFELKK-ENLEKEIDEKNKEIE----ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE---EKEKKISS 614
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 383872874 208 LKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKE 260
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| |
